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Conserved domains on  [gi|17542472|ref|NP_499896|]
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Leucine-rich repeats and immunoglobulin-like domains protein sma-10 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-451 2.26e-31

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 127.74  E-value: 2.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  38 CSSLDLSEIPTTIPNNTRILLLSDNEIESIDKSRLKGFYFLQTLDISNNIIRHIDFEFFYNLPNLKILNIRKNRLARIPR 117
Cdd:COG4886  11 KLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 118 GSHELGHLEKLDLRSNlistvtsEELSYLAAVRSVDLSRNLISYLPKPTTSAKvNIEKLDLASNSITDIGTDhFSSFNTL 197
Cdd:COG4886  91 DLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLT-NLKELDLSNNQLTDLPEP-LGNLTNL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 198 VTLKLARNHITTLNQfSFSRLRKLESLDLTRNMIREVRfLAFNQLPSLQNVSLARNDVYRLDDGmFYACEGLKHLNLSTN 277
Cdd:COG4886 162 KSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 278 RVQAVTegWMFGLTSLEVLDLSYNQIQSfhISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKF 357
Cdd:COG4886 239 QLTDLP--ELGNLTNLEELDLSNNQLTD--LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 358 ALVGMSSLHKLDLSSNTLAVCVEDGAVLYNTSMPFLRSLRFTNNQLRVIPKRAFERFPALEELDLTDNPIATIHPEAFEP 437
Cdd:COG4886 315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394

                       410
                ....*....|....
gi 17542472 438 LELKRLVMNSSSIL 451
Cdd:COG4886 395 TTTAGVLLLTLALL 408
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 618-705 6.20e-24

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 cd05763:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 91  Bit Score: 96.53  E-value: 6.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 618 FTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQ-IPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQ 696
Cdd:cd05763   2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81


                ....*....
gi 17542472 697 TQASANLIV 705
Cdd:cd05763  82 ISANATLTV 90
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 506-612 1.00e-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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   506 KIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVmeNGQPrvlVQDSATFlsinRTAVVNGTfderelaaAELLLDNVA 585
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--DGQP---LRSSDRF----KVTYEGGT--------YTLTISNVQ 64

                          90       100
                  ....*....|....*....|....*..
gi 17542472   586 MTDNSEYQCVARNRFGSDfSTHVKLQV 612
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEA-EASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 719-788 5.59e-04

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: 39.80  E-value: 5.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542472    719 SPMLIKKRDALKIDCSCDLiSSRQRMVWKRQQQVILFLK---KAKFSDNDQILTLTQTTFSDSGEYSCELWVD 788
Cdd:smart00410   2 PSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-451 2.26e-31

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 127.74  E-value: 2.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  38 CSSLDLSEIPTTIPNNTRILLLSDNEIESIDKSRLKGFYFLQTLDISNNIIRHIDFEFFYNLPNLKILNIRKNRLARIPR 117
Cdd:COG4886  11 KLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 118 GSHELGHLEKLDLRSNlistvtsEELSYLAAVRSVDLSRNLISYLPKPTTSAKvNIEKLDLASNSITDIGTDhFSSFNTL 197
Cdd:COG4886  91 DLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLT-NLKELDLSNNQLTDLPEP-LGNLTNL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 198 VTLKLARNHITTLNQfSFSRLRKLESLDLTRNMIREVRfLAFNQLPSLQNVSLARNDVYRLDDGmFYACEGLKHLNLSTN 277
Cdd:COG4886 162 KSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 278 RVQAVTegWMFGLTSLEVLDLSYNQIQSfhISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKF 357
Cdd:COG4886 239 QLTDLP--ELGNLTNLEELDLSNNQLTD--LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 358 ALVGMSSLHKLDLSSNTLAVCVEDGAVLYNTSMPFLRSLRFTNNQLRVIPKRAFERFPALEELDLTDNPIATIHPEAFEP 437
Cdd:COG4886 315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394

                       410
                ....*....|....
gi 17542472 438 LELKRLVMNSSSIL 451
Cdd:COG4886 395 TTTAGVLLLTLALL 408
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 618-705 6.20e-24

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: 96.53  E-value: 6.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 618 FTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQ-IPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQ 696
Cdd:cd05763   2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81


                ....*....
gi 17542472 697 TQASANLIV 705
Cdd:cd05763  82 ISANATLTV 90
I-set pfam07679
Immunoglobulin I-set domain;
616-705 4.49e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.39  E-value: 4.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                          90
                  ....*....|
gi 17542472   696 QTQASANLIV 705
Cdd:pfam07679  81 EAEASAELTV 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 32-375 2.02e-15

