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Conserved domains on  [gi|568973811|ref|XP_006533316|]
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protein sidekick-2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1276-1526 9.55e-17

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.21  E-value: 9.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1276 YEVQVLAFTRIGDGSPShPPILERTLDDVPGPPMGILFPEVRTTSVRLIWQPPAAPNgiILAYQItHRlnATTANTATVE 1355
Cdd:COG3401   205 YYYRVAATDTGGESAPS-NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRV-YR--SNSGDGPFTK 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1356 VLAPSARQYMATGLKPESVYLFRITAQTRKG-WGEAAEALVVTTEkrdrPQPPSKPV-VQQEDVKARSVLLSWEPGSDgl 1433
Cdd:COG3401   279 VATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTD----LTPPAAPSgLTATAVGSSSITLSWTASSD-- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1434 SPVRYYTIQTRELPSGRWALHSASVshNASAFTVDRLKPFTSYKFRVKATNDIGDSEFSEESESLTTLQAAPDEAPTILS 1513
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTKIAETV--TTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASV 430

                         250
                  ....*....|...
gi 568973811 1514 VTPHTTTSVLIRW 1526
Cdd:COG3401   431 DAVPLTDVAGATA 443
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 408-496 9.59e-17

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


The actual alignment was detected with superfamily member cd20952:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 87  Bit Score: 77.15  E-value: 9.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  408 ITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILAsgsVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568973811  488 DEASADLVV 496
Cdd:cd20952    79 ATWSAVLDV 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1611-1704 8.55e-16

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1611 APQNVAIHSATATQLDVTWEPPPLDNqnGDIQGYKIYFWEVQRRNlTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDG--GPITGYVVEYREKGSGD-WKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 568973811 1691 AGDGPRSTPTRGQT 1704
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1679-1910 1.95e-15

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 82.36  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1679 TAYMVSVAAFNAAGDGPRSTPTRGQTQQAAPSAPGSVKFSELTTTSVNVSWDAPqfPNGPLEGYRlVYEPCTPVDGVSKI 1758
Cdd:COG3401   203 TTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV--TESDATGYR-VYRSNSGDGPFTKV 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1759 VTvdVKGNSplwLKVKDLAEGMTYRFRIKAKTFTYGPEIEANI--TTGPGEGAPGPPGVPIIVRYSSAIAIHWSSGDPgk 1836
Cdd:COG3401   280 AT--VTTTS---YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD-- 352

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811 1837 GPITRYVIEARPSDEGLWDIlikdIPKEVTSYTFSMDILKPGVSYDFRVIAVNDYgfGTPSSPSQSVPAQKASP 1910
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTK----IAETVTTTSYTDTGLTPGTTYYYKVTAVDAA--GNESAPSEEVSATTASA 420
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1103-1198 4.57e-15

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1103 APANVTLRTASETSLWLRWMPLPEmeynGNPESVGYKIKYgRSDGHGKTLSHTVQDRVEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPED----DGGPITGYVVEY-REKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 568973811 1183 NAIGSGPWSQAVVGRT 1198
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 312-401 6.02e-14

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


The actual alignment was detected with superfamily member cd20978:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 88  Bit Score: 68.96  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEvGKLTRFkQRSDGGLQISGLLPDDTGMLQCFAHNAAG 391
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERA-TVEDGTLTIINVQPEDTGYYGCVATNEIG 78

                          90
                  ....*....|
gi 568973811  392 EAQTSTYLAV 401
Cdd:cd20978    79 DIYTETLLHV 88
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
737-1220 1.91e-13

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  737 AGLPVGYQFKNITDADVNNLLLEDLIIWTNYEIEVAAYNSAGLGVYSSKVTEWTLQGVPTVPPGNVHAEATNSTTIRFTW 816
Cdd:COG3401    63 SGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  817 NAPSPQFINGINQGYKLIAWEPAQEEEVTMVTARPNFQDSIHVGFVS--------GLKKFTEYFTSVLCFTTPGDGPRSS 888
Cdd:COG3401   143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSttlvdgggDIEPGTTYYYRVAATDTGGESAPSN 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  889 PQLVRTHEDVPGPVGHLSFNDILDTSLKVSWQEPGEKNgiLTGYRI--------SWEEYNRTNTrvthylpnvtLEYRVT 960
Cdd:COG3401   223 EVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVyrsnsgdgPFTKVATVTT----------TSYTDT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  961 GLTALTTYTIEVAAMTSKGQGQVSASTISSGVPPELPGAPTNLGISNIGPRSVTLQFRPGYDGKtsISRWVVEAQVGVIG 1040
Cdd:COG3401   291 GLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGG 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1041 egeEWLLIYQLGNEPdarSMEVPDLNPFTYYSFRMRQVNIVGTSPPSQPSRKIQTLQAPPDIAPANVTLRTASETSLWLR 1120
Cdd:COG3401   369 ---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGAT 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1121 WMPLPEmeynGNPESVGYKIKYGRSDGHGKTlshTVQDRVEREYTIEDLEEWTEYRVQVQAFNAIGSGPWSQAVVGRTRE 1200
Cdd:COG3401   443 AAASAA----SNPGVSAAVLADGGDTGNAVP---FTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515

                         490       500
                  ....*....|....*....|
gi 568973811 1201 SVPSSGPTNVSALATTSSSM 1220
Cdd:COG3401   516 AAAAVGGAPDGTPNVTGASP 535
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 594-685 5.35e-13

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 66.75  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  594 PHAPEHPvaTLSTVERRAINLTWAKPFDGNSPLMRYVLEMSENNAPWTILLASVDPEATSVMVKGLVPARSYQFRLCAVN 673
Cdd:cd00063     1 PSPPTNL--RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|..
gi 568973811  674 DVGKGQFSKDTE 685
Cdd:cd00063    79 GGGESPPSESVT 90
fn3 pfam00041
Fibronectin type III domain;
1207-1292 7.50e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1207 PTNVSALATTSSSMLVRWSeiPEADRNGLVLGYKVRYKEKDsDSQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFTRI 1286
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811  1287 GDGSPS 1292
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1507-1601 4.95e-10

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.28  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1507 EAPTILSVTPHTTTSVLIRWQPPSEDkiNGILLGFRIRYRELLYDGLRGFTLRGINNPgakWAELTYLSKHRRYEIRMSI 1586
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*
gi 568973811 1587 YNAVGEGPLSPPQEV 1601
Cdd:cd00063    77 VNGGGESPPSESVTV 91
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 502-590 8.24e-10

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


The actual alignment was detected with superfamily member cd20952:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 87  Bit Score: 57.51  E-value: 8.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVEtNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGGN 581
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTIS--WLKDGVPLLGK-DERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd20952    79 ATWSAVLDV 87
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 126-201 1.01e-09

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


The actual alignment was detected with superfamily member cd20957:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 88  Bit Score: 57.16  E-value: 1.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811  126 QSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVNDKNGDNKTSQ 201
Cdd:cd20957    11 QTVDFGRTAVFNC-SVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAE 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 29-99 6.86e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 6.86e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811    29 PPYFKTEPVRTQVhLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYM--------ITSLDRTHAGFYRCIVRN 99
Cdd:pfam13927    1 KPVITVSPSSVTV-REGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLsgsnstltISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 226-290 5.04e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.80  E-value: 5.04e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811   226 KNTSVVAGtSEVTMECVANARPliKLHIVWKKDGAPLSSG------ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:pfam13927    9 SSVTVREG-ETVTLTCEATGSP--PPTITWYKNGEPISSGstrsrsLSGSNSTLTISNVTRSDAGTYTCVA 76
 
Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1276-1526 9.55e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.21  E-value: 9.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1276 YEVQVLAFTRIGDGSPShPPILERTLDDVPGPPMGILFPEVRTTSVRLIWQPPAAPNgiILAYQItHRlnATTANTATVE 1355
Cdd:COG3401   205 YYYRVAATDTGGESAPS-NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRV-YR--SNSGDGPFTK 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1356 VLAPSARQYMATGLKPESVYLFRITAQTRKG-WGEAAEALVVTTEkrdrPQPPSKPV-VQQEDVKARSVLLSWEPGSDgl 1433
Cdd:COG3401   279 VATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTD----LTPPAAPSgLTATAVGSSSITLSWTASSD-- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1434 SPVRYYTIQTRELPSGRWALHSASVshNASAFTVDRLKPFTSYKFRVKATNDIGDSEFSEESESLTTLQAAPDEAPTILS 1513
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTKIAETV--TTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASV 430

                         250
                  ....*....|...
gi 568973811 1514 VTPHTTTSVLIRW 1526
Cdd:COG3401   431 DAVPLTDVAGATA 443
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 408-496 9.59e-17

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 77.15  E-value: 9.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  408 ITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILAsgsVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568973811  488 DEASADLVV 496
Cdd:cd20952    79 ATWSAVLDV 87
I-set pfam07679
Immunoglobulin I-set domain;
406-496 2.28e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.14  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLLESG---SLLISPTHISDAGTYTCLAT 482
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGgtyTLTISNVQPDDSGKYTCVAT 76

                           90
                   ....*....|....
gi 568973811   483 NSRGVDEASADLVV 496
Cdd:pfam07679   77 NSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1611-1704 8.55e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1611 APQNVAIHSATATQLDVTWEPPPLDNqnGDIQGYKIYFWEVQRRNlTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDG--GPITGYVVEYREKGSGD-WKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 568973811 1691 AGDGPRSTPTRGQT 1704
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1679-1910 1.95e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 82.36  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1679 TAYMVSVAAFNAAGDGPRSTPTRGQTQQAAPSAPGSVKFSELTTTSVNVSWDAPqfPNGPLEGYRlVYEPCTPVDGVSKI 1758
Cdd:COG3401   203 TTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV--TESDATGYR-VYRSNSGDGPFTKV 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1759 VTvdVKGNSplwLKVKDLAEGMTYRFRIKAKTFTYGPEIEANI--TTGPGEGAPGPPGVPIIVRYSSAIAIHWSSGDPgk 1836
Cdd:COG3401   280 AT--VTTTS---YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD-- 352

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811 1837 GPITRYVIEARPSDEGLWDIlikdIPKEVTSYTFSMDILKPGVSYDFRVIAVNDYgfGTPSSPSQSVPAQKASP 1910
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTK----IAETVTTTSYTDTGLTPGTTYYYKVTAVDAA--GNESAPSEEVSATTASA 420
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1305-1398 3.22e-15

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.91  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1305 PGPPMGILFPEVRTTSVRLIWQPPAAPNGIILAYQITHRlNATTANTATVEVLAPSARQYMATGLKPESVYLFRITAQTR 1384
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR-EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 568973811 1385 KGWGEAAEALVVTT 1398
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1103-1198 4.57e-15

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1103 APANVTLRTASETSLWLRWMPLPEmeynGNPESVGYKIKYgRSDGHGKTLSHTVQDRVEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPED----DGGPITGYVVEY-REKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 568973811 1183 NAIGSGPWSQAVVGRT 1198
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
1103-1191 5.24e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1103 APANVTLRTASETSLWLRWMPLPEmeynGNPESVGYKIKYgRSDGHGKTLSHTVQDRVEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD----GNGPITGYEVEY-RPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 568973811  1183 NAIGSGPWS 1191
Cdd:pfam00041   77 NGGGEGPPS 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 312-401 6.02e-14

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 68.96  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEvGKLTRFkQRSDGGLQISGLLPDDTGMLQCFAHNAAG 391
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERA-TVEDGTLTIINVQPEDTGYYGCVATNEIG 78

                          90
                  ....*....|
gi 568973811  392 EAQTSTYLAV 401
Cdd:cd20978    79 DIYTETLLHV 88
fn3 pfam00041
Fibronectin type III domain;
1611-1697 9.30e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 9.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1611 APQNVAIHSATATQLDVTWEPPPldNQNGDIQGYKIYFWEVqRRNLTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP--DGNGPITGYEVEYRPK-NSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 568973811  1691 AGDGPRS 1697
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1709-1790 1.15e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 68.68  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1709 PSAPGSVKFSELTTTSVNVSWDAPQFPNGPLEGYRLVYEPctpvDGVSKIVTVDVKGNSPLWLKVKDLAEGMTYRFRIKA 1788
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYRE----KGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76


                  ..
gi 568973811 1789 KT 1790
Cdd:cd00063    77 VN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
737-1220 1.91e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  737 AGLPVGYQFKNITDADVNNLLLEDLIIWTNYEIEVAAYNSAGLGVYSSKVTEWTLQGVPTVPPGNVHAEATNSTTIRFTW 816
Cdd:COG3401    63 SGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  817 NAPSPQFINGINQGYKLIAWEPAQEEEVTMVTARPNFQDSIHVGFVS--------GLKKFTEYFTSVLCFTTPGDGPRSS 888
Cdd:COG3401   143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSttlvdgggDIEPGTTYYYRVAATDTGGESAPSN 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  889 PQLVRTHEDVPGPVGHLSFNDILDTSLKVSWQEPGEKNgiLTGYRI--------SWEEYNRTNTrvthylpnvtLEYRVT 960
Cdd:COG3401   223 EVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVyrsnsgdgPFTKVATVTT----------TSYTDT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  961 GLTALTTYTIEVAAMTSKGQGQVSASTISSGVPPELPGAPTNLGISNIGPRSVTLQFRPGYDGKtsISRWVVEAQVGVIG 1040
Cdd:COG3401   291 GLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGG 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1041 egeEWLLIYQLGNEPdarSMEVPDLNPFTYYSFRMRQVNIVGTSPPSQPSRKIQTLQAPPDIAPANVTLRTASETSLWLR 1120
Cdd:COG3401   369 ---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGAT 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1121 WMPLPEmeynGNPESVGYKIKYGRSDGHGKTlshTVQDRVEREYTIEDLEEWTEYRVQVQAFNAIGSGPWSQAVVGRTRE 1200
Cdd:COG3401   443 AAASAA----SNPGVSAAVLADGGDTGNAVP---FTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515

                         490       500
                  ....*....|....*....|
gi 568973811 1201 SVPSSGPTNVSALATTSSSM 1220
Cdd:COG3401   516 AAAAVGGAPDGTPNVTGASP 535
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 899-987 2.12e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  899 PGPVGHLSFNDILDTSLKVSWQEPGEKNGILTGYRISWEEYNRTNTRVTHYLPNVTLEYRVTGLTALTTYTIEVAAMTSK 978
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*....
gi 568973811  979 GQGQVSAST 987
Cdd:cd00063    81 GESPPSESV 89
I-set pfam07679
Immunoglobulin I-set domain;
312-401 3.33e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 3.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   312 PQFVREPeRHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKltRFKQRSDGG---LQISGLLPDDTGMLQCFAHN 388
Cdd:pfam07679    1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD--RFKVTYEGGtytLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 568973811   389 AAGEAQTSTYLAV 401
Cdd:pfam07679   78 SAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 412-496 4.86e-13

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 66.37  E-value: 4.86e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    412 PLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlPRFTLLESG---SLLISPTHISDAGTYTCLATNSRGVD 488
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES---GRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                    ....*...
gi 568973811    489 EASADLVV 496
Cdd:smart00410   78 SSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
1710-1790 5.12e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1710 SAPGSVKFSELTTTSVNVSWDAPQFPNGPLEGYRLVYEPCtpvDGVSKIVTVDVKGNSPLwLKVKDLAEGMTYRFRIKAK 1789
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK---NSGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQAV 76