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 81.05  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   32 VGNVVDCSSLDL------SEIPTTIPN--NTRILLLSDNEIE-SIDKSrLKGFYFLQTLDISNNIIRHIDFEFFYNLPNL 102
Cdd:PLN00113 232 IGGLTSLNHLDLvynnltGPIPSSLGNlkNLQYLFLYQNKLSgPIPPS-IFSLQKLISLDLSDNSLSGEIPELVIQLQNL 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  103 KILNIRKNRL-ARIPRGSHELGHLEKLDLRSNLISTVTSEELSYLAAVRSVDLSRN-LISYLPKPTTSAKvNIEKLDLAS 180
Cdd:PLN00113 311 EILHLFSNNFtGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNnLTGEIPEGLCSSG-NLFKLILFS 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  181 NSITDIGTDHFSSFNTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARNDVY-RLD 259
Cdd:PLN00113 390 NSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKFFgGLP 469

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  260 DgmFYACEGLKHLNLSTNRVQAVTEGWMFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLR 339
Cdd:PLN00113 470 D--SFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMP 547

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 17542472  340 QLEELILSANSIDSLHKFALVGMSSLHKLDLSSNTL 375
Cdd:PLN00113 548 VLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHL 583
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 172-354 9.46e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 74.05  E-value: 9.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 172 NIEKLDLASNSITDIgtDHFSSFNTLVTLKLARNHITTLNqfSFSRLRKLESLDLTRNMIREVRFLafNQLPSLQ----- 246
Cdd:cd21340  25 NLKVLYLYDNKITKI--ENLEFLTNLTHLYLQNNQIEKIE--NLENLVNLKKLYLGGNRISVVEGL--ENLTNLEelhie 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 247 NVSLARNDVYRLDDG-MFYACEGLKHLNLSTNRVQAVTEgwMFGLTSLEVLDLSYNQIQSFH-----ISSWshtPKLKWL 320
Cdd:cd21340  99 NQRLPPGEKLTFDPRsLAALSNSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEelldlLSSW---PSLREL 173

                       170       180       190
                ....*....|....*....|....*....|....
gi 17542472 321 SLHSNRIQSLPsgSFRvlrqlEELILSANSIDSL 354
Cdd:cd21340 174 DLTGNPVCKKP--KYR-----DKIILASKSLEVL 200
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 622-705 7.25e-14

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: 67.53  E-value: 7.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472    622 PEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEAR-RLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 17542472    701 ANLIV 705
Cdd:smart00410  81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
506-612 1.00e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   506 KIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVmeNGQPrvlVQDSATFlsinRTAVVNGTfderelaaAELLLDNVA 585
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--DGQP---LRSSDRF----KVTYEGGT--------YTLTISNVQ 64

                          90       100
                  ....*....|....*....|....*..
gi 17542472   586 MTDNSEYQCVARNRFGSDfSTHVKLQV 612
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEA-EASAELTV 90
LRR_8 pfam13855
Leucine rich repeat;
172-231 2.49e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 2.49e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   172 NIEKLDLASNSITDIGTDHFSSFNTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMI 231
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 511-607 3.53e-08

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: 52.27  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 511 PVEVSTLIGEKARFTCNVYGASPLSIEW--RVMENGQPrvLVQDSATFLSINRTAVVNGTFDERELaaaeLLLDNVAMTD 588
Cdd:cd05858   8 PANTSVVVGTDAEFVCKVYSDAQPHIQWlkHVEKNGSK--YGPDGLPYVEVLKTAGVNTTDKEIEV----LYLRNVTFED 81

                        90
                ....*....|....*....
gi 17542472 589 NSEYQCVARNRFGsdFSTH 607
Cdd:cd05858  82 AGEYTCLAGNSIG--ISHH 98
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 511-612 2.87e-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: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472    511 PVEVSTLIGEKARFTCNVYGASPLSIEWRvmeNGQPRVLVQDSatflsinRTAVVNGTFDerelaaAELLLDNVAMTDNS 590
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWY---KQGGKLLAESG-------RFSVSRSGST------STLTISNVTPEDSG 64

                           90       100
                   ....*....|....*....|..
gi 17542472    591 EYQCVARNRFGSDFSThVKLQV 612
Cdd:smart00410  65 TYTCAATNSSGSASSG-TTLTV 85
LRRNT smart00013
Leucine rich repeat N-terminal domain;
29-54 1.68e-05

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 42.30  E-value: 1.68e-05
                           10        20
                   ....*....|....*....|....*.
gi 17542472     29 CHCVGNVVDCSSLDLSEIPTTIPNNT 54
Cdd:smart00013   6 CNCSGTAVDCSGRGLTEVPLDLPPDT 31
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 719-788 5.59e-04

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: 39.80  E-value: 5.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542472    719 SPMLIKKRDALKIDCSCDLiSSRQRMVWKRQQQVILFLK---KAKFSDNDQILTLTQTTFSDSGEYSCELWVD 788
Cdd:smart00410   2 PSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 722-786 2.48e-03

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: 37.94  E-value: 2.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472   722 LIKKRDALKIDCSCDLISSRQRMVWKRQQQVILFLKKAKFSDNDQI---LTLTQTTFSDSGEYSCELW 786
Cdd:pfam00047   7 TVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTqssLLISNVTKEDAGTYTCVVN 74
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-451 2.26e-31

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 127.74  E-value: 2.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  38 CSSLDLSEIPTTIPNNTRILLLSDNEIESIDKSRLKGFYFLQTLDISNNIIRHIDFEFFYNLPNLKILNIRKNRLARIPR 117
Cdd:COG4886  11 KLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLT 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 118 GSHELGHLEKLDLRSNlistvtsEELSYLAAVRSVDLSRNLISYLPKPTTSAKvNIEKLDLASNSITDIGTDhFSSFNTL 197
Cdd:COG4886  91 DLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLT-NLKELDLSNNQLTDLPEP-LGNLTNL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 198 VTLKLARNHITTLNQfSFSRLRKLESLDLTRNMIREVRfLAFNQLPSLQNVSLARNDVYRLDDGmFYACEGLKHLNLSTN 277
Cdd:COG4886 162 KSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNN 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 278 RVQAVTegWMFGLTSLEVLDLSYNQIQSfhISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKF 357
Cdd:COG4886 239 QLTDLP--ELGNLTNLEELDLSNNQLTD--LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 358 ALVGMSSLHKLDLSSNTLAVCVEDGAVLYNTSMPFLRSLRFTNNQLRVIPKRAFERFPALEELDLTDNPIATIHPEAFEP 437
Cdd:COG4886 315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394

                       410
                ....*....|....
gi 17542472 438 LELKRLVMNSSSIL 451
Cdd:COG4886 395 TTTAGVLLLTLALL 408
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
32-254 4.36e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 111.95  E-value: 4.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  32 VGNVVDCSSLDLSEIPTTIP-NNTRILLLSDNEIESIDKSrLKGFYFLQTLDISNNIIRHIDFEFFyNLPNLKILNIRKN 110
Cdd:COG4886  92 LGDLTNLTELDLSGNEELSNlTNLESLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNN 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 111 RLARIPRGSHELGHLEKLDLRSNLISTVtSEELSYLAAVRSVDLSRNLISYLPKPTTSAKvNIEKLDLASNSITDIgtDH 190
Cdd:COG4886 170 QLTDLPEELGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDLPEPLANLT-NLETLDLSNNQLTDL--PE 245

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542472 191 FSSFNTLVTLKLARNHITTLNqfSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARND 254
Cdd:COG4886 246 LGNLTNLEELDLSNNQLTDLP--PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 618-705 6.20e-24

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: 96.53  E-value: 6.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 618 FTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQ-IPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQ 696
Cdd:cd05763   2 FTKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81


                ....*....
gi 17542472 697 TQASANLIV 705
Cdd:cd05763  82 ISANATLTV 90
I-set pfam07679
Immunoglobulin I-set domain;
616-705 4.49e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 85.39  E-value: 4.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                          90
                  ....*....|
gi 17542472   696 QTQASANLIV 705
Cdd:pfam07679  81 EAEASAELTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 616-705 2.22e-16

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: 74.84  E-value: 2.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDH-IYIMNVTKEDQGAYTCHATNVA 694
Cdd:cd05744   1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRA 80

                        90
                ....*....|.
gi 17542472 695 GQTQASANLIV 705
Cdd:cd05744  81 GENSFNAELVV 91
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 621-705 2.83e-16