                   .
gi 568973811  1790 T 1790
Cdd:pfam00041   77 N 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 594-685 5.35e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 66.75  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  594 PHAPEHPvaTLSTVERRAINLTWAKPFDGNSPLMRYVLEMSENNAPWTILLASVDPEATSVMVKGLVPARSYQFRLCAVN 673
Cdd:cd00063     1 PSPPTNL--RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|..
gi 568973811  674 DVGKGQFSKDTE 685
Cdd:cd00063    79 GGGESPPSESVT 90
fn3 pfam00041
Fibronectin type III domain;
900-984 6.54e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 6.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   900 GPVGHLSFNDILDTSLKVSWQEPGEKNGILTGYRISWEEYNrTNTRVTHY-LPNVTLEYRVTGLTALTTYTIEVAAMTSK 978
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKN-SGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811   979 GQGQVS 984
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1611-1694 7.35e-13

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.71  E-value: 7.35e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1611 APQNVAIHSATATQLDVTWEPPPLDNQNGDIQGYKIYFWEVQRRNLTERVKTlflAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 568973811   1691 AGDG 1694
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
1207-1292 7.50e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1207 PTNVSALATTSSSMLVRWSeiPEADRNGLVLGYKVRYKEKDsDSQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFTRI 1286
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811  1287 GDGSPS 1292
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1205-1294 1.49e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1205 SGPTNVSALATTSSSMLVRWSeiPEADRNGLVLGYKVRYKEKDSDsQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFT 1284
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWT--PPEDDGGPITGYVVEYREKGSG-DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|
gi 568973811 1285 RIGDGSPSHP 1294
Cdd:cd00063    79 GGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1103-1188 4.88e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.40  E-value: 4.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1103 APANVTLRTASETSLWLRWMPlPEMEYNGNPEsVGYKIKYGRSDGHGKTLSHTVQdrvEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEP-PPDDGITGYI-VGYRVEYREEGSEWKEVNVTPS---STSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 568973811   1183 NAIGSG 1188
Cdd:smart00060   78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 330-401 2.33e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 2.33e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811    330 VDIPCRAKGVPPPSITWYKDAA--LVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:smart00410   12 VTLSCEASGSPPPEVTWYKQGGklLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
596-681 4.01e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   596 APEHPvaTLSTVERRAINLTWAKPFDGNSPLMRYVLEMSENNAPWTILLASVDPEATSVMVKGLVPARSYQFRLCAVNDV 675
Cdd:pfam00041    2 APSNL--TVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811   676 GKGQFS 681
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 899-981 1.00e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.94  E-value: 1.00e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    899 PGPVGHLSFNDILDTSLKVSWQEPGEKNGI--LTGYRISWEEYNRTNTRVTHylPNVTLEYRVTGLTALTTYTIEVAAMT 976
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 568973811    977 SKGQG 981
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1404-1488 1.08e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.55  E-value: 1.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1404 PQPPSKPVVqqEDVKARSVLLSWEPGSD--GLSPVRYYTIQTRElPSGRWalHSASVSHNASAFTVDRLKPFTSYKFRVK 1481
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEPPPDdgITGYIVGYRVEYRE-EGSEW--KEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*..
gi 568973811   1482 ATNDIGD 1488
Cdd:smart00060   76 AVNGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1709-1790 3.06e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 3.06e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1709 PSAPGSVKFSELTTTSVNVSWDAPQFPNGplEGYRLVYEPC-TPVDGVSKIVTVDVKGNSplwLKVKDLAEGMTYRFRIK 1787
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEyREEGSEWKEVNVTPSSTS---YTLTGLKPGTEYEFRVR 75


                    ...
gi 568973811   1788 AKT 1790
Cdd:smart00060   76 AVN 78
fn3 pfam00041
Fibronectin type III domain;
1306-1389 4.34e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 4.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1306 GPPMGILFPEVRTTSVRLIWQPPAAPNGIILAYQITHRlNATTANTATVEVLAPSARQYMATGLKPESVYLFRITAQTRK 1385
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR-PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....
gi 568973811  1386 GWGE 1389
Cdd:pfam00041   80 GEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1507-1601 4.95e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.28  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1507 EAPTILSVTPHTTTSVLIRWQPPSEDkiNGILLGFRIRYRELLYDGLRGFTLRGINNPgakWAELTYLSKHRRYEIRMSI 1586
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*
gi 568973811 1587 YNAVGEGPLSPPQEV 1601
Cdd:cd00063    77 VNGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1205-1289 5.28e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.62  E-value: 5.28e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1205 SGPTNVSALATTSSSMLVRWSEIPEADRNGLVLGYKVRYKEKDSDSQPrfwLVEGNSSRSAQLTGLGKYVLYEVQVLAFT 1284
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKE---VNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 568973811   1285 RIGDG 1289
Cdd:smart00060   79 GAGEG 83
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 502-590 8.24e-10

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 57.51  E-value: 8.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVEtNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGGN 581
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTIS--WLKDGVPLLGK-DERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd20952    79 ATWSAVLDV 87
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 126-201 1.01e-09

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 57.16  E-value: 1.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811  126 QSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVNDKNGDNKTSQ 201
Cdd:cd20957    11 QTVDFGRTAVFNC-SVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAE 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 594-678 2.52e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.70  E-value: 2.52e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    594 PHAPEHPvaTLSTVERRAINLTWAKPFDGN--SPLMRYVLEMSENNAPWTILlaSVDPEATSVMVKGLVPARSYQFRLCA 671
Cdd:smart00060    1 PSPPSNL--RVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*..
gi 568973811    672 VNDVGKG 678
Cdd:smart00060   77 VNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 506-590 3.66e-09

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.59  E-value: 3.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    506 PQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLaVETNPRIRLDRNG---SLHISQTWSGDIGTYTCRVLSAGGND 582
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVT--WYKQGGKL-LAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                    ....*...
gi 568973811    583 SRNAHLRV 590
Cdd:smart00410   78 SSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 29-99 6.86e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 6.86e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811    29 PPYFKTEPVRTQVhLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYM--------ITSLDRTHAGFYRCIVRN 99
Cdd:pfam13927    1 KPVITVSPSSVTV-REGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLsgsnstltISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 501-575 1.06e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 1.06e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811   501 RITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLA-VETNPRIRLDRNGSLHISQTWSGDIGTYTCRV 575
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPTIT--WYKNGEPISsGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
fn3 pfam00041
Fibronectin type III domain;
1508-1596 1.32e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1508 APTILSVTPHTTTSVLIRWQPPSEdkINGILLGFRIRYRELLyDGLRGFTlrgINNPGAKW-AELTYLSKHRRYEIRMSI 1586
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKN-SGEPWNE---ITVPGTTTsVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 568973811  1587 YNAVGEGPLS 1596
Cdd:pfam00041   76 VNGGGEGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 226-290 5.04e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.80  E-value: 5.04e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811   226 KNTSVVAGtSEVTMECVANARPliKLHIVWKKDGAPLSSG------ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:pfam13927    9 SSVTVREG-ETVTLTCEATGSP--PPTITWYKNGEPISSGstrsrsLSGSNSTLTISNVTRSDAGTYTCVA 76
I-set pfam07679
Immunoglobulin I-set domain;
124-191 9.13e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.49  E-value: 9.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811   124 KRQSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLEN---TLVILSTVAPDAGRYYVQAVN 191
Cdd:pfam07679    8 KDVEVQEGESARFTC-TVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATN 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1508-1593 1.16e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 1.16e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1508 APTILSVTPHTTTSVLIRWQPPSEDKINGILLGFRIRYRELLYDglrgfTLRGINNPGAKWAELTYLSKHRRYEIRMSIY 1587
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSE-----WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 568973811   1588 NAVGEG 1593
Cdd:smart00060   78 NGAGEG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 237-290 1.47e-07

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.41  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  237 VTMECVANARPliKLHIVWKKDGAPLSSG------ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:cd00096     1 VTLTCSASGNP--PPTITWYKNGKPLPPSsrdsrrSELGNGTLTISNVTLEDSGTYTCVA 58
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 33-102 3.10e-06

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.51  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   33 KTEPVRTQVHLEGNRLVLTCMAEGSWP-LEFKWLHNNRELTRFSLEY----------RYMITSLDRTHAGFYRCIVRNRM 101
Cdd:cd05750     2 KLKEMKSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELNRKRPKNikirnkkknsELQINKAKLEDSGEYTCVVENIL 81


                  .
gi 568973811  102 G 102
Cdd:cd05750    82 G 82
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 44-113 6.91e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 6.91e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811     44 EGNRLVLTCMAEGSWPLEFKWLHNNREL----TRFSLEYRY-----MITSLDRTHAGFYRCIVRNRMGaLLQRQTEVQV 113
Cdd:smart00410    8 EGESVTLSCEASGSPPPEVTWYKQGGKLlaesGRFSVSRSGststlTISNVTPEDSGTYTCAATNSSG-SASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 226-308 8.33e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 8.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    226 KNTSVVAGtSEVTMECVANARPliKLHIVWKKDGAPLSSGISDYNRR-------LTIANPTVSDAGYYECEAmlrSSSVA 298
Cdd:smart00410    2 PSVTVKEG-ESVTLSCEASGSP--PPEVTWYKQGGKLLAESGRFSVSrsgststLTISNVTPEDSGTYTCAA---TNSSG 75

                            90
                    ....*....|
gi 568973811    299 PVTRGAYLSV 308
Cdd:smart00410   76 SASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 124-207 6.12e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.65  E-value: 6.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    124 KRQSVNHGEAAVIRaPRISSFPRPQVTWFRDG-RKIPPSSRIAITLEN---TLVILSTVAPDAGRYYVQAvndKNGDNKT 199
Cdd:smart00410    2 PSVTVKEGESVTLS-CEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAA---TNSSGSA 77


                    ....*...
gi 568973811    200 SQPITLAV 207
Cdd:smart00410   78 SSGTTLTV 85
 
Name Accession Description Interval E-value
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1276-1526 9.55e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.21  E-value: 9.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1276 YEVQVLAFTRIGDGSPShPPILERTLDDVPGPPMGILFPEVRTTSVRLIWQPPAAPNgiILAYQItHRlnATTANTATVE 1355
Cdd:COG3401   205 YYYRVAATDTGGESAPS-NEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRV-YR--SNSGDGPFTK 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1356 VLAPSARQYMATGLKPESVYLFRITAQTRKG-WGEAAEALVVTTEkrdrPQPPSKPV-VQQEDVKARSVLLSWEPGSDgl 1433
Cdd:COG3401   279 VATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTD----LTPPAAPSgLTATAVGSSSITLSWTASSD-- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1434 SPVRYYTIQTRELPSGRWALHSASVshNASAFTVDRLKPFTSYKFRVKATNDIGDSEFSEESESLTTLQAAPDEAPTILS 1513
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTKIAETV--TTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASV 430

                         250
                  ....*....|...
gi 568973811 1514 VTPHTTTSVLIRW 1526
Cdd:COG3401   431 DAVPLTDVAGATA 443
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 408-496 9.59e-17

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 77.15  E-value: 9.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  408 ITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILAsgsVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLL---GKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568973811  488 DEASADLVV 496
Cdd:cd20952    79 ATWSAVLDV 87
I-set pfam07679
Immunoglobulin I-set domain;
406-496 2.28e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 76.14  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLLESG---SLLISPTHISDAGTYTCLAT 482
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD----RFKVTYEGgtyTLTISNVQPDDSGKYTCVAT 76

                           90
                   ....*....|....
gi 568973811   483 NSRGVDEASADLVV 496
Cdd:pfam07679   77 NSAGEAEASAELTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 406-496 3.84e-16

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 75.57  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLD--STVIDGMSVVLACETSGAPRPAITWQKGERILasgsVQLPRFTLLESGSLLISPTHISDAGTYTCLATN 483
Cdd:cd04969     1 PDFELNPVKkkILAAKGGDVIIECKPKASPKPTISWSKGTELL----TNSSRICILPDGSLKIKNVTKSDEGKYTCFAVN 76

                          90
                  ....*....|...
gi 568973811  484 SRGVDEASADLVV 496
Cdd:cd04969    77 FFGKANSTGSLSV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1611-1704 8.55e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1611 APQNVAIHSATATQLDVTWEPPPLDNqnGDIQGYKIYFWEVQRRNlTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDG--GPITGYVVEYREKGSGD-WKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 568973811 1691 AGDGPRSTPTRGQT 1704
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1679-1910 1.95e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 82.36  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1679 TAYMVSVAAFNAAGDGPRSTPTRGQTQQAAPSAPGSVKFSELTTTSVNVSWDAPqfPNGPLEGYRlVYEPCTPVDGVSKI 1758
Cdd:COG3401   203 TTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV--TESDATGYR-VYRSNSGDGPFTKV 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1759 VTvdVKGNSplwLKVKDLAEGMTYRFRIKAKTFTYGPEIEANI--TTGPGEGAPGPPGVPIIVRYSSAIAIHWSSGDPgk 1836
Cdd:COG3401   280 AT--VTTTS---YTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsVTTDLTPPAAPSGLTATAVGSSSITLSWTASSD-- 352

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811 1837 GPITRYVIEARPSDEGLWDIlikdIPKEVTSYTFSMDILKPGVSYDFRVIAVNDYgfGTPSSPSQSVPAQKASP 1910
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTK----IAETVTTTSYTDTGLTPGTTYYYKVTAVDAA--GNESAPSEEVSATTASA 420
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1305-1398 3.22e-15

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.91  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1305 PGPPMGILFPEVRTTSVRLIWQPPAAPNGIILAYQITHRlNATTANTATVEVLAPSARQYMATGLKPESVYLFRITAQTR 1384
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR-EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 568973811 1385 KGWGEAAEALVVTT 1398
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1103-1198 4.57e-15

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 72.53  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1103 APANVTLRTASETSLWLRWMPLPEmeynGNPESVGYKIKYgRSDGHGKTLSHTVQDRVEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPED----DGGPITGYVVEY-REKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 568973811 1183 NAIGSGPWSQAVVGRT 1198
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 406-483 5.89e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 71.83  E-value: 5.89e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811   406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQlPRFTLLESGSLLISPTHISDAGTYTCLATN 483
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTR-SRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 408-487 6.18e-15

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 71.89  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  408 ITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLLESGSLLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd20968     2 ITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENN----RIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGI 77
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 410-496 1.73e-14

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 70.50  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  410 RGPLDSTVIDGMSVVLACETSGAPRPAITWQKGErilasGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDE 489
Cdd:cd05725     2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKED-----GELPKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIE 76


                  ....*..
gi 568973811  490 ASADLVV 496
Cdd:cd05725    77 ASATLTV 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1316-1803 3.25e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.12  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1316 VRTTSVRLIWQPPAAPNGIILAYQITHRLNATTANTATVEVLAPSARQYMATGLKPESVYLFRITAQTRKGWGEAAEALV 1395
Cdd:COG3401    45 SVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1396 VTTEKRDRPQPPSKPVVQQEDVKARSVLLSWEPGSDGLSPVRYYTIQTRELPSGRWALHSASVSHNASAFTVDRLKPFTS 1475
Cdd:COG3401   125 ATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTT 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1476 YKFRVKATNDIGDSEFSEESEsLTTLQAAPdEAPTILSVTPHTTTSVLIRWQPPSEDKINgillGFRIrYRELLYDGlrG 1555
Cdd:COG3401   205 YYYRVAATDTGGESAPSNEVS-VTTPTTPP-SAPTGLTATADTPGSVTLSWDPVTESDAT----GYRV-YRSNSGDG--P 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1556 FTLRginnpgAKWAELTY----LSKHRRYEIRMSIYNAVG-EGPLSPPQEVFVGEAVPtAAPQNVAIHSATATQLDVTWE 1630
Cdd:COG3401   276 FTKV------ATVTTTSYtdtgLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPP-AAPSGLTATAVGSSSITLSWT 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1631 PPPldnqNGDIQGYKIYFWEVQRRNLTERVKTlfLAENSVKLKNLTGYTAYMVSVAAFNAAGD-GPRSTPTRGQTQQAAP 1709
Cdd:COG3401   349 ASS----DADVTGYNVYRSTSGGGTYTKIAET--VTTTSYTDTGLTPGTTYYYKVTAVDAAGNeSAPSEEVSATTASAAS 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1710 SAPgsvkfselTTTSVNVSWDAPQFPNGPLEGYRLVYEPCTPVDGVSKIVTVDVKGNSPLWLKVKDLAEGMTYRFRIKAK 1789
Cdd:COG3401   423 GES--------LTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTG 494

                         490
                  ....*....|....
gi 568973811 1790 TFTYGPEIEANITT 1803
Cdd:COG3401   495 SLVGGSGASSVTNS 508
fn3 pfam00041
Fibronectin type III domain;
1103-1191 5.24e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1103 APANVTLRTASETSLWLRWMPLPEmeynGNPESVGYKIKYgRSDGHGKTLSHTVQDRVEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD----GNGPITGYEVEY-RPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 568973811  1183 NAIGSGPWS 1191
Cdd:pfam00041   77 NGGGEGPPS 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 312-401 6.02e-14

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 68.96  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEvGKLTRFkQRSDGGLQISGLLPDDTGMLQCFAHNAAG 391
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQ-GPMERA-TVEDGTLTIINVQPEDTGYYGCVATNEIG 78

                          90
                  ....*....|
gi 568973811  392 EAQTSTYLAV 401
Cdd:cd20978    79 DIYTETLLHV 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1404-1488 6.58e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.06  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1404 PQPPSKPVVqqEDVKARSVLLSWEPGSDGLSPVRYYTIQTRELPSGRWALHSaSVSHNASAFTVDRLKPFTSYKFRVKAT 1483
Cdd:cd00063     1 PSPPTNLRV--TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVE-VTPGSETSYTLTGLKPGTEYEFRVRAV 77


                  ....*
gi 568973811 1484 NDIGD 1488
Cdd:cd00063    78 NGGGE 82
fn3 pfam00041
Fibronectin type III domain;
1611-1697 9.30e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 9.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1611 APQNVAIHSATATQLDVTWEPPPldNQNGDIQGYKIYFWEVqRRNLTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP--DGNGPITGYEVEYRPK-NSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 568973811  1691 AGDGPRS 1697
Cdd:pfam00041   79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1709-1790 1.15e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 68.68  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1709 PSAPGSVKFSELTTTSVNVSWDAPQFPNGPLEGYRLVYEPctpvDGVSKIVTVDVKGNSPLWLKVKDLAEGMTYRFRIKA 1788
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYRE----KGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76


                  ..
gi 568973811 1789 KT 1790
Cdd:cd00063    77 VN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
737-1220 1.91e-13

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.81  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  737 AGLPVGYQFKNITDADVNNLLLEDLIIWTNYEIEVAAYNSAGLGVYSSKVTEWTLQGVPTVPPGNVHAEATNSTTIRFTW 816
Cdd:COG3401    63 SGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  817 NAPSPQFINGINQGYKLIAWEPAQEEEVTMVTARPNFQDSIHVGFVS--------GLKKFTEYFTSVLCFTTPGDGPRSS 888
Cdd:COG3401   143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSttlvdgggDIEPGTTYYYRVAATDTGGESAPSN 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  889 PQLVRTHEDVPGPVGHLSFNDILDTSLKVSWQEPGEKNgiLTGYRI--------SWEEYNRTNTrvthylpnvtLEYRVT 960
Cdd:COG3401   223 EVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVyrsnsgdgPFTKVATVTT----------TSYTDT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  961 GLTALTTYTIEVAAMTSKGQGQVSASTISSGVPPELPGAPTNLGISNIGPRSVTLQFRPGYDGKtsISRWVVEAQVGVIG 1040
Cdd:COG3401   291 GLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGG 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1041 egeEWLLIYQLGNEPdarSMEVPDLNPFTYYSFRMRQVNIVGTSPPSQPSRKIQTLQAPPDIAPANVTLRTASETSLWLR 1120
Cdd:COG3401   369 ---TYTKIAETVTTT---SYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGAT 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1121 WMPLPEmeynGNPESVGYKIKYGRSDGHGKTlshTVQDRVEREYTIEDLEEWTEYRVQVQAFNAIGSGPWSQAVVGRTRE 1200
Cdd:COG3401   443 AAASAA----SNPGVSAAVLADGGDTGNAVP---FTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515

                         490       500
                  ....*....|....*....|
gi 568973811 1201 SVPSSGPTNVSALATTSSSM 1220
Cdd:COG3401   516 AAAAVGGAPDGTPNVTGASP 535
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 899-987 2.12e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  899 PGPVGHLSFNDILDTSLKVSWQEPGEKNGILTGYRISWEEYNRTNTRVTHYLPNVTLEYRVTGLTALTTYTIEVAAMTSK 978
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ....*....
gi 568973811  979 GQGQVSAST 987
Cdd:cd00063    81 GESPPSESV 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 406-496 2.61e-13

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 67.52  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLL--ESG--SLLISPTHISDAGTYTCLA 481
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDS----AHKMLvrENGrhSLIIEPVTKRDAGIYTCIA 76

                          90
                  ....*....|....*
gi 568973811  482 TNSRGVDEASADLVV 496
Cdd:cd05744    77 RNRAGENSFNAELVV 91
I-set pfam07679
Immunoglobulin I-set domain;
312-401 3.33e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 66.90  E-value: 3.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   312 PQFVREPeRHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKltRFKQRSDGG---LQISGLLPDDTGMLQCFAHN 388
Cdd:pfam07679    1 PKFTQKP-KDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSD--RFKVTYEGGtytLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 568973811   389 AAGEAQTSTYLAV 401
Cdd:pfam07679   78 SAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 412-496 4.86e-13

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 66.37  E-value: 4.86e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    412 PLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlPRFTLLESG---SLLISPTHISDAGTYTCLATNSRGVD 488
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES---GRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                    ....*...
gi 568973811    489 EASADLVV 496
Cdd:smart00410   78 SSGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
1710-1790 5.12e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1710 SAPGSVKFSELTTTSVNVSWDAPQFPNGPLEGYRLVYEPCtpvDGVSKIVTVDVKGNSPLwLKVKDLAEGMTYRFRIKAK 1789
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK---NSGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQAV 76


                   .
gi 568973811  1790 T 1790
Cdd:pfam00041   77 N 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 594-685 5.35e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 66.75  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  594 PHAPEHPvaTLSTVERRAINLTWAKPFDGNSPLMRYVLEMSENNAPWTILLASVDPEATSVMVKGLVPARSYQFRLCAVN 673
Cdd:cd00063     1 PSPPTNL--RVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|..
gi 568973811  674 DVGKGQFSKDTE 685
Cdd:cd00063    79 GGGESPPSESVT 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 423-492 5.97e-13

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.81  E-value: 5.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811  423 VVLACETSGAPRPAITWQKGERILASgSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNS-RGVDEASA 492
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPP-SSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSaGGSASASV 70
fn3 pfam00041
Fibronectin type III domain;
900-984 6.54e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 6.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   900 GPVGHLSFNDILDTSLKVSWQEPGEKNGILTGYRISWEEYNrTNTRVTHY-LPNVTLEYRVTGLTALTTYTIEVAAMTSK 978
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKN-SGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811   979 GQGQVS 984
Cdd:pfam00041   80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1611-1694 7.35e-13

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.71  E-value: 7.35e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1611 APQNVAIHSATATQLDVTWEPPPLDNQNGDIQGYKIYFWEVQRRNLTERVKTlflAENSVKLKNLTGYTAYMVSVAAFNA 1690
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 568973811   1691 AGDG 1694
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
1207-1292 7.50e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1207 PTNVSALATTSSSMLVRWSeiPEADRNGLVLGYKVRYKEKDsDSQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFTRI 1286
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWT--PPPDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811  1287 GDGSPS 1292
Cdd:pfam00041   80 GEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1205-1294 1.49e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1205 SGPTNVSALATTSSSMLVRWSeiPEADRNGLVLGYKVRYKEKDSDsQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFT 1284
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWT--PPEDDGGPITGYVVEYREKGSG-DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|
gi 568973811 1285 RIGDGSPSHP 1294
Cdd:cd00063    79 GGGESPPSES 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 412-492 1.65e-12

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 65.11  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETS-GAPRPAITWQKGERILASGSvqlPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEA 490
Cdd:cd05724     4 PSDTQVAVGEMAVLECSPPrGHPEPTVSWRKDGQPLNLDN---ERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERES 80


                  ..
gi 568973811  491 SA 492
Cdd:cd05724    81 RA 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1103-1188 4.88e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.40  E-value: 4.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1103 APANVTLRTASETSLWLRWMPlPEMEYNGNPEsVGYKIKYGRSDGHGKTLSHTVQdrvEREYTIEDLEEWTEYRVQVQAF 1182
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEP-PPDDGITGYI-VGYRVEYREEGSEWKEVNVTPS---STSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 568973811   1183 NAIGSG 1188
Cdd:smart00060   78 NGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1817-1897 1.05e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1817 IIVRYSSAIAIHWSSGDPGKGPITRYVIEARPSDEGLWDILIkDIPKEVTSYTFSMdiLKPGVSYDFRVIAVNDYGFGTP 1896
Cdd:pfam00041    8 VTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEI-TVPGTTTSVTLTG--LKPGTEYEVRVQAVNGGGEGPP 84


                   .
gi 568973811  1897 S 1897
Cdd:pfam00041   85 S 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 330-397 1.06e-11

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 62.35  E-value: 1.06e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  330 VDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGG-LQISGLLPDDTGMLQCFAHNAAGEAQTST 397
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGtLTISNVTLEDSGTYTCVASNSAGGSASAS 69
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1822-1901 1.28e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.51  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1822 SSAIAIHWSSGDPGKGPITRYVIEARPSDEGLWDILIKDIPKEvTSYTFsmDILKPGVSYDFRVIAVNDYGFGTPSSPSQ 1901
Cdd:cd00063    14 STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTL--TGLKPGTEYEFRVRAVNGGGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 697-790 1.63e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.51  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  697 PPQNVIASGRTNQSIMIQWQPPPEShqNGILKGYIIRYCLAGLPVGYQFkNITDADVNNLLLEDLIIWTNYEIEVAAYNS 776
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDWKEV-EVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 568973811  777 AGLGVYSSKVTEWT 790
Cdd:cd00063    80 GGESPPSESVTVTT 93
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 334-401 1.98e-11

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 62.13  E-value: 1.98e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  334 CRAKGVPPPSITWYKDAALVeVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd20952    21 CQATGEPVPTISWLKDGVPL-LGKDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 330-401 2.33e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 2.33e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811    330 VDIPCRAKGVPPPSITWYKDAA--LVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:smart00410   12 VTLSCEASGSPPPEVTWYKQGGklLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
385-970 3.84e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.49  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  385 FAHNAAGEAQTSTYLAVTSIAPNITRGPLDSTVIDGM-SVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLESGS 463
Cdd:COG3401    13 IAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKeSPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTAT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  464 LLISPTHISDAGTYTCLATNSRGVDEASADLVVWARTRITKPPQDqSVIKGTQASMVCGVTHDPRVTVRYVWEKDGATLA 543
Cdd:COG3401    93 GLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAAT-AGTYALGAGLYGVDGANASGTTASSVAGAGVVVS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  544 VETNPRIRLDRNGSLHISQTWSGDIG--------TYTCRVLSAGGNDSRNAHLRVRQLPHAPEHPVA-TLSTVERRAINL 614
Cdd:COG3401   172 PDTSATAAVATTSLTVTSTTLVDGGGdiepgttyYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGlTATADTPGSVTL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  615 TWAKPfdGNSPLMRYVLEMSEN-NAPWTILlASVDpeATSVMVKGLVPARSYQFRLCAVNDVGKGqfSKDTERVSL-PEE 692
Cdd:COG3401   252 SWDPV--TESDATGYRVYRSNSgDGPFTKV-ATVT--TTSYTDTGLTNGTTYYYRVTAVDAAGNE--SAPSNVVSVtTDL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  693 PPTAPPQNVIASGRTNQSIMIQWQPPPESHqngiLKGYIIRYclaGLPVGYQFKNITD-ADVNNLLLEDLIIWTNYEIEV 771
Cdd:COG3401   325 TPPAAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVYR---STSGGGTYTKIAEtVTTTSYTDTGLTPGTTYYYKV 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  772 AAYNSAGL-GVYSSKVTEWTLQGVPTVPPGNVHAEATNSTTIRFTWNA---PSPQFINGINQGYKLIAWEPAQEEEVTMV 847
Cdd:COG3401   398 TAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAsaaSNPGVSAAVLADGGDTGNAVPFTTTSSTV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  848 TARPNFQDSIHVGFVSGLKKFTEYFTSVLCFTTPgDGPRSSPQLVRTHEDVPgpvghlsfNDILDTSLKVSWQEPGEKNG 927
Cdd:COG3401   478 TATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV-IGASAAAAVGGAPDGTP--------NVTGASPVTVGASTGDVLIT 548

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 568973811  928 ILTGYRISWEEYNRTNTrvthyLPNVTLEYRVTGLTALTTYTI 970
Cdd:COG3401   549 DLVSLTTSASSSVSGAG-----LGSGNLYLITTLGGSLLTTTS 586
fn3 pfam00041
Fibronectin type III domain;
596-681 4.01e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   596 APEHPvaTLSTVERRAINLTWAKPFDGNSPLMRYVLEMSENNAPWTILLASVDPEATSVMVKGLVPARSYQFRLCAVNDV 675
Cdd:pfam00041    2 APSNL--TVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 568973811   676 GKGQFS 681
Cdd:pfam00041   80 GEGPPS 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 406-496 6.93e-11

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 60.48  E-value: 6.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMS-VVLACETSGAPRPAITW-QKGERIlasgSVQLPRFTLlESGSLLISPTHISDAGTYTCLATN 483
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQdVTLPCQVTGVPQPKITWlHNGKPL----QGPMERATV-EDGTLTIINVQPEDTGYYGCVATN 75

                          90
                  ....*....|...
gi 568973811  484 SRGVDEASADLVV 496
Cdd:cd20978    76 EIGDIYTETLLHV 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 899-981 1.00e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.94  E-value: 1.00e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    899 PGPVGHLSFNDILDTSLKVSWQEPGEKNGI--LTGYRISWEEYNRTNTRVTHylPNVTLEYRVTGLTALTTYTIEVAAMT 976
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 568973811    977 SKGQG 981
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1404-1488 1.08e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 59.55  E-value: 1.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1404 PQPPSKPVVqqEDVKARSVLLSWEPGSD--GLSPVRYYTIQTRElPSGRWalHSASVSHNASAFTVDRLKPFTSYKFRVK 1481
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEPPPDdgITGYIVGYRVEYRE-EGSEW--KEVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*..
gi 568973811   1482 ATNDIGD 1488
Cdd:smart00060   76 AVNGAGE 82
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 311-401 1.22e-10

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 59.90  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  311 PPQFVREPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAAlvEVGKLTRFKQRSDGGLQ---ISGLLPDDTGMLQCFAH 387
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVR-LECRVTGNPTPVVRWFCEGK--ELQNSPDIQIHQEGDLHsliIAEAFEEDTGRYSCLAT 77

                          90
                  ....*....|....
gi 568973811  388 NAAGEAQTSTYLAV 401
Cdd:cd20972    78 NSVGSDTTSAEIFV 91
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 412-496 1.65e-10

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 59.58  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQK--GERILASGSVQLP--RFTLLESGSLLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd05726     6 PRDQVVALGRTVTFQCETKGNPQPAIFWQKegSQNLLFPYQPPQPssRFSVSPTGDLTITNVQRSDVGYYICQALNVAGS 85