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: 74.35  E-value: 2.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 621 TPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLyvtpnDDH-IYIMNVTKEDQGAYTCHATNVAGQTQA 699
Cdd:cd05725   3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEIL-----DDHsLKIRKVTAGDMGSYTCVAENMVGKIEA 77


                ....*.
gi 17542472 700 SANLIV 705
Cdd:cd05725  78 SATLTV 83
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 32-375 2.02e-15

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 81.05  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   32 VGNVVDCSSLDL------SEIPTTIPN--NTRILLLSDNEIE-SIDKSrLKGFYFLQTLDISNNIIRHIDFEFFYNLPNL 102
Cdd:PLN00113 232 IGGLTSLNHLDLvynnltGPIPSSLGNlkNLQYLFLYQNKLSgPIPPS-IFSLQKLISLDLSDNSLSGEIPELVIQLQNL 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  103 KILNIRKNRL-ARIPRGSHELGHLEKLDLRSNLISTVTSEELSYLAAVRSVDLSRN-LISYLPKPTTSAKvNIEKLDLAS 180
Cdd:PLN00113 311 EILHLFSNNFtGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNnLTGEIPEGLCSSG-NLFKLILFS 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  181 NSITDIGTDHFSSFNTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARNDVY-RLD 259
Cdd:PLN00113 390 NSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKFFgGLP 469

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  260 DgmFYACEGLKHLNLSTNRVQAVTEGWMFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLR 339
Cdd:PLN00113 470 D--SFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMP 547

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 17542472  340 QLEELILSANSIDSLHKFALVGMSSLHKLDLSSNTL 375
Cdd:PLN00113 548 VLSQLDLSQNQLSGEIPKNLGNVESLVQVNISHNHL 583
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 172-354 9.46e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 74.05  E-value: 9.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 172 NIEKLDLASNSITDIgtDHFSSFNTLVTLKLARNHITTLNqfSFSRLRKLESLDLTRNMIREVRFLafNQLPSLQ----- 246
Cdd:cd21340  25 NLKVLYLYDNKITKI--ENLEFLTNLTHLYLQNNQIEKIE--NLENLVNLKKLYLGGNRISVVEGL--ENLTNLEelhie 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 247 NVSLARNDVYRLDDG-MFYACEGLKHLNLSTNRVQAVTEgwMFGLTSLEVLDLSYNQIQSFH-----ISSWshtPKLKWL 320
Cdd:cd21340  99 NQRLPPGEKLTFDPRsLAALSNSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEelldlLSSW---PSLREL 173

                       170       180       190
                ....*....|....*....|....*....|....
gi 17542472 321 SLHSNRIQSLPsgSFRvlrqlEELILSANSIDSL 354
Cdd:cd21340 174 DLTGNPVCKKP--KYR-----DKIILASKSLEVL 200
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 616-692 1.73e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 69.13  E-value: 1.73e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542472   616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATN 692
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 616-705 1.74e-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: 69.34  E-value: 1.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPED-MPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYvtpNDDHIYIMNVTKEDQGAYTCHATNVA 694
Cdd:cd20978   1 PKFIQKPEKnVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATV---EDGTLTIINVQPEDTGYYGCVATNEI 77

                        90
                ....*....|.
gi 17542472 695 GQTQASANLIV 705
Cdd:cd20978  78 GDIYTETLLHV 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-425 2.03e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.58  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   52 NNTRI--LLLSDNEIESIDKSRLKGFYFLQTLDISNNIIR-HIDFEFFYNLPNLKILNIRKNRLA-RIPRGSheLGHLEK 127
Cdd:PLN00113  67 NSSRVvsIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNNFTgSIPRGS--IPNLET 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  128 LDLRSNLISTVTSEELSYLAAVRSVDLSRN-LISYLPkPTTSAKVNIEKLDLASNSITDIGTDHFSSFNTLVTLKLARNH 206
Cdd:PLN00113 145 LDLSNNMLSGEIPNDIGSFSSLKVLDLGGNvLVGKIP-NSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  207 ITTLNQFSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARNDVYRLDDGMFYACEGLKHLNLSTNRVQAVTEGW 286
Cdd:PLN00113 224 LSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPEL 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  287 MFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKFALVGMSSLH 366
Cdd:PLN00113 304 VIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLF 383

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  367 KLDLSSNTLavcveDGAVLYNTSM-PFLRSLRFTNNQLRVIPKRAFERFPALEELDLTDN 425
Cdd:PLN00113 384 KLILFSNSL-----EGEIPKSLGAcRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNN 438
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 615-705 2.65e-14