                  ....*....
gi 568973811  488 DEASADLVV 496
Cdd:cd05726    86 ILAKAQLEV 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 405-496 1.93e-10

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 59.13  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  405 APNITRGPLDSTVIDGMSVVLACETSGAPRPAITW-QKGERILASgsvqlPRFTLLESG---SLLISPTHISDAGTYTCL 480
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWfCEGKELQNS-----PDIQIHQEGdlhSLIIAEAFEEDTGRYSCL 75

                          90
                  ....*....|....*.
gi 568973811  481 ATNSRGVDEASADLVV 496
Cdd:cd20972    76 ATNSVGSDTTSAEIFV 91
fn3 pfam00041
Fibronectin type III domain;
697-783 1.95e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   697 PPQNVIASGRTNQSIMIQWQPPPesHQNGILKGYIIRYCLAGLPvGYQFKNITDADVNNLLLEDLIIWTNYEIEVAAYNS 776
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP--DGNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 568973811   777 AGLGVYS 783
Cdd:pfam00041   79 GGEGPPS 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 405-496 2.05e-10

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 59.19  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  405 APNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILasgSVQLPRFTL-LESGSLLISPTHISDAGTYTCLATN 483
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL---QYAADRSTCeAGVGELHIQDVLPEDHGTYTCLAKN 77

                          90
                  ....*....|...
gi 568973811  484 SRGVDEASADLVV 496
Cdd:cd20976    78 AAGQVSCSAWVTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 697-780 2.40e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 2.40e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    697 PPQNVIASGRTNQSIMIQWQPPPESHQNgilkGYIIRYCLAGLPVGYQFKNI-TDADVNNLLLEDLIIWTNYEIEVAAYN 775
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGIT----GYIVGYRVEYREEGSEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 568973811    776 SAGLG 780
Cdd:smart00060   79 GAGEG 83
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 406-496 2.67e-10

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 58.64  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlPRFTLLESGSLLISPTHISDAGTYTCLATNSR 485
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNS---SRTLVYDNGTLDILITTVKDTGAFTCIASNPA 77

                          90
                  ....*....|.
gi 568973811  486 GVDEASADLVV 496
Cdd:cd05764    78 GEATARVELHI 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1709-1790 3.06e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 3.06e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1709 PSAPGSVKFSELTTTSVNVSWDAPQFPNGplEGYRLVYEPC-TPVDGVSKIVTVDVKGNSplwLKVKDLAEGMTYRFRIK 1787
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEyREEGSEWKEVNVTPSSTS---YTLTGLKPGTEYEFRVR 75


                    ...
gi 568973811   1788 AKT 1790
Cdd:smart00060   76 AVN 78
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 406-496 3.08e-10

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 58.57  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQlpRFTLLESG--SLLISPTHISDAGTYTCLATN 483
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAH--KMLVRENGvhSLIIEPVTSRDAGIYTCIATN 78

                          90
                  ....*....|...
gi 568973811  484 SRGVDEASADLVV 496
Cdd:cd20990    79 RAGQNSFNLELVV 91
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 412-496 3.20e-10

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 58.38  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQK-GERILASGSVQLprftllESGSLLISPTHISDAGTYTCLATNSRGVDEA 490
Cdd:cd05728     6 ISDTEADIGSSLRWECKASGNPRPAYRWLKnGQPLASENRIEV------EAGDLRITKLSLSDSGMYQCVAENKHGTIYA 79


                  ....*.
gi 568973811  491 SADLVV 496
Cdd:cd05728    80 SAELAV 85
fn3 pfam00041
Fibronectin type III domain;
1306-1389 4.34e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 4.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1306 GPPMGILFPEVRTTSVRLIWQPPAAPNGIILAYQITHRlNATTANTATVEVLAPSARQYMATGLKPESVYLFRITAQTRK 1385
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR-PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....
gi 568973811  1386 GWGE 1389
Cdd:pfam00041   80 GEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1507-1601 4.95e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.28  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811 1507 EAPTILSVTPHTTTSVLIRWQPPSEDkiNGILLGFRIRYRELLYDGLRGFTLRGINNPgakWAELTYLSKHRRYEIRMSI 1586
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*
gi 568973811 1587 YNAVGEGPLSPPQEV 1601
Cdd:cd00063    77 VNGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1205-1289 5.28e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.62  E-value: 5.28e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1205 SGPTNVSALATTSSSMLVRWSEIPEADRNGLVLGYKVRYKEKDSDSQPrfwLVEGNSSRSAQLTGLGKYVLYEVQVLAFT 1284
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKE---VNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 568973811   1285 RIGDG 1289
Cdd:smart00060   79 GAGEG 83
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 406-496 7.77e-10

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 57.82  E-value: 7.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKgERILASGSVQLPRFTLLESG---SLLISPTHISDAGTYTCLAT 482
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYK-NGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAK 79

                          90
                  ....*....|....
gi 568973811  483 NSRGVDEASADLVV 496
Cdd:cd20951    80 NIHGEASSSASVVV 93
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 502-590 8.24e-10

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 57.51  E-value: 8.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVEtNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGGN 581
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTIS--WLKDGVPLLGK-DERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd20952    79 ATWSAVLDV 87
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 406-496 8.81e-10

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 57.32  E-value: 8.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVI--DGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLLESGSLLISPTHISDAGTYTCLATN 483
Cdd:cd05852     1 PTFEFNPMKKKILaaKGGRVIIECKPKAAPKPKFSWSKGTELLVNNS----RISIWDDGSLEILNITKLDEGSYTCFAEN 76

                          90
                  ....*....|...
gi 568973811  484 SRGVDEASADLVV 496
Cdd:cd05852    77 NRGKANSTGVLSV 89
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 126-201 1.01e-09

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 57.16  E-value: 1.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811  126 QSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVNDKNGDNKTSQ 201
Cdd:cd20957    11 QTVDFGRTAVFNC-SVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAE 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 311-388 1.44e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.42  E-value: 1.44e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811   311 PPQFVREPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGG-LQISGLLPDDTGMLQCFAHN 388
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVT-LTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNStLTISNVTRSDAGTYTCVASN 78
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 330-400 2.38e-09

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 55.27  E-value: 2.38e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811  330 VDIPCRAKGVPPPSITWYKDAalVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLA 400
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDG--VQVTESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 594-678 2.52e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.70  E-value: 2.52e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    594 PHAPEHPvaTLSTVERRAINLTWAKPFDGN--SPLMRYVLEMSENNAPWTILlaSVDPEATSVMVKGLVPARSYQFRLCA 671
Cdd:smart00060    1 PSPPSNL--RVTDVTSTSVTLSWEPPPDDGitGYIVGYRVEYREEGSEWKEV--NVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*..
gi 568973811    672 VNDVGKG 678
Cdd:smart00060   77 VNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
1406-1487 2.88e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 2.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1406 PPSKPVVqqEDVKARSVLLSWEPGSDGLSPVRYYTIQTRELPSGRWALHSaSVSHNASAFTVDRLKPFTSYKFRVKATND 1485
Cdd:pfam00041    2 APSNLTV--TDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEI-TVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ..
gi 568973811  1486 IG 1487
Cdd:pfam00041   79 GG 80
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 506-590 3.39e-09

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 55.48  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  506 PQDQSVIKGTQASMVCG--VTH-DPRVTvryvWEKDGATLaVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVL-SAGGN 581
Cdd:cd05724     4 PSDTQVAVGEMAVLECSppRGHpEPTVS----WRKDGQPL-NLDNERVRIVDDGNLLIAEARKSDEGTYKCVATnMVGER 78


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd05724    79 ESRAARLSV 87
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 412-483 3.46e-09

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 55.95  E-value: 3.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQlpRFTLLESGSLLI-----SPTHISDAGTYTCLATN 483
Cdd:cd05722     8 PSDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDE--RRQQLPNGSLLItsvvhSKHNKPDEGFYQCVAQN 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 997-1091 3.48e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.58  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  997 PGAPTNLGISNIGPRSVTLQFRPGYDGKTSISRWVVEAQVGVIGEGEEWLliyqlGNEPDARSMEVPDLNPFTYYSFRMR 1076
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVE-----VTPGSETSYTLTGLKPGTEYEFRVR 75

                          90
                  ....*....|....*
gi 568973811 1077 QVNIVGTSPPSQPSR 1091
Cdd:cd00063    76 AVNGGGESPPSESVT 90
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 409-496 3.56e-09

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 55.80  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  409 TRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLESGsLLISPTHISDAGTYTCLATNSRGVD 488
Cdd:cd20949     3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADG-LLINKVTQDDTGEYTCRAYQVNSIA 81


                  ....*...
gi 568973811  489 EASADLVV 496
Cdd:cd20949    82 SDMQERTV 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 506-590 3.66e-09

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 55.59  E-value: 3.66e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    506 PQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLaVETNPRIRLDRNG---SLHISQTWSGDIGTYTCRVLSAGGND 582
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVT--WYKQGGKL-LAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                    ....*...
gi 568973811    583 SRNAHLRV 590
Cdd:smart00410   78 SSGTTLTV 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 403-494 3.83e-09

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


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  403 SIAPNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLESgSLLISPTHISDAGTYTCLAT 482
Cdd:cd05747     1 TLPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKS-TFEISKVQMSDEGNYTVVVE 79

                          90
                  ....*....|..
gi 568973811  483 NSRGVDEASADL 494
Cdd:cd05747    80 NSEGKQEAQFTL 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1305-1388 3.99e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 3.99e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1305 PGPPMGILFPEVRTTSVRLIWQPPAAPNGI--ILAYQITHRLNATTANTATVEvlaPSARQYMATGLKPESVYLFRITAQ 1382
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVT---PSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 568973811   1383 TRKGWG 1388
Cdd:smart00060   78 NGAGEG 83
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 420-496 4.21e-09

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 55.73  E-value: 4.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  420 GMSVVLACETSGAPRPAITWQK-GERILASGSVQLprfTLLESGS-LLISPTHISDAGTYTCLATNSRGVDEASADLVV 496
Cdd:cd05736    15 GVEASLRCHAEGIPLPRVQWLKnGMDINPKLSKQL---TLIANGSeLHISNVRYEDTGAYTCIAKNEGGVDEDISSLFV 90
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 500-594 4.43e-09

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 55.63  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  500 TRITKPPQDQSVIKGTQASMVCGVTHDPRVTVRYVWEKDGATLAVET-----NPRIRLDRNGSLHISQTWSGDIGTYTCR 574
Cdd:cd04970     3 TRITLAPSNADITVGENATLQCHASHDPTLDLTFTWSFNGVPIDLEKieghyRRRYGKDSNGDLEIVNAQLKHAGRYTCT 82

                          90       100
                  ....*....|....*....|
gi 568973811  575 VLSAGGNDSRNAHLRVRQLP 594
Cdd:cd04970    83 AQTVVDSDSASATLVVRGPP 102
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 29-99 6.86e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 54.49  E-value: 6.86e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811    29 PPYFKTEPVRTQVhLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYM--------ITSLDRTHAGFYRCIVRN 99
Cdd:pfam13927    1 KPVITVSPSSVTV-REGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLsgsnstltISNVTRSDAGTYTCVASN 78
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 409-496 7.01e-09

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 54.93  E-value: 7.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  409 TRGPLDSTVIDGMSVVLACETSGAPRPAITWQKgerilaSGSVQLP-----RFTLL-ESGSLLISPTHISDAGTYTCLAT 482
Cdd:cd05763     3 TKTPHDITIRAGSTARLECAATGHPTPQIAWQK------DGGTDFPaarerRMHVMpEDDVFFIVDVKIEDTGVYSCTAQ 76

                          90
                  ....*....|....
gi 568973811  483 NSRGVDEASADLVV 496
Cdd:cd05763    77 NSAGSISANATLTV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 416-486 9.26e-09

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 54.50  E-value: 9.26e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973811  416 TVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQlprfTLLESGSLLISPTH-ISDAGTYTCLATNSRG 486
Cdd:cd20958    11 TAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQ----RVFPNGTLVIENVQrSSDEGEYTCTARNQQG 78
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 312-401 1.03e-08

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 54.39  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREP-ERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKltRFKQRSDGGLQISGLLPDDTGMLQCFAHNAA 390
Cdd:cd04969     1 PDFELNPvKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSS--RICILPDGSLKIKNVTKSDEGKYTCFAVNFF 78

                          90
                  ....*....|.
gi 568973811  391 GEAQTSTYLAV 401
Cdd:cd04969    79 GKANSTGSLSV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 501-575 1.06e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 53.72  E-value: 1.06e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811   501 RITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLA-VETNPRIRLDRNGSLHISQTWSGDIGTYTCRV 575
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPTIT--WYKNGEPISsGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
fn3 pfam00041
Fibronectin type III domain;
1508-1596 1.32e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  1508 APTILSVTPHTTTSVLIRWQPPSEdkINGILLGFRIRYRELLyDGLRGFTlrgINNPGAKW-AELTYLSKHRRYEIRMSI 1586
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVEYRPKN-SGEPWNE---ITVPGTTTsVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 568973811  1587 YNAVGEGPLS 1596
Cdd:pfam00041   76 VNGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
501-590 1.37e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 53.80  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   501 RITKPPQDQSVIKGTQASMVCGVTHDPRVTVryVWEKDGATLAveTNPRIRLDRNG---SLHISQTWSGDIGTYTCRVLS 577
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEV--SWFKDGQPLR--SSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 568973811   578 AGGNDSRNAHLRV 590
Cdd:pfam07679   78 SAGEAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
998-1087 2.07e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   998 GAPTNLGISNIGPRSVTLQFRPGYDGKTSISRWVVEAQVgvIGEGEEWLliyQLGNEPDARSMEVPDLNPFTYYSFRMRQ 1077
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRP--KNSGEPWN---EITVPGTTTSVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 568973811  1078 VNIVGTSPPS 1087
Cdd:pfam00041   76 VNGGGEGPPS 85
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 419-496 2.95e-08

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 52.63  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  419 DGMSVVLACETSGAPRPAITWQKGerilasGSvQLP---RFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASADLV 495
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAWTKG------GS-QLSvdrRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLT 73


                  .
gi 568973811  496 V 496
Cdd:cd05745    74 V 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 798-894 2.98e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 53.27  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  798 PPGNVHAEATNSTTIRFTWNAPSPqfINGINQGYKlIAWEPAQEEEVTMVTARPNFQDSIHvgfVSGLKKFTEYFTSVLC 877
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPED--DGGPITGYV-VEYREKGSGDWKEVEVTPGSETSYT---LTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 568973811  878 FTTPGDGPRSSPQLVRT 894
Cdd:cd00063    77 VNGGGESPPSESVTVTT 93
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 504-590 3.65e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 52.40  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  504 KPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVeTNPRIRLDRngSLHISQTWSGDIGTYTCRVLSAGGNDS 583
Cdd:cd05725     2 KRPQNQVVLVDDSAEFQCEVGGDPVPTVR--WRKEDGELPK-GRYEILDDH--SLKIRKVTAGDMGSYTCVAENMVGKIE 76


                  ....*..
gi 568973811  584 RNAHLRV 590
Cdd:cd05725    77 ASATLTV 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 226-290 5.04e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.80  E-value: 5.04e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811   226 KNTSVVAGtSEVTMECVANARPliKLHIVWKKDGAPLSSG------ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:pfam13927    9 SSVTVREG-ETVTLTCEATGSP--PPTITWYKNGEPISSGstrsrsLSGSNSTLTISNVTRSDAGTYTCVA 76
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 406-496 5.07e-08

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 52.55  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKG----ERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLA 481
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQvpgkENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTA 80