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: 69.13  E-value: 2.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 615 APKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRL--YVTPNDD---HIYIMNVTKEDQGAYTCH 689
Cdd:cd20956   1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdYVTSDGDvvsYVNISSVRVEDGGEYTCT 80

                        90
                ....*....|....*.
gi 17542472 690 ATNVAGQTQASANLIV 705
Cdd:cd20956  81 ATNDVGSVSHSARINV 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 622-705 7.25e-14

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: 67.53  E-value: 7.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472    622 PEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEAR-RLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 17542472    701 ANLIV 705
Cdd:smart00410  81 TTLTV 85
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 48-253 3.37e-13

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 69.81  E-value: 3.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  48 TTIPN-----NTRILLLSDNEIESIDKsrLKGFYFLQTLDISNNIIRHIdfEFFYNLPNLKILNIRKNRLARIprgshel 122
Cdd:cd21340  15 TKIDNlslckNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGNRISVV------- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 123 GHLEKLdlrSNListvtsEELsYLAAVRsvdlsrnlisyLPKPttsakvniEKLDLASNSITDIGtdhfssfNTLVTLKL 202
Cdd:cd21340  84 EGLENL---TNL------EEL-HIENQR-----------LPPG--------EKLTFDPRSLAALS-------NSLRVLNI 127

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542472 203 ARNHITTLNQFSFsrLRKLESLDLTRNMIREVR--FLAFNQLPSLQNVSLARN 253
Cdd:cd21340 128 SGNNIDSLEPLAP--LRNLEQLDASNNQISDLEelLDLLSSWPSLRELDLTGN 178
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
37-262 1.25e-12

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 70.73  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  37 DCSSLDLSEIPTTIPNNT--RILLLSDNEIESIDKSrLKGFYFLQTLDISNNIIRhiDFEFFYNLPNLKILNIRKNRLAR 114
Cdd:COG4886 188 DLSNNQITDLPEPLGNLTnlEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLT--DLPELGNLTNLEELDLSNNQLTD 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 115 IPrGSHELGHLEKLDLRSNLISTVTSEELSYLAAVRSVDLSRNLISYLPKPTTSAKVNIEKLDLASNSITDIGTDHFSSF 194
Cdd:COG4886 265 LP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALS 343

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472 195 NTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARNDVYRLDDGM 262
Cdd:COG4886 344 LSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 176-431 1.86e-12

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 67.50  E-value: 1.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 176 LDLASNSITDIgtDHFSSFNTLVTLKLARNHITTLNQFSFsrLRKLESLDLTRNMIREVRFLAfnqlpSLQNvslarndv 255
Cdd:cd21340   7 LYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEF--LTNLTHLYLQNNQIEKIENLE-----NLVN-------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 256 yrlddgmfyacegLKHLNLSTNRVqAVTEGwMFGLTSLEVLDLSYnqiqsfhisswshtpklkwlslhsnriQSLPSGsf 335
Cdd:cd21340  70 -------------LKKLYLGGNRI-SVVEG-LENLTNLEELHIEN---------------------------QRLPPG-- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 336 rvlrqlEELILSANSIDSLHKfalvgmsSLHKLDLSSNTLAvCVEDGAVLYNtsmpfLRSLRFTNNQLRVIP--KRAFER 413
Cdd:cd21340 106 ------EKLTFDPRSLAALSN-------SLRVLNISGNNID-SLEPLAPLRN-----LEQLDASNNQISDLEelLDLLSS 166

                       250
                ....*....|....*...
gi 17542472 414 FPALEELDLTDNPIATIH 431
Cdd:cd21340 167 WPSLRELDLTGNPVCKKP 184
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 616-705 2.82e-12

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: 63.58  E-value: 2.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMN-VTKEDQGAYTCHATNVA 694
Cdd:cd20990   1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEpVTSRDAGIYTCIATNRA 80

                        90
                ....*....|.
gi 17542472 695 GQTQASANLIV 705
Cdd:cd20990  81 GQNSFNLELVV 91
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 616-705 3.35e-12

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: 63.21  E-value: 3.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPF-PAAEARRLYVTPNDD-HIYIMN-VTKEDQGAYTCHATN 692
Cdd:cd20951   1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdPSSIPGKYKIESEYGvHVLHIRrVTVEDSAVYSAVAKN 80

                        90
                ....*....|...
gi 17542472 693 VAGQTQASANLIV 705
Cdd:cd20951  81 IHGEASSSASVVV 93
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 622-706 4.08e-12