                          90
                  ....*....|....*
gi 568973811  482 TNSRGVDEASADLVV 496
Cdd:cd05765    81 RNSGGLLRANFPLSV 95
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 412-486 5.57e-08

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 52.31  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQK------GE-RILASGsvqlPRFTLLESGSLLISPTHISDAGTYTCLATNS 484
Cdd:cd20954     8 PVDANVAAGQDVMLHCQADGFPTPTVTWKKatgstpGEyKDLLYD----PNVRILPNGTLVFGHVQKENEGHYLCEAKNG 83


                  ..
gi 568973811  485 RG 486
Cdd:cd20954    84 IG 85
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 423-496 5.78e-08

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 51.41  E-value: 5.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811  423 VVLACETSGAPRPAITWQK-GERILASGsvqlpRFTLLESGSLLISPTHISDAGTYTCLATNSRGVdeASADLVV 496
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKdGVQVTESG-----KFHISPEGYLAIRDVGVADQGRYECVARNTIGY--ASVSMVL 68
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 315-401 6.49e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 51.63  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  315 VREPERHITAeMEKVVDIPCRAKGVPPPSITWYKdaalvEVGKL--TRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGE 392
Cdd:cd05725     1 VKRPQNQVVL-VDDSAEFQCEVGGDPVPTVRWRK-----EDGELpkGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGK 74


                  ....*....
gi 568973811  393 AQTSTYLAV 401
Cdd:cd05725    75 IEASATLTV 83
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 420-499 6.51e-08

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 52.24  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  420 GMSVVLACETSGAPRPAITWQKGERILASGSvqlPRFTLLESGS-LLISPTHISDAGTYTCLATNSRGVDEASADLVVWA 498
Cdd:cd05730    18 GQSVTLACDADGFPEPTMTWTKDGEPIESGE---EKYSFNEDGSeMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVFA 94


                  .
gi 568973811  499 R 499
Cdd:cd05730    95 K 95
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 406-487 6.70e-08

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 52.17  E-value: 6.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQK-GERILASGSVQLPRFTLLESGSLLI-----SPTHISDAGTYTC 479
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKnGQPLETDKDDPRSHRIVLPSGSLFFlrvvhGRKGRSDEGVYVC 80


                  ....*...
gi 568973811  480 LATNSRGV 487
Cdd:cd07693    81 VAHNSLGE 88
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 423-496 7.11e-08

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 52.29  E-value: 7.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  423 VVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLES----GSLLISPTHISDAGTYTCLATNSRGVDEASADLVV 496
Cdd:cd05869    20 ITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSharvSSLTLKYIQYTDAGEYLCTASNTIGQDSQSMYLEV 97
I-set pfam07679
Immunoglobulin I-set domain;
124-191 9.13e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.49  E-value: 9.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811   124 KRQSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLEN---TLVILSTVAPDAGRYYVQAVN 191
Cdd:pfam07679    8 KDVEVQEGESARFTC-TVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATN 77
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 328-401 1.04e-07

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 51.09  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811  328 KVVDIPCRAKGVPPPSITWYKDAALVEVGKltRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd05745     3 QTVDFLCEAQGYPQPVIAWTKGGSQLSVDR--RHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1508-1593 1.16e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 1.16e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   1508 APTILSVTPHTTTSVLIRWQPPSEDKINGILLGFRIRYRELLYDglrgfTLRGINNPGAKWAELTYLSKHRRYEIRMSIY 1587
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSE-----WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 568973811   1588 NAVGEG 1593
Cdd:smart00060   78 NGAGEG 83
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 408-496 1.27e-07

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 51.01  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  408 ITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKgerilASGSvQLPRFTLLESGSLL-ISPTHISDAGTYTCLATNSRG 486
Cdd:cd04968     4 KVRFPADTYALKGQTVTLECFALGNPVPQIKWRK-----VDGS-PSSQWEITTSEPVLeIPNVQFEDEGTYECEAENSRG 77

                          90
                  ....*....|
gi 568973811  487 VDEASADLVV 496
Cdd:cd04968    78 KDTVQGRIIV 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 406-496 1.30e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 51.35  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNIT--RGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlPRFTLLESGSLLISPTHI-SDAGTYTCLAT 482
Cdd:cd20970     1 PVIStpQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN---TRYIVRENGTTLTIRNIRrSDMGIYLCIAS 77

                          90
                  ....*....|....*
gi 568973811  483 N-SRGVDEASADLVV 496
Cdd:cd20970    78 NgVPGSVEKRITLQV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 237-290 1.47e-07

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 50.41  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  237 VTMECVANARPliKLHIVWKKDGAPLSSG------ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:cd00096     1 VTLTCSASGNP--PPTITWYKNGKPLPPSsrdsrrSELGNGTLTISNVTLEDSGTYTCVA 58
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 314-388 3.65e-07

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 50.17  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  314 FVREPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGGLQISGLL------PDDtGMLQCFAH 387
Cdd:cd05722     4 FLSEPSDIVAMRGGPVV-LNCSAESDPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLITSVVhskhnkPDE-GFYQCVAQ 81


                  .
gi 568973811  388 N 388
Cdd:cd05722    82 N 82
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 311-401 3.66e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 49.94  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  311 PPQFVREPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAA 390
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFV-AQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                          90
                  ....*....|.
gi 568973811  391 GEAQTSTYLAV 401
Cdd:cd20976    80 GQVSCSAWVTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 517-586 4.07e-07

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.25  E-value: 4.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973811  517 ASMVCGVTHDPRVTVRyvWEKDGATLAVETNPRIRL-DRNGSLHISQTWSGDIGTYTCRVL-SAGGNDSRNA 586
Cdd:cd00096     1 VTLTCSASGNPPPTIT--WYKNGKPLPPSSRDSRRSeLGNGTLTISNVTLEDSGTYTCVASnSAGGSASASV 70
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 311-401 4.45e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 49.93  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  311 PPQF-VREPERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKlTRFKQRSDGG-LQISGLLPDDTGMLQCFAHN 388
Cdd:cd05730     1 PPTIrARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGE-EKYSFNEDGSeMTILDVDKLDEAEYTCIAEN 79

                          90
                  ....*....|...
gi 568973811  389 AAGEAQTSTYLAV 401
Cdd:cd05730    80 KAGEQEAEIHLKV 92
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 412-496 4.65e-07

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 49.50  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQKgerilaSGSVQLPR--FTLLESGSLLISPTHISDAGTYTCLATNSRGVDE 489
Cdd:cd05723     4 PSNIYAHESMDIVFECEVTGKPTPTVKWVK------NGDVVIPSdyFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQ 77


                  ....*..
gi 568973811  490 ASADLVV 496
Cdd:cd05723    78 ASAQLII 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 140-195 5.15e-07

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 5.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  140 RISSFPRPQVTWFRDGRKIPPSSRIAITLEN---TLVILSTVAPDAGRYYVQAVNDKNG 195
Cdd:cd00096     6 SASGNPPPTITWYKNGKPLPPSSRDSRRSELgngTLTISNVTLEDSGTYTCVASNSAGG 64
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 322-401 5.37e-07

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 49.70  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  322 ITAEMEKVVDIPCRAKGVPPPSITW-YKDAALVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLA 400
Cdd:cd20969    12 VFVDEGHTVQFVCRADGDPPPAILWlSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLH 91


                  .
gi 568973811  401 V 401
Cdd:cd20969    92 V 92
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 318-391 6.12e-07

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 49.24  E-value: 6.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811  318 PERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKLT-RFKQRSDGGLQISGLLPDDTGMLQCFAHNAAG 391
Cdd:cd05738     5 GPQLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTATSNgRIKQLRSGALQIENSEESDQGKYECVATNSAG 79
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 416-492 6.58e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 49.12  E-value: 6.58e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811   416 TVIDGMSVVLACETS-GAPRPAITWQKGERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASA 492
Cdd:pfam00047    7 TVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 412-488 6.68e-07

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 49.41  E-value: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQ--KG------ERILASGSvqlpRFTLLESGSLLISPTHISDAGTYTCLATN 483
Cdd:cd05734     8 PNDQDGIYGKAVVLNCSADGYPPPTIVWKhsKGsgvpqfQHIVPLNG----RIQLLSNGSLLIKHVLEEDSGYYLCKVSN 83


                  ....*
gi 568973811  484 SRGVD 488
Cdd:cd05734    84 DVGAD 88
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 314-401 8.12e-07

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 48.74  E-value: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  314 FVREPERHITAEMEkVVDIPCRAKGVPPPSITWYKDAALVE-VGKLTRFKQRSdGGLQISGLLPDDTGMLQCFAHNAAGE 392
Cdd:cd05867     2 WTRRPQSHLYGPGE-TARLDCQVEGIPTPNITWSINGAPIEgTDPDPRRHVSS-GALILTDVQPSDTAVYQCEARNRHGN 79


                  ....*....
gi 568973811  393 AQTSTYLAV 401
Cdd:cd05867    80 LLANAHVHV 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 334-401 8.97e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 48.72  E-value: 8.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  334 CRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDG--GLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd20973    19 CKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGlcSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 334-401 1.14e-06

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 48.35  E-value: 1.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  334 CRAKGVPPPSITWYKDAALVEVGKLtrFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd05723    19 CEVTGKPTPTVKWVKNGDVVIPSDY--FKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQLII 84
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 312-401 1.16e-06

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 48.57  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGKLTR-FKQRSDGG---LQISGLLPDDTGMLQCFAH 387
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAK-LRVEVQGKPDPEVKWYKNGVPIDPSSIPGkYKIESEYGvhvLHIRRVTVEDSAVYSAVAK 79

                          90
                  ....*....|....
gi 568973811  388 NAAGEAQTSTYLAV 401
Cdd:cd20951    80 NIHGEASSSASVVV 93
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 312-401 1.91e-06

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.88  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHITAEmEKVVDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDG--GLQISGLLPDDTGMLQCFAHNA 389
Cdd:cd05744     1 PHFLQAPGDLEVQE-GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGrhSLIIEPVTKRDAGIYTCIARNR 79

                          90
                  ....*....|..
gi 568973811  390 AGEAQTSTYLAV 401
Cdd:cd05744    80 AGENSFNAELVV 91
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 409-496 1.93e-06

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 47.59  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  409 TRGPLDSTVIDGMSVVLACETSGAPRPAITWQKgerilasGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVD 488
Cdd:cd05739     1 SIPPSNHEVMPGGSVNLTCVAVGAPMPYVKWMK-------GGEELTKEDEMPVGRNVLELTNIYESANYTCVAISSLGMI 73


                  ....*...
gi 568973811  489 EASADLVV 496
Cdd:cd05739    74 EATAQVTV 81
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 408-496 1.94e-06

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 48.08  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  408 ITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKG----ERILASGsvqlpRFTLLESGSLLISPTHISDAGTYTCLATN 483
Cdd:cd05738     2 IDMGPQLKVVEKARTATMLCAASGNPDPEISWFKDflpvDTATSNG-----RIKQLRSGALQIENSEESDQGKYECVATN 76

                          90
                  ....*....|....
gi 568973811  484 SRGVD-EASADLVV 496
Cdd:cd05738    77 SAGTRySAPANLYV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 126-191 2.03e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.56  E-value: 2.03e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811   126 QSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLEN---TLVILSTVAPDAGRYYVQAVN 191
Cdd:pfam13927   11 VTVREGETVTLTC-EATGSPPPTITWYKNGEPISSGSTRSRSLSGsnsTLTISNVTRSDAGTYTCVASN 78
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 412-487 2.07e-06

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 48.02  E-value: 2.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  412 PLDStviDGMSVVLACETSGAPRPAITW-QKGERILASGSVqlpRFTLLEsGSLLIS-PTHISDAGTYTCLATNSRGV 487
Cdd:cd05848    14 PTDS---DEKKVILNCEARGNPVPTYRWlRNGTEIDTESDY---RYSLID-GNLIISnPSEVKDSGRYQCLATNSIGS 84
fn3 pfam00041
Fibronectin type III domain;
798-887 2.21e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.41  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   798 PPGNVHAEATNSTTIRFTWNAPSPQfiNGINQGYKLIAWEPAQEEEVTMVTARPNfQDSIHvgfVSGLKKFTEYFTSVLC 877
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDG--NGPITGYEVEYRPKNSGEPWNEITVPGT-TTSVT---LTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 568973811   878 FTTPGDGPRS 887
Cdd:pfam00041   76 VNGGGEGPPS 85
IgI_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig ...
 332-396 2.47e-06

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409459  Cd Length: 95  Bit Score: 47.66  E-value: 2.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  332 IPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRS-DGGLQI---SGLLPDD-TGMLQCFAHNAAGEAQTS 396
Cdd:cd05875    21 IECEAKGNPVPTFHWTRNGKFFNVAKDPRVSMRRrSGTLVIdfrGGGRPEDyEGEYQCFARNKFGTALSN 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 140-200 2.54e-06

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 47.49  E-value: 2.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811  140 RISSFPRPQVTWFRDGRKIPPSSRIAITLEN----TLVILSTVAPDAGRYYVQAVNdKNGDNKTS 200
Cdd:cd05744    23 KVSGLPTPDLFWQLNGKPVRPDSAHKMLVREngrhSLIIEPVTKRDAGIYTCIARN-RAGENSFN 86
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 416-491 2.67e-06

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 47.52  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  416 TVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLES----GSLLISPTHISDAGTYTCLATNSRGVDEAS 491
Cdd:cd05732    12 TAVELEQITLTCEAEGDPIPEITWRRATRGISFEEGDLDGRIVVRGharvSSLTLKDVQLTDAGRYDCEASNRIGGDQQS 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 412-496 2.80e-06

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 47.46  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlPRFTLLESGS----LLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd05892     7 PQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNT---DRISLYQDNCgricLLIQNANKKDAGWYTVSAVNEAGV 83


                  ....*....
gi 568973811  488 DEASADLVV 496
Cdd:cd05892    84 VSCNARLDV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 33-102 3.10e-06

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 47.51  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   33 KTEPVRTQVHLEGNRLVLTCMAEGSWP-LEFKWLHNNRELTRFSLEY----------RYMITSLDRTHAGFYRCIVRNRM 101
Cdd:cd05750     2 KLKEMKSQTVQEGSKLVLKCEATSENPsPRYRWFKDGKELNRKRPKNikirnkkknsELQINKAKLEDSGEYTCVVENIL 81


                  .
gi 568973811  102 G 102
Cdd:cd05750    82 G 82
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 413-496 3.26e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 47.18  E-value: 3.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  413 LDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLLESG----SLLISPTHISDAGTYTCLATNSRGVD 488
Cdd:cd20973     5 RDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESR----RFQIDQDEdglcSLIISDVCGDDSGKYTCKAVNSLGEA 80


                  ....*...
gi 568973811  489 EASADLVV 496
Cdd:cd20973    81 TCSAELTV 88
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 318-393 3.84e-06

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 47.02  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  318 PERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGG---LQISGLLPDD-TGMLQCFAHNAAGEA 393
Cdd:cd05733     8 PKDYIVDPRDNIT-IKCEAKGNPQPTFRWTKDGKFFDPAKDPRVSMRRRSGtlvIDNHNGGPEDyQGEYQCYASNELGTA 86
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 312-391 4.21e-06

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 47.24  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHI--TAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQrSDGGLQISGllPD---DTGMLQCFA 386
Cdd:cd04967     2 PVFEEQPDDTIfpEDSDEKKVALNCRARANPVPSYRWLMNGTEIDLESDYRYSL-VDGTLVISN--PSkakDAGHYQCLA 78


                  ....*
gi 568973811  387 HNAAG 391
Cdd:cd04967    79 TNTVG 83
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 405-496 4.36e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 46.62  E-value: 4.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   405 APNITRGPldSTVIDGMSVVLACETSGAPRPAITWQKGERILASgsvqlprftlleSGSLLISPTHISDAGTYTCLATNS 484
Cdd:pfam13895    1 KPVLTPSP--TVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISS------------SPNFFTLSVSAEDSGTYTCVARNG 66

                           90
                   ....*....|...
gi 568973811   485 RGV-DEASADLVV 496
Cdd:pfam13895   67 RGGkVSNPVELTV 79
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 334-401 4.73e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.44  E-value: 4.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  334 CRAKGVPPPSITWYKDAA-LVEVGKLtrfkQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd05728    21 CKASGNPRPAYRWLKNGQpLASENRI----EVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 798-884 5.15e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 5.15e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    798 PPGNVHAEATNSTTIRFTWNAPSPQFINGINQGYKLIAWEP-AQEEEVTMVTARPNFQdsihvgfVSGLKKFTEYFTSVL 876
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYT-------LTGLKPGTEYEFRVR 75


                    ....*...
gi 568973811    877 CFTTPGDG 884
Cdd:smart00060   76 AVNGAGEG 83
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 313-404 5.84e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 46.87  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  313 QFVREPERHITAeMEKVVDIPCRAKGVPPPSITWYKDAALV------EVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFA 386
Cdd:cd05726     1 QFVVKPRDQVVA-LGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqPPQPSSRFSVSPTGDLTITNVQRSDVGYYICQA 79

                          90
                  ....*....|....*...
gi 568973811  387 HNAAGEAQTSTYLAVTSI 404
Cdd:cd05726    80 LNVAGSILAKAQLEVTDV 97
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 48-102 6.71e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.78  E-value: 6.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568973811   48 LVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYM--------ITSLDRTHAGFYRCIVRNRMG 102
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSelgngtltISNVTLEDSGTYTCVASNSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 44-113 6.91e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 6.91e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811     44 EGNRLVLTCMAEGSWPLEFKWLHNNREL----TRFSLEYRY-----MITSLDRTHAGFYRCIVRNRMGaLLQRQTEVQV 113
Cdd:smart00410    8 EGESVTLSCEASGSPPPEVTWYKQGGKLlaesGRFSVSRSGststlTISNVTPEDSGTYTCAATNSSG-SASSGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1822-1894 7.12e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 7.12e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811   1822 SSAIAIHWS--SGDPGKGPITRYVIEARPSDEGlWDILIKDIPKevTSYTFSMdiLKPGVSYDFRVIAVNDYGFG 1894
Cdd:smart00060   14 STSVTLSWEppPDDGITGYIVGYRVEYREEGSE-WKEVNVTPSS--TSYTLTG--LKPGTEYEFRVRAVNGAGEG 83
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 131-192 7.43e-06

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 7.43e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811  131 GEAAVIRAPrISSFPRPQVTWFRDGRKIPPSSRIAI--TLENT-LVILSTVAPDAGRYYVQAVND 192
Cdd:cd05748     7 GESLRLDIP-IKGRPTPTVTWSKDGQPLKETGRVQIetTASSTsLVIKNAKRSDSGKYTLTLKNS 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 226-308 8.33e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 8.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    226 KNTSVVAGtSEVTMECVANARPliKLHIVWKKDGAPLSSGISDYNRR-------LTIANPTVSDAGYYECEAmlrSSSVA 298
Cdd:smart00410    2 PSVTVKEG-ESVTLSCEASGSP--PPEVTWYKQGGKLLAESGRFSVSrsgststLTISNVTPEDSGTYTCAA---TNSSG 75

                            90
                    ....*....|
gi 568973811    299 PVTRGAYLSV 308
Cdd:smart00410   76 SASSGTTLTV 85
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 420-486 8.49e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 46.01  E-value: 8.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  420 GMSVVLACETSGAPRPAITWQKGERILASGSVQLPR---FTLLESGsllISPthiSDAGTYTCLATNSRG 486
Cdd:cd05856    19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKkkkWTLSLKN---LKP---EDSGKYTCHVSNRAG 82
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 314-401 1.34e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.69  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  314 FVREPeRHITAEMEKVVDIPCRAKGVPPPSITWYKDAAlvevgklTRF---KQR------SDGGLQISGLLPDDTGMLQC 384
Cdd:cd05763     2 FTKTP-HDITIRAGSTARLECAATGHPTPQIAWQKDGG-------TDFpaaRERrmhvmpEDDVFFIVDVKIEDTGVYSC 73

                          90
                  ....*....|....*..
gi 568973811  385 FAHNAAGEAQTSTYLAV 401
Cdd:cd05763    74 TAQNSAGSISANATLTV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 323-401 1.68e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 45.19  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  323 TAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKlTRFKQRSDGG-LQISGLLPDDTGMLQCFAHN-AAGEAQTSTYLA 400
Cdd:cd20970    13 TAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN-TRYIVRENGTtLTIRNIRRSDMGIYLCIASNgVPGSVEKRITLQ 91


                  .
gi 568973811  401 V 401
Cdd:cd20970    92 V 92
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 503-590 1.79e-05

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.30  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  503 TKPPQDQSVIKGTQASMVCGVTHDPrvTVRYVWEKDGAT---LAVETNPRIRLDrNGSLHISQTWSGDIGTYTCRVLSAG 579
Cdd:cd05763     3 TKTPHDITIRAGSTARLECAATGHP--TPQIAWQKDGGTdfpAARERRMHVMPE-DDVFFIVDVKIEDTGVYSCTAQNSA 79

                          90
                  ....*....|.
gi 568973811  580 GNDSRNAHLRV 590
Cdd:cd05763    80 GSISANATLTV 90
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 337-401 1.85e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 45.08  E-value: 1.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  337 KGVPPPSITWYKDAA-LVEVGKltRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTST-YLAV 401
Cdd:cd05724    23 RGHPEPTVSWRKDGQpLNLDNE--RVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESRAaRLSV 87
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 416-496 1.93e-05

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 45.07  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  416 TVIDGMSVVLACETSGAPRPAITW-QKGERILASGSVQlpRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASADL 494
Cdd:cd20969    13 FVDEGHTVQFVCRADGDPPPAILWlSPRKHLVSAKSNG--RLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 90


                  ..
gi 568973811  495 VV 496
Cdd:cd20969    91 HV 92
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 412-496 1.96e-05

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 45.34  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQKGERILAS--GSVQLPRFTLLESGS----------LLISPTHISDAGTYTC 479
Cdd:cd05858     8 PANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSkyGPDGLPYVEVLKTAGvnttdkeievLYLRNVTFEDAGEYTC 87

                          90
                  ....*....|....*..
gi 568973811  480 LATNSRGVDEASADLVV 496
Cdd:cd05858    88 LAGNSIGISHHSAWLTV 104
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 226-290 1.99e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 45.08  E-value: 1.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  226 KNTSVVaGTSEVTMECVANARPliKLHIVWKKDGAPLS--SGISDYNR-RLTIANPTVSDAGYYECEA 290
Cdd:cd20978     9 KNVVVK-GGQDVTLPCQVTGVP--QPKITWLHNGKPLQgpMERATVEDgTLTIINVQPEDTGYYGCVA 73
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 420-496 2.18e-05

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 44.40  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  420 GMSVVLACETSGAPRPAITWQkgeriLASGSVQLPRFTLLES----GSLLISPTHISDAGTYTCLATNSRGVDEASADLV 495
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWR-----LNWGHVPDSARVSITSeggyGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGI 75


                  .
gi 568973811  496 V 496
Cdd:cd05743    76 L 76
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 504-590 2.46e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  504 KPPQDQSVIKGTQASMVCGVT-HDPrvTVRYVWEKDGATLAVETNPRIRL---DRNGSLHISQTWSGDIGTYTCRVLSAG 579
Cdd:cd05750     4 KEMKSQTVQEGSKLVLKCEATsENP--SPRYRWFKDGKELNRKRPKNIKIrnkKKNSELQINKAKLEDSGEYTCVVENIL 81

                          90
                  ....*....|.
gi 568973811  580 GNDSRNAHLRV 590
Cdd:cd05750    82 GKDTVTGNVTV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 423-496 2.68e-05

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.50  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  423 VVLACET-------SGAPRPAITWQKGERILA-SGSVQLPrfTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASADL 494
Cdd:cd05748     3 VVRAGESlrldipiKGRPTPTVTWSKDGQPLKeTGRVQIE--TTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80


                  ..
gi 568973811  495 VV 496
Cdd:cd05748    81 KV 82
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 29-113 2.71e-05

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 44.78  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   29 PPYFKTEPVRTqVHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYMIT--SL----------DRTHAGFYRCI 96
Cdd:cd05722     1 ELYFLSEPSDI-VAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDERRQQLPngSLlitsvvhskhNKPDEGFYQCV 79

                          90
                  ....*....|....*...
gi 568973811   97 VRN-RMGALLQRQTEVQV 113
Cdd:cd05722    80 AQNeSLGSIVSRTARVTV 97
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 997-1084 2.83e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 2.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    997 PGAPTNLGISNIGPRSVTLQFRPGYDGktSISRWVVEAQVGVIGEGEEWLliyQLGNEPDARSMEVPDLNPFTYYSFRMR 1076
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDD--GITGYIVGYRVEYREEGSEWK---EVNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ....*...
gi 568973811   1077 QVNIVGTS 1084
Cdd:smart00060   76 AVNGAGEG 83
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 312-401 2.97e-05

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 44.60  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREP-ERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGklTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAA 390
Cdd:cd05852     1 PTFEFNPmKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTELLVNN--SRISIWDDGSLEILNITKLDEGSYTCFAENNR 78

                          90
                  ....*....|.
gi 568973811  391 GEAQTSTYLAV 401
Cdd:cd05852    79 GKANSTGVLSV 89
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 30-115 3.08e-05

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 44.54  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   30 PYFKTEPVRT---QVHLEGnRLVLTCMAEGSWPLEFKWLHNNRELtRFSLEYRY-------MITSLDRTH-AGFYRCIVR 98
Cdd:cd04967     2 PVFEEQPDDTifpEDSDEK-KVALNCRARANPVPSYRWLMNGTEI-DLESDYRYslvdgtlVISNPSKAKdAGHYQCLAT 79

                          90
                  ....*....|....*..
gi 568973811   99 NRMGALLQRQTEVQVAY 115
Cdd:cd04967    80 NTVGSVLSREATLQFGY 96
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 416-486 3.42e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 43.94  E-value: 3.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811  416 TVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFtlleSGSLLISPTHISDAGTYTCLATNSRG 486
Cdd:cd05731     6 MVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENF----NKTLKIENVSEADSGEYQCTASNTMG 72
I-set pfam07679
Immunoglobulin I-set domain;
30-114 3.49e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.17  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    30 PYFKTEPVRTQVHlEGNRLVLTCMAEGSWPLEFKWLHNNRELT---RFSL-----EYRYMITSLDRTHAGFYRCIVRNRM 101
Cdd:pfam07679    1 PKFTQKPKDVEVQ-EGESARFTCTVTGTPDPEVSWFKDGQPLRssdRFKVtyeggTYTLTISNVQPDDSGKYTCVATNSA 79

                           90
                   ....*....|...
gi 568973811   102 GallQRQTEVQVA 114
Cdd:pfam07679   80 G---EAEASAELT 89
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 334-393 3.52e-05

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 44.46  E-value: 3.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  334 CRAKGVPPPSITWYKDAALVEVGKLTRFKQR---SDGGLQISGLLPD-----DTGMLQCFAHNAAGEA 393
Cdd:cd07693    22 CKAEGRPTPTIQWLKNGQPLETDKDDPRSHRivlPSGSLFFLRVVHGrkgrsDEGVYVCVAHNSLGEA 89
I-set pfam07679
Immunoglobulin I-set domain;
226-290 3.53e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.17  E-value: 3.53e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973811   226 KNTSVVAGTSeVTMECVANARPliKLHIVWKKDGAPLSSG------ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:pfam07679    8 KDVEVQEGES-ARFTCTVTGTP--DPEVSWFKDGQPLRSSdrfkvtYEGGTYTLTISNVQPDDSGKYTCVA 75
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 414-496 3.65e-05

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 44.24  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  414 DSTVIDGMSVVLACETSGAPRPAITWQK-GERILASGSVQLprftlleSGSLL-ISPTHISDAGTYTCLATNSRGVDEAS 491
Cdd:cd05851    10 DTYALKGQNVTLECFALGNPVPVIRWRKiLEPMPATAEISM-------SGAVLkIFNIQPEDEGTYECEAENIKGKDKHQ 82


                  ....*
gi 568973811  492 ADLVV 496
Cdd:cd05851    83 ARVYV 87
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 332-401 3.81e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 44.24  E-value: 3.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973811  332 IPCRAKGVPPPSITWYKDAALVE--VGKLTRFKQRSDgGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd20949    19 ILCEVKGEPQPNVTWHFNGQPISasVADMSKYRILAD-GLLINKVTQDDTGEYTCRAYQVNSIASDMQERTV 89
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
 504-590 4.10e-05

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 44.21  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  504 KPPQDQSVIKGTQASMVCGVTHDpRVTVRYVWEKDGATLAVETNP---RIRLDRNGS-LHISQTWSGDIGTYTCRVLSAG 579
Cdd:cd05895     4 KEMKSQEVAAGSKLVLRCETSSE-YPSLRFKWFKNGKEINRKNKPeniKIQKKKKKSeLRINKASLADSGEYMCKVSSKL 82

                          90
                  ....*....|.
gi 568973811  580 GNDSRNAHLRV 590
Cdd:cd05895    83 GNDSASANVTI 93
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 126-193 5.04e-05

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 5.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811  126 QSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITL------ENTLVILSTVAPDAGRYYVQAVNDK 193
Cdd:cd20951    10 HTVWEKSDAKLRV-EVQGKPDPEVKWYKNGVPIDPSSIPGKYKieseygVHVLHIRRVTVEDSAVYSAVAKNIH 82
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 506-590 5.13e-05

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 44.18  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  506 PQDQSVIKGTQASMVCGVTHDPRVTVryVWEKDGATLAV------ETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAG 579
Cdd:cd05726     6 PRDQVVALGRTVTFQCETKGNPQPAI--FWQKEGSQNLLfpyqppQPSSRFSVSPTGDLTITNVQRSDVGYYICQALNVA 83

                          90
                  ....*....|.
gi 568973811  580 GNDSRNAHLRV 590
Cdd:cd05726    84 GSILAKAQLEV 94
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 502-590 5.94e-05

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 43.62  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVRYVWEKDGAtlaVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGGN 581
Cdd:cd05764     3 ITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKL---ISNSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGE 79


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd05764    80 ATARVELHI 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 124-207 6.12e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.65  E-value: 6.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811    124 KRQSVNHGEAAVIRaPRISSFPRPQVTWFRDG-RKIPPSSRIAITLEN---TLVILSTVAPDAGRYYVQAvndKNGDNKT 199
Cdd:smart00410    2 PSVTVKEGESVTLS-CEASGSPPPEVTWYKQGgKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAA---TNSSGSA 77


                    ....*...
gi 568973811    200 SQPITLAV 207
Cdd:smart00410   78 SSGTTLTV 85
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 409-496 6.40e-05

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 43.73  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  409 TRGPLDSTVIDGMSVVLACETSGAPRPAITWQ-KGERILASGSVQLPRftlLESGSLLISPTHISDAGTYTCLATNSRGV 487
Cdd:cd05867     3 TRRPQSHLYGPGETARLDCQVEGIPTPNITWSiNGAPIEGTDPDPRRH---VSSGALILTDVQPSDTAVYQCEARNRHGN 79