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: 62.95  E-value: 4.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAATGTPRPEIKW-AFEQIPFPAAEARRlyvtpNDDHIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd04968   8 PADTYALKGQTVTLECFALGNPVPQIKWrKVDGSPSSQWEITT-----SEPVLEIPNVQFEDEGTYECEAENSRGKDTVQ 82


                ....*.
gi 17542472 701 ANLIVF 706
Cdd:cd04968  83 GRIIVQ 88
I-set pfam07679
Immunoglobulin I-set domain;
506-612 1.00e-11

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 61.89  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   506 KIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVmeNGQPrvlVQDSATFlsinRTAVVNGTfderelaaAELLLDNVA 585
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--DGQP---LRSSDRF----KVTYEGGT--------YTLTISNVQ 64

                          90       100
                  ....*....|....*....|....*..
gi 17542472   586 MTDNSEYQCVARNRFGSDfSTHVKLQV 612
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEA-EASAELTV 90
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 612-705 1.58e-11

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: 61.37  E-value: 1.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 612 VYQAPKftyTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDhIYIMNVTKEDQGAYTCHAT 691
Cdd:cd20970   2 VISTPQ---PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGTT-LTIRNIRRSDMGIYLCIAS 77

                        90
                ....*....|....*
gi 17542472 692 N-VAGQTQASANLIV 705
Cdd:cd20970  78 NgVPGSVEKRITLQV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 615-705 1.93e-11

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: 61.11  E-value: 1.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 615 APKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARrLYVTPNDDHIYIMNVTKEDQGAYTCHATNVA 694
Cdd:cd20976   1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADR-STCEAGVGELHIQDVLPEDHGTYTCLAKNAA 79

                        90
                ....*....|.
gi 17542472 695 GQTQASANLIV 705
Cdd:cd20976  80 GQVSCSAWVTV 90
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 619-703 2.17e-11

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: 60.62  E-value: 2.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 619 TYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVtpnDDHIYIMNVTKEDQGAYTCHATNVAGQTQ 698
Cdd:cd20957   5 TIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILS---EDVLVIPSVKREDKGMYQCFVRNDGDSAQ 81


                ....*
gi 17542472 699 ASANL 703
Cdd:cd20957  82 ATAEL 86
LRR_8 pfam13855
Leucine rich repeat;
172-231 2.49e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 2.49e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   172 NIEKLDLASNSITDIGTDHFSSFNTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMI 231
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
315-373 3.44e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.08  E-value: 3.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542472   315 PKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKFALVGMSSLHKLDLSSN 373
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
LRR_8 pfam13855
Leucine rich repeat;
243-303 5.13e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 58.69  E-value: 5.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542472   243 PSLQNVSLARNDVYRLDDGMFYACEGLKHLNLSTNRVQAVTEGWMFGLTSLEVLDLSYNQI 303
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 100-303 6.74e-11

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 64.68  E-value: 6.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 100 PNLKILNIRKNRLARIPRGSHELGH-------LEKLDLRSNLISTVTS---EELSYLAAVRSVDLSRNLISYLPKPT--- 166
Cdd:cd00116  51 PSLKELCLSLNETGRIPRGLQSLLQgltkgcgLQELDLSDNALGPDGCgvlESLLRSSSLQELKLNNNGLGDRGLRLlak 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 167 --TSAKVNIEKLDLASNSITDIGTDH----FSSFNTLVTLKLARNH-----ITTLNQfSFSRLRKLESLDLTRNMIRE-- 233
Cdd:cd00116 131 glKDLPPALEKLVLGRNRLEGASCEAlakaLRANRDLKELNLANNGigdagIRALAE-GLKANCNLEVLDLNNNGLTDeg 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 234 VRFLA--FNQLPSLQNVSLARN-----DVYRLDDGMFYACEGLKHLNLSTNR-----VQAVTEGwMFGLTSLEVLDLSYN 301
Cdd:cd00116 210 ASALAetLASLKSLEVLNLGDNnltdaGAAALASALLSPNISLLTLSLSCNDitddgAKDLAEV-LAEKESLLELDLRGN 288


                ..
gi 17542472 302 QI 303
Cdd:cd00116 289 KF 290
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 618-705 6.96e-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: 59.43  E-value: 6.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 618 FTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARrlYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQT 697
Cdd:cd20952   2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDER--ITTLENGSLQIKGAEKSDTGEYTCVALNLSGEA 79