                  ....*....
gi 568973811  488 DEASADLVV 496
Cdd:cd05867    80 LLANAHVHV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 321-399 6.81e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 43.29  E-value: 6.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  321 HITAEMEKVVDIPCRAKGVPPPSITWYKDAAlvEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYL 399
Cdd:cd20957    10 VQTVDFGRTAVFNCSVTGNPIHTVLWMKDGK--PLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 144-191 7.41e-05

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.22  E-value: 7.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568973811  144 FPRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVN 191
Cdd:cd04969    29 SPKPTISWSKGTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVN 76
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 140-192 8.20e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.33  E-value: 8.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  140 RISSFPRPQVTWFRDGRKIPPSSRIAITLE---NTLVILSTVAP-DAGRYYVQAVND 192
Cdd:cd20973    20 KVEGYPDPEVKWMKDDNPIVESRRFQIDQDedgLCSLIISDVCGdDSGKYTCKAVNS 76
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 412-494 8.24e-05

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 42.93  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACET-SGAPRPAITWQKGERILASGSVQLprftlleSGSLLISPTHISDAGTYTCLATNSRGVDEA 490
Cdd:cd05754     8 PRSQEVRPGADVSFICRAkSKSPAYTLVWTRVNGTLPSRAMDF-------NGILTIRNVQLSDAGTYVCTGSNMLDTDEA 80


                  ....
gi 568973811  491 SADL 494
Cdd:cd05754    81 TATL 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 30-113 8.36e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.15  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   30 PYFKTEPVRTQVHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRY-----MITSLDRTHAGFYRCIVRNRMGAl 104
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVedgtlTIINVQPEDTGYYGCVATNEIGD- 79


                  ....*....
gi 568973811  105 LQRQTEVQV 113
Cdd:cd20978    80 IYTETLLHV 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 504-590 8.81e-05

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 42.94  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  504 KPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVetNPRIRLDRNGSLHISQ-TWSGDIGTYTCRVLSAGGN- 581
Cdd:cd20958     5 RPMGNLTAVAGQTLRLHCPVAGYPISSIT--WEKDGRRLPL--NHRQRVFPNGTLVIENvQRSSDEGEYTCTARNQQGQs 80


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd20958    81 ASRSVFVKV 89
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 423-486 9.17e-05

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 43.39  E-value: 9.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  423 VVLACETSGAPRPAITWQK--GERILASGSvqlpRFTLLeSGSLLIS-PTHISDAGTYTCLATNSRG 486
Cdd:cd04967    22 VALNCRARANPVPSYRWLMngTEIDLESDY----RYSLV-DGTLVISnPSKAKDAGHYQCLATNTVG 83
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 416-491 9.76e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 42.90  E-value: 9.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811  416 TVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEAS 491
Cdd:cd05894     6 VVVAGNKLRLDVPISGEPAPTVTWSRGDKAFTATEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 502-591 9.91e-05

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 43.08  E-value: 9.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVryVWEKDgaTLAVET---NPRIRLDRNGSLHISQTWSGDIGTYTCRVL-S 577
Cdd:cd05738     2 IDMGPQLKVVEKARTATMLCAASGNPDPEI--SWFKD--FLPVDTatsNGRIKQLRSGALQIENSEESDQGKYECVATnS 77

                          90
                  ....*....|....
gi 568973811  578 AGGNDSRNAHLRVR 591
Cdd:cd05738    78 AGTRYSAPANLYVR 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 128-207 1.04e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 42.88  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  128 VNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLEN--TLVILSTVAPDAGRYYVQAVNDKNGDnkTSQPITL 205
Cdd:cd20970    14 AREGENATFMC-RAEGSPEPEISWTRNGNLIIEFNTRYIVRENgtTLTIRNIRRSDMGIYLCIASNGVPGS--VEKRITL 90


                  ..
gi 568973811  206 AV 207
Cdd:cd20970    91 QV 92
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 311-401 1.08e-04

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 43.25  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  311 PPQFVREPERHiTAEMEKVVDIPCRAKGVPPPSITW-YKDAALVE-----VGKLTRFKQRSDGGLQISGLLPDDTGMLQC 384
Cdd:cd05734     1 PPRFVVQPNDQ-DGIYGKAVVLNCSADGYPPPTIVWkHSKGSGVPqfqhiVPLNGRIQLLSNGSLLIKHVLEEDSGYYLC 79

                          90
                  ....*....|....*...
gi 568973811  385 FAHNAAG-EAQTSTYLAV 401
Cdd:cd05734    80 KVSNDVGaDISKSMYLTV 97
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 412-494 1.47e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 42.52  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  412 PLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSvqlpRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEAS 491
Cdd:cd20957     8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSS----RVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQAT 83


                  ...
gi 568973811  492 ADL 494
Cdd:cd20957    84 AEL 86
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 312-391 1.53e-04

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 42.62  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPERHI--TAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKLTRFkQRSDGGLQISGllPD---DTGMLQCFA 386
Cdd:cd05848     2 PVFVQEPDDAIfpTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDTESDYRY-SLIDGNLIISN--PSevkDSGRYQCLA 78


                  ....*
gi 568973811  387 HNAAG 391
Cdd:cd05848    79 TNSIG 83
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 312-401 2.02e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.39  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  312 PQFVREPErHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDG--GLQISGLLPDDTGMLQCFAHNA 389
Cdd:cd20990     1 PHFLQAPG-DLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGvhSLIIEPVTSRDAGIYTCIATNR 79

                          90
                  ....*....|..
gi 568973811  390 AGEAQTSTYLAV 401
Cdd:cd20990    80 AGQNSFNLELVV 91
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
 316-396 2.12e-04

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409458  Cd Length: 95  Bit Score: 42.28  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  316 REPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGG---LQISGLLPDDT--GMLQCFAHNAA 390
Cdd:cd05874     6 QSPKDYIVDPRENIV-IQCEAKGKPPPSFSWTRNGTHFDIDKDPKVTMKPNTGtlvINIMNGEKAEAyeGVYQCTARNER 84


                  ....*.
gi 568973811  391 GEAQTS 396
Cdd:cd05874    85 GAAVSN 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 504-584 2.13e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.80  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   504 KPPQDQSVIKGTQASMVCGVTHDPRVTVrYVWEKDGATL--AVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGGN 581
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTGSPGPD-VTWSKEGGTLieSLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79


                   ...
gi 568973811   582 DSR 584
Cdd:pfam00047   80 ATL 82
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 501-573 2.14e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 41.84  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568973811  501 RITKPPQDQSVIKGTQASMVCGVTHDPRVTVRYVWEKDgatlAVETNPRIRLDRNGSLHISQTWSGDIGTYTC 573
Cdd:cd20968     1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDD----LIKENNRIAVLESGSLRIHNVQKEDAGQYRC 69
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 330-398 2.15e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 42.15  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  330 VDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKqRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQtSTY 398
Cdd:cd05856    22 VRLKCVASGNPRPDITWLKDNKPLTPPEIGENK-KKKWTLSLKNLKPEDSGKYTCHVSNRAGEIN-ATY 88
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 145-192 2.37e-04

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 42.16  E-value: 2.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811  145 PRPQVTWFRDGRKIPPSSRIAI----TLENTLV----ILSTVAPDAGRYYVQAVND 192
Cdd:cd20956    29 PLPQITWTLDGFPIPESPRFRVgdyvTSDGDVVsyvnISSVRVEDGGEYTCTATND 84
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 140-201 2.43e-04

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.80  E-value: 2.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811  140 RISSFPRPQVTWFRDGRKIPPSSRIAITLE---NTLVILSTVAPDAGRYYVQAVNDKNGDNKTSQ 201
Cdd:cd20972    24 RVTGNPTPVVRWFCEGKELQNSPDIQIHQEgdlHSLIIAEAFEEDTGRYSCLATNSVGSDTTSAE 88
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 237-308 2.51e-04

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 42.08  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  237 VTMECVANARPLIKlhIVWKKDGAPLSSGISDynRRLTIANPTV------------SDAGYYECEAMLRSS-SVapVTRG 303
Cdd:cd05722    19 VVLNCSAESDPPPK--IEWKKDGVLLNLVSDE--RRQQLPNGSLlitsvvhskhnkPDEGFYQCVAQNESLgSI--VSRT 92


                  ....*
gi 568973811  304 AYLSV 308
Cdd:cd05722    93 ARVTV 97
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 30-102 2.79e-04

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 41.71  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   30 PYFKTEPVRTQVhLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRY---------MITSLDRTHAGFYRCIVRNR 100
Cdd:cd05744     1 PHFLQAPGDLEV-QEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLvrengrhslIIEPVTKRDAGIYTCIARNR 79


                  ..
gi 568973811  101 MG 102
Cdd:cd05744    80 AG 81
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 39-113 2.94e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 41.72  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   39 TQVHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYM-------ITSLDRTHAGFYRCIVRNRMGALLQRQTEV 111
Cdd:cd20970    11 TVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRengttltIRNIRRSDMGIYLCIASNGVPGSVEKRITL 90


                  ..
gi 568973811  112 QV 113
Cdd:cd20970    91 QV 92
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 503-590 3.02e-04

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 41.69  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  503 TKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVETNPRIRLDRNGSLHI-----SQTWSGDIGTYTC--RV 575
Cdd:cd05722     5 LSEPSDIVAMRGGPVVLNCSAESDPPPKIE--WKKDGVLLNLVSDERRQQLPNGSLLItsvvhSKHNKPDEGFYQCvaQN 82

                          90
                  ....*....|....*
gi 568973811  576 LSAGGNDSRNAHLRV 590
Cdd:cd05722    83 ESLGSIVSRTARVTV 97
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
 33-102 3.18e-04

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.52  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   33 KTEPVRTQVHLEGNRLVLTCMAEGSWP-LEFKWLHNNRELTR--------------FSLEYRYMITSLDrthAGFYRCIV 97
Cdd:cd05895     2 KLKEMKSQEVAAGSKLVLRCETSSEYPsLRFKWFKNGKEINRknkpenikiqkkkkKSELRINKASLAD---SGEYMCKV 78


                  ....*
gi 568973811   98 RNRMG 102
Cdd:cd05895    79 SSKLG 83
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 405-496 3.39e-04

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 41.77  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  405 APNITRGPLDSTVIDGMSVVLACETSGAPRPAIT--WQ-KGERI-LASGSVQLPRFTLLES-GSLLISPTHISDAGTYTC 479
Cdd:cd04970     2 ATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSfNGVPIdLEKIEGHYRRRYGKDSnGDLEIVNAQLKHAGRYTC 81

                          90
                  ....*....|....*..
gi 568973811  480 LATNSRGVDEASADLVV 496
Cdd:cd04970    82 TAQTVVDSDSASATLVV 98
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 313-393 3.46e-04

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 41.46  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  313 QFVREPERHITAEMEKVVdIPCRAKGVPPPSITWYKDAALVEVGklTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGE 392
Cdd:cd20968     1 KITRPPTNVTIIEGLKAV-LPCTTMGNPKPSVSWIKGDDLIKEN--NRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGI 77


                  .
gi 568973811  393 A 393
Cdd:cd20968    78 A 78
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 417-496 3.55e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 41.62  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  417 VIDGMSVVLACETSGAPRPAITWQK-GERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASADLV 495
Cdd:cd05893    12 IFEGMPVTFTCRVAGNPKPKIYWFKdGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQGRISCTGRLM 91


                  .
gi 568973811  496 V 496
Cdd:cd05893    92 V 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 118-191 3.69e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 41.22  E-value: 3.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973811  118 SFEEG-EKRQSVNHGEAAVIRApRISSFPRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVN 191
Cdd:cd20978     2 KFIQKpEKNVVVKGGQDVTLPC-QVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATN 75
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
 500-594 4.36e-04

Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells (AC) in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 409440  Cd Length: 102  Bit Score: 41.57  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  500 TRITKPPQDQSVIKGTQASMVCGVTHDPRVTVRYVWEKDGATLAVEtNPRIRLDRN------GSLHISQTWSGDIGTYTC 573
Cdd:cd05854     3 TKITLAPSSADINQGENLTLQCHASHDPTMDLTFTWSLDDFPIDLD-KPNGHYRRMevketiGDLVIVNAQLSHAGTYTC 81

                          90       100
                  ....*....|....*....|.
gi 568973811  574 RVLSAGGNDSRNAHLRVRQLP 594
Cdd:cd05854    82 TAQTVVDSASASATLVVRGPP 102
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 311-391 5.12e-04

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 41.14  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  311 PPQFVREPERHITAEMEKVVdIPCRAKGVPPPSITW----------YKDAAlvevgKLTRFKQRSDGGLQISGLLPDDTG 380
Cdd:cd20954     1 PPRWIVEPVDANVAAGQDVM-LHCQADGFPTPTVTWkkatgstpgeYKDLL-----YDPNVRILPNGTLVFGHVQKENEG 74

                          90
                  ....*....|.
gi 568973811  381 MLQCFAHNAAG 391
Cdd:cd20954    75 HYLCEAKNGIG 85
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 420-496 5.47e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.05  E-value: 5.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  420 GMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASADLVV 496
Cdd:cd05729    19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 235-290 5.51e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 40.99  E-value: 5.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  235 SEVTMECVA--NARPLIKlhivWKK-DGAPLSS-GISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:cd04968    17 QTVTLECFAlgNPVPQIK----WRKvDGSPSSQwEITTSEPVLEIPNVQFEDEGTYECEA 72
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 310-401 6.35e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 40.51  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  310 EPPQFVREPERhiTAEMEkvvdipCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNA 389
Cdd:cd04978     5 EPPSLVLSPGE--TGELI------CEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNV 76

                          90
                  ....*....|..
gi 568973811  390 AGEAQTSTYLAV 401
Cdd:cd04978    77 HGYLLANAFLHV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 227-292 7.38e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 40.07  E-value: 7.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973811   227 NTSVVAGTSEVTMECVANARPLIKlhIVWKKDGAPLSSgisdyNRRLTIANPTVSDAGYYECEAML 292
Cdd:pfam13895    7 SPTVVTEGEPVTLTCSAPGNPPPS--YTWYKDGSAISS-----SPNFFTLSVSAEDSGTYTCVARN 65
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
 511-590 7.55e-04

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 40.30  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  511 VIKGTQASMVCGVThDPRVTVRyvWEKDGATLAVETnpRIRLDRNGS---LHISQTWSGDIGTYTCRVlsagGNDSRNAH 587
Cdd:cd20967     9 VSKGHKIRLTVELA-DPDAEVK--WYKDGQELQSSS--KVIFESIGAkrtLTVQQASLADAGEYQCVA----GGEKCSFE 79


                  ...
gi 568973811  588 LRV 590
Cdd:cd20967    80 LFV 82
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 423-486 9.18e-04

First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 40.68  E-value: 9.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  423 VVLACETSGAPRPAITWQKG--ERILASGSvqlpRFTLLeSGSLLIS-PTHISDAGTYTCLATNSRG 486
Cdd:cd05850    23 VTLACRARASPPATYRWKMNgtELKMEPDS----RYRLV-AGNLVISnPVKAKDAGSYQCLASNRRG 84
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 235-288 9.42e-04

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 40.23  E-value: 9.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568973811  235 SEVTMECVANARPlIKLHIVWKKDGAPLSSGISDYNRRLTIANPTVSDAGYYEC 288
Cdd:cd05754    17 ADVSFICRAKSKS-PAYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVC 69
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 409-496 1.07e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 40.12  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  409 TRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRftLLESGSLLISPTHISDAGTYTCLATNSRGVD 488
Cdd:cd04978     3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRR--TVDGRTLIFSNLQPNDTAVYQCNASNVHGYL 80


                  ....*...
gi 568973811  489 EASADLVV 496
Cdd:cd04978    81 LANAFLHV 88
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 506-582 1.09e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 40.32  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  506 PQDQSVIKGTQASMVCGVTH--DPRVTvryvWEKDGATLAVETNPRIRLDRNGS-LHISQTWSGDIGTYTCRVLSAGGND 582
Cdd:cd05736     7 PEFQAKEPGVEASLRCHAEGipLPRVQ----WLKNGMDINPKLSKQLTLIANGSeLHISNVRYEDTGAYTCIAKNEGGVD 82
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 319-395 1.15e-03

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 40.15  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  319 ERHIT---AEMEKVVDIPCRAKGVPPPSITWYKDAALV--EVGKLTRFKQRSDGGLQISGL-LPDDTGMLQCFAHNAAGE 392
Cdd:cd20971     5 KEELRnlnVRYQSNATLVCKVTGHPKPIVKWYRQGKEIiaDGLKYRIQEFKGGYHQLIIASvTDDDATVYQVRATNQGGS 84


                  ...
gi 568973811  393 AQT 395
Cdd:cd20971    85 VSG 87
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 145-191 1.23e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 39.47  E-value: 1.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568973811  145 PRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVN 191
Cdd:cd05746    11 PEPTITWNKDGVQVTESGKFHISPEGYLAIRDVGVADQGRYECVARN 57
IgI_2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 416-483 1.23e-03

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 409416  Cd Length: 98  Bit Score: 40.13  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  416 TVIDGMSVV---------LACETSGA-PRPAITWQK-GERILASGSVQlprfTLLESG-------SLLISPTHISDAGTY 477
Cdd:cd05759     2 PVIEGGPVIslqagvpynLTCRARGAkPAAEIIWFRdGEQLEGAVYSK----ELLKDGkrettvsTLLITPSDLDTGRTF 77


                  ....*.
gi 568973811  478 TCLATN 483
Cdd:cd05759    78 TCRARN 83
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 406-496 1.24e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 40.32  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGsvQLPRFTLLESGS-LLISPTHISDAGTYTCLATNS 484
Cdd:cd05762     2 PQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEG--EGIKIENTENSSkLTITEGQQEHCGCYTLEVENK 79

                          90
                  ....*....|..
gi 568973811  485 RGVDEASADLVV 496
Cdd:cd05762    80 LGSRQAQVNLTV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 416-496 1.62e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 39.80  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  416 TVIDGMSVVLACE-TSGAPRPAITWQK-GERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASAD 493
Cdd:cd05750    10 TVQEGSKLVLKCEaTSENPSPRYRWFKdGKELNRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89


                  ...
gi 568973811  494 LVV 496
Cdd:cd05750    90 VTV 92
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 30-115 1.70e-03

First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409436 [Multi-domain]  Cd Length: 95  Bit Score: 39.55  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   30 PYFKTEPVRT---QVHLEGnRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEY-----RYMITSLDRTH-AGFYRCIVRNR 100
Cdd:cd05849     2 PVFEEQPIDTiypEESTEG-KVSVNCRARANPFPIYKWRKNNLDIDLTNDRYsmvggNLVINNPDKYKdAGRYVCIVSNI 80

                          90
                  ....*....|....*
gi 568973811  101 MGALLQRQTEVQVAY 115
Cdd:cd05849    81 YGKVRSREATLSFGY 95
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 503-590 1.77e-03

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 39.40  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  503 TKPPQDQSVIKGTQASMVCGVTHDPrvTVRYVWEKDGATLAVETNPRIRLDRNG--SLHISQTWSGDIGTYTCRVLSAGG 580
Cdd:cd05744     4 LQAPGDLEVQEGRLCRFDCKVSGLP--TPDLFWQLNGKPVRPDSAHKMLVRENGrhSLIIEPVTKRDAGIYTCIARNRAG 81

                          90
                  ....*....|
gi 568973811  581 NDSRNAHLRV 590
Cdd:cd05744    82 ENSFNAELVV 91
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
 227-290 1.84e-03

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 39.30  E-value: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811  227 NTSVVAGTSEVTMECVANArplIKLHIVWKKDGAPLSSG----ISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:cd05740     8 NSNPVEDKDAVTLTCEPET---QNTSYLWWFNGQSLPVTprltLSNGNRTLTLLNVTREDAGAYQCEI 72
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 406-496 2.00e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 39.38  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  406 PNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTllESG--SLLISPTHISDAGTYTCLATN 483
Cdd:cd20975     1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEA--EGGlcRLRILAAERGDAGFYTCKAVN 78

                          90
                  ....*....|...
gi 568973811  484 SRGVDEASADLVV 496
Cdd:cd20975    79 EYGARQCEARLEV 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 140-207 2.13e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 38.92  E-value: 2.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811   140 RISSFPRPQVTWFRDGRKIPPSSRiaitlentLVILSTVAPDAGRYYVQAVNDKNGdnKTSQPITLAV 207
Cdd:pfam13895   22 SAPGNPPPSYTWYKDGSAISSSPN--------FFTLSVSAEDSGTYTCVARNGRGG--KVSNPVELTV 79
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 30-115 2.15e-03

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 39.54  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   30 PYFKTEP--VRTQVHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSlEYRYMI--------TSLDRTHAGFYRCIVRN 99
Cdd:cd05848     2 PVFVQEPddAIFPTDSDEKKVILNCEARGNPVPTYRWLRNGTEIDTES-DYRYSLidgnliisNPSEVKDSGRYQCLATN 80

                          90
                  ....*....|....*.
gi 568973811  100 RMGALLQRQTEVQVAY 115
Cdd:cd05848    81 SIGSILSREALLQFAY 96
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 499-590 2.20e-03

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 39.30  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  499 RTRITKPPQDQ-SVIKGTQASMVCGVTHDPRVTVRYVWEKDgATLAVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLS 577
Cdd:cd20969     1 RAAIRDRKAQQvFVDEGHTVQFVCRADGDPPPAILWLSPRK-HLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN 79

                          90
                  ....*....|...
gi 568973811  578 AGGNDSRNAHLRV 590
Cdd:cd20969    80 AGGNDSMPAHLHV 92
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 140-191 2.63e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 38.92  E-value: 2.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  140 RISSFPRPQVTWFRDGRKIPPSS---RIAITLENTLVILSTVAP--DAGRYYVQAVN 191
Cdd:cd05893    23 RVAGNPKPKIYWFKDGKQISPKSdhyTIQRDLDGTCSLHTTASTldDDGNYTIMAAN 79
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 506-587 2.84e-03

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 39.01  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  506 PQDQSVIKGTQASMVCGVTHDPRVTVryVWE-KDGA-----TLAVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAG 579
Cdd:cd05734     8 PNDQDGIYGKAVVLNCSADGYPPPTI--VWKhSKGSgvpqfQHIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCKVSNDV 85


                  ....*...
gi 568973811  580 GNDSRNAH 587
Cdd:cd05734    86 GADISKSM 93
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 35-113 2.94e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 38.53  E-value: 2.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811    35 EPVRTQVHlEGNRLVLTCMAEGSWPLEFKWLHNNRELtrfSLEYRYMITSLDRTHAGFYRCIVRNRMGALLQRQTEVQV 113
Cdd:pfam13895    5 TPSPTVVT-EGEPVTLTCSAPGNPPPSYTWYKDGSAI---SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVELTV 79
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 226-290 3.09e-03

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 38.85  E-value: 3.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  226 KNTSVVAGTSeVTMECVANARPLIKlhIVWKK--DGAPLSSGISDYNRRLTIANPTVSDAGYYECEA 290
Cdd:cd05851     9 KDTYALKGQN-VTLECFALGNPVPV--IRWRKilEPMPATAEISMSGAVLKIFNIQPEDEGTYECEA 72
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 334-401 3.37e-03

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 38.61  E-value: 3.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  334 CRAKGVPPPSITW-YKDAALVevGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAV 401
Cdd:cd05764    22 CKARGDPEPAIHWiSPEGKLI--SNSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGEATARVELHI 88
IgC1_hNephrin_like cd05773
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ...
 405-499 3.52e-03

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.


Pssm-ID: 143250  Cd Length: 109  Bit Score: 39.14  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  405 APNITRGPLDSTVI---DGMSVV-LACETSGAPRPAITWQKGERILasgSVQLPRFT--LLESGSLLISPTHIS------ 472
Cdd:cd05773     4 APDLQKGPQLRKVAsrgDGSSDAnLVCQAQGVPRVQFRWAKNGVPL---DLGNPRYEetTEHTGTVHTSILTIInvsaal 80

                          90       100
                  ....*....|....*....|....*..
gi 568973811  473 DAGTYTCLATNSRGVDEASADLVVWAR 499
Cdd:cd05773    81 DYALFTCTAHNSLGEDSLDIQLVSTSR 107
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 415-486 3.67e-03

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 38.70  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  415 STVIDGMSVVLACETSGAPRPAITWQKGERILASGsvqlPRFTL----LESGSLL----ISPTHISDAGTYTCLATNSRG 486
Cdd:cd20956    11 QTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPES----PRFRVgdyvTSDGDVVsyvnISSVRVEDGGEYTCTATNDVG 86
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 330-396 4.00e-03

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 38.76  E-value: 4.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973811  330 VDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTS 396
Cdd:cd05760    19 VTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAFGSVCSS 85
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 45-102 4.07e-03

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 38.63  E-value: 4.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973811   45 GNRLVLTCMAE-GSWPLEFKWLHNNRELT-----RFSLEYRY----MITSLDRTHAGFYRCIVRNRMG 102
Cdd:cd20959    17 GMRAQLHCGVPgGDLPLNIRWTLDGQPISddlgiTVSRLGRRssilSIDSLEASHAGNYTCHARNSAG 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 226-290 4.16e-03

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 38.21  E-value: 4.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973811  226 KNTSVVAGTSEVTMECVANARPliKLHIVWKKDGAPLSSG----ISDyNRRLTIANPTVSDAGYYECEA 290
Cdd:cd04969     9 KKKILAAKGGDVIIECKPKASP--KPTISWSKGTELLTNSsricILP-DGSLKIKNVTKSDEGKYTCFA 74
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 506-573 5.07e-03

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 38.45  E-value: 5.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568973811  506 PQDQSVIKGTQASMVCGVTHDPRVTVryVWEKD-GATLA----VETNPRIRLDRNGSLHISQTWSGDIGTYTC 573
Cdd:cd20954     8 PVDANVAAGQDVMLHCQADGFPTPTV--TWKKAtGSTPGeykdLLYDPNVRILPNGTLVFGHVQKENEGHYLC 78
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 505-573 5.38e-03

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 37.92  E-value: 5.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  505 PPQDQSVIKGTQASMVC-GVTHDPRVTVryVWEKDGATLavetnPRIRLDRNGSLHISQTWSGDIGTYTC 573
Cdd:cd05754     7 EPRSQEVRPGADVSFICrAKSKSPAYTL--VWTRVNGTL-----PSRAMDFNGILTIRNVQLSDAGTYVC 69
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 502-591 5.46e-03

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 38.17  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVETNPRI-RLDRNG---SLHISQTWSGDIGTYTCRVLS 577
Cdd:cd20951     3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVK--WYKNGVPIDPSSIPGKyKIESEYgvhVLHIRRVTVEDSAVYSAVAKN 80

                          90
                  ....*....|....
gi 568973811  578 AGGNDSRNAHLRVR 591
Cdd:cd20951    81 IHGEASSSASVVVE 94
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 41-104 5.58e-03

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 37.48  E-value: 5.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811   41 VHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTrfsLEYRYMITSLDRTHAGFYRCIVRNRMGAL 104
Cdd:cd20948     6 YYLSGENLNLSCHAASNPPAQYSWTINGTFQT---SSQELFLPAITENNEGTYTCSAHNSLTGK 66
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 411-494 5.76e-03

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409363  Cd Length: 102  Bit Score: 38.17  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  411 GPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILAS--GSVQLPRFTLLESGS---------LLISPTHISDAGTYTC 479
Cdd:cd04974     7 LPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSkyGPDGLPYVTVLKVAGvnttgeentLTISNVTFDDAGEYIC 86

                          90
                  ....*....|....*
gi 568973811  480 LATNSRGVDEASADL 494
Cdd:cd04974    87 LAGNSIGLSFHSAWL 101
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 411-496 6.11e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 38.59  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   411 GPLDSTVIDGMSVVLACE---TSGAPRPAITWQKGERILASGSVQL------------PRFTLLES-----GSLLISPTH 470
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTyssSMSEASTSVYWYRQPPGKGPTFLIAyysngseegvkkGRFSGRGDpsngdGSLTIQNLT 81

                           90       100
                   ....*....|....*....|....*..
gi 568973811   471 ISDAGTYTC-LATNSRGVDEASADLVV 496
Cdd:pfam07686   82 LSDSGTYTCaVIPSGEGVFGKGTRLTV 108
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 45-99 6.24e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 37.90  E-value: 6.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811   45 GNRLVLTCMAEGSWPLEFKWLHNNRELTRFS-----LEYRYMITSLDRTHAGFYRCIVRN 99
Cdd:cd20957    16 GRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSrvqilSEDVLVIPSVKREDKGMYQCFVRN 75
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 501-591 6.84e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 37.81  E-value: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  501 RITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGG 580
Cdd:cd04978     1 YWIIEPPSLVLSPGETGELICEAEGNPQPTIT--WRLNGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 78

                          90
                  ....*....|.
gi 568973811  581 NDSRNAHLRVR 591
Cdd:cd04978    79 YLLANAFLHVL 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 227-308 6.89e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 37.86  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  227 NTSVVAGtSEVTMECVANARPLIKlhIVWKKDGAPLSSGISDY----NRRLTIANPTVSDAGYYECEAmlrSSSVAPVTR 302
Cdd:cd20952     8 NQTVAVG-GTVVLNCQATGEPVPT--ISWLKDGVPLLGKDERIttleNGSLQIKGAEKSDTGEYTCVA---LNLSGEATW 81


                  ....*.
gi 568973811  303 GAYLSV 308
Cdd:cd20952    82 SAVLDV 87
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 131-191 6.94e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 37.77  E-value: 6.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973811  131 GEAAVIR--APRisSFPRPQVTWFRDGRKIP-PSSRIAITLENTLVILSTVAPDAGRYYVQAVN 191
Cdd:cd05724    12 GEMAVLEcsPPR--GHPEPTVSWRKDGQPLNlDNERVRIVDDGNLLIAEARKSDEGTYKCVATN 73
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 502-590 7.01e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 37.76  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  502 ITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAvETNPRIRLDRNGsLHISQTWSGDIGTYTCRVLSAGGN 581
Cdd:cd20978     4 IQKPEKNVVVKGGQDVTLPCQVTGVPQPKIT--WLHNGKPLQ-GPMERATVEDGT-LTIINVQPEDTGYYGCVATNEIGD 79


                  ....*....
gi 568973811  582 DSRNAHLRV 590
Cdd:cd20978    80 IYTETLLHV 88
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 501-590 7.41e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 37.92  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  501 RITKPPQDQSVIKGTQASMVCGVTHDPRVTVRyvWEKDGATLAVETNP----RIRLDrNGSLHISQTWSG-----DIGTY 571
Cdd:cd07693     2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQ--WLKNGQPLETDKDDprshRIVLP-SGSLFFLRVVHGrkgrsDEGVY 78

                          90       100
                  ....*....|....*....|
gi 568973811  572 TCRVLSAGGND-SRNAHLRV 590
Cdd:cd07693    79 VCVAHNSLGEAvSRNASLEV 98
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 417-486 9.57e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 37.20  E-value: 9.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973811  417 VIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFtlleSGSLLISPTHISDAGTYTCLATNSRG 486
Cdd:cd05876     7 ALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNH----NKTLQLLNVGESDDGEYVCLAENSLG 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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