                ....*...
gi 17542472 698 QASANLIV 705
Cdd:cd20952  80 TWSAVLDV 87
LRR_8 pfam13855
Leucine rich repeat;
268-327 1.36e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.53  E-value: 1.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   268 GLKHLNLSTNRVQAVTEGWMFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRI 327
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 617-705 1.57e-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: 58.81  E-value: 1.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 617 KFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFE---QIPFPAAEAR---RLYVTPNDDhIYIMNVTKEDQGAYTCHA 690
Cdd:cd05726   1 QFVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEgsqNLLFPYQPPQpssRFSVSPTGD-LTITNVQRSDVGYYICQA 79

                        90
                ....*....|....*
gi 17542472 691 TNVAGQTQASANLIV 705
Cdd:cd05726  80 LNVAGSILAKAQLEV 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 633-700 1.75e-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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 57.72  E-value: 1.75e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472 633 AKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 615-705 2.67e-10

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: 57.86  E-value: 2.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 615 APKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEArrlYVTPNDD----HIYIMNVT-KEDQGAYTCH 689
Cdd:cd20971   1 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGL---KYRIQEFkggyHQLIIASVtDDDATVYQVR 77

                        90
                ....*....|....*.
gi 17542472 690 ATNVAGQTQASANLIV 705
Cdd:cd20971  78 ATNQGGSVSGTASLEV 93
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 172-412 4.73e-10

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 62.89  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 172 NIEKLDLASNSITDIGT----DHFSSFNTLVTLKLARNHITTLNQFSF----SRLRKLESLDLTRNMIREVRFLAFNQlp 243
Cdd:COG5238 181 SVETVYLGCNQIGDEGIeelaEALTQNTTVTTLWLKRNPIGDEGAEILaealKGNKSLTTLDLSNNQIGDEGVIALAE-- 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 244 slqnvSLARND-VYRLDDGMFY-ACEGLKHLN--LSTNrvqavtegwmfglTSLEVLDLSYNQIqSFH-----ISSWSHT 314
Cdd:COG5238 259 -----ALKNNTtVETLYLSGNQiGAEGAIALAkaLQGN-------------TTLTSLDLSVNRI-GDEgaialAEGLQGN 319

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 315 PKLKWLSLHSNRIQslPSG------SFRVLRQLEELILSANSI-----DSLHKFaLVGMSSLHKLDLSSNTLAvcvEDGA 383
Cdd:COG5238 320 KTLHTLNLAYNGIG--AQGaialakALQENTTLHSLDLSDNQIgdegaIALAKY-LEGNTTLRELNLGKNNIG---KQGA 393

                       250       260       270
                ....*....|....*....|....*....|.
gi 17542472 384 VLYNTSMPF--LRSLRFTNNQLRVIPKRAFE 412
Cdd:COG5238 394 EALIDALQTnrLHTLILDGNLIGAEAQQRLE 424
LRR_8 pfam13855
Leucine rich repeat;
78-135 4.77e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.99  E-value: 4.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542472    78 LQTLDISNNIIRHIDFEFFYNLPNLKILNIRKNRLARIPRGS-HELGHLEKLDLRSNLI 135
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 616-705 5.60e-10

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: 56.89  E-value: 5.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:cd05736   1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80

                        90
                ....*....|
gi 17542472 696 QTQASANLIV 705
Cdd:cd05736  81 VDEDISSLFV 90
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 624-705 8.56e-10

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: 56.04  E-value: 8.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 624 DMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFpaAEARRLYVTPNDDH---IYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd20973   6 DKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPI--VESRRFQIDQDEDGlcsLIISDVCGDDSGKYTCKAVNSLGEATCS 83


                ....*
gi 17542472 701 ANLIV 705
Cdd:cd20973  84 AELTV 88
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 622-706 1.08e-09

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: 55.92  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPF-PAAEARRLYVtpNDDHIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd04978   6 PPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIePAPEDMRRTV--DGRTLIFSNLQPNDTAVYQCNASNVHGYLLAN 83


                ....*.
gi 17542472 701 ANLIVF 706
Cdd:cd04978  84 AFLHVL 89
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 616-705 1.12e-09

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: 56.02  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAfEQIPfpaaEARRLYVTPNddHIY------------IMNVTKEDQ 683
Cdd:cd05765   1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWE-KQVP----GKENLIMRPN--HVRgnvvvtnigqlvIYNAQPQDA 73

                        90       100
                ....*....|....*....|..
gi 17542472 684 GAYTCHATNVAGQTQASANLIV 705
Cdd:cd05765  74 GLYTCTARNSGGLLRANFPLSV 95
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 617-695 1.40e-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: 1.40e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542472 617 KFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:cd20949   1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCRAYQVNS 79
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 631-705 1.41e-09

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: 55.79  E-value: 1.41e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542472 631 QTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAG-QTQASANLIV 705
Cdd:cd05738  15 RTATMLCAASGNPDPEISWFKDFLPVDTATSNGRIKQLRSGALQIENSEESDQGKYECVATNSAGtRYSAPANLYV 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 124-450 1.50e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 61.79  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  124 HLEKLDLRSNLISTVTSEELSYLAAVRSVDLSRNLISY-LPKPTTSAKVNIEKLDLASNSITdiGTDHFSSFNTLVTLKL 202
Cdd:PLN00113  70 RVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGpIPDDIFTTSSSLRYLNLSNNNFT--GSIPRGSIPNLETLDL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  203 ARNHIT---TLNQFSFSRLRkleSLDLTRNMIREVRFLAFNQLPSLQNVSLARNDVYRLDDGMFYACEGLKHLNLSTNRV 279
Cdd:PLN00113 148 SNNMLSgeiPNDIGSFSSLK---VLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNL 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  280 QAVTEGWMFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRIQ-SLPSGSFRvLRQLEELILSANSIDSLHKFA 358
Cdd:PLN00113 225 SGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFS-LQKLISLDLSDNSLSGEIPEL 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  359 LVGMSSLHKLDLSSNTLAVCVEDGAvlynTSMPFLRSLRFTNNQLR-VIPKRAFERfPALEELDLTDNPIATIHPEAF-E 436
Cdd:PLN00113 304 VIQLQNLEILHLFSNNFTGKIPVAL----TSLPRLQVLQLWSNKFSgEIPKNLGKH-NNLTVLDLSTNNLTGEIPEGLcS 378

                        330
                 ....*....|....
gi 17542472  437 PLELKRLVMNSSSI 450
Cdd:PLN00113 379 SGNLFKLILFSNSL 392
LRR_8 pfam13855
Leucine rich repeat;
291-351 1.51e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.45  E-value: 1.51e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542472   291 TSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSI 351
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 629-706 2.01e-09

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: 55.32  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 629 VGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYvtpNDD--HIYIMNVTKEDQGAYTCHATNVAGQTQASANLIVF 706
Cdd:cd05730  17 LGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSF---NEDgsEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKVF 93
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 616-705 6.89e-09

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: 53.76  E-value: 6.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTyTPEDM-----PLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIM-NVTKEDQGAYTCH 689
Cdd:cd05729   1 PRFT-DTEKMeerehALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIeRAIPRDKGKYTCI 79

                        90
                ....*....|....*.
gi 17542472 690 ATNVAGQTQASANLIV 705
Cdd:cd05729  80 VENEYGSINHTYDVDV 95
LRR_8 pfam13855
Leucine rich repeat;
100-159 7.39e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.53  E-value: 7.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542472   100 PNLKILNIRKNRLARIPRGS-HELGHLEKLDLRSNLISTVTSEELSYLAAVRSVDLSRNLI 159
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 630-705 7.77e-09

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: 53.26  E-value: 7.77e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472 630 GQTAKFLCAATGTPRPEIKWAFEQIPFPaaEARRLYVTPNDDH--IYIMNVTKEDQGAYTCHATNVAGQTQASANLIV 705
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRLNWGHVP--DSARVSITSEGGYgtLTIRDVKESDQGAYTCEAINTRGMVFGIPDGIL 76
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 630-705 9.19e-09

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: 53.02  E-value: 9.19e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542472 630 GQTAKFLCAATGTPRPEIKWAFEQIPFPaaeARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLIV 705
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTKGGSQLS---VDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 637-705 2.48e-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: 52.08  E-value: 2.48e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542472 637 CAATGTPRPEIKWAF--EQIpfpaAEARRLYVTPnDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLIV 705
Cdd:cd04969  24 CKPKASPKPTISWSKgtELL----TNSSRICILP-DGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 629-700 2.54e-08

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: 52.17  E-value: 2.54e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542472 629 VGQTAKFLCAATGTPRPEIKWAFEQ---IPFPAAEARRLYVTPNddhiyIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd05856  18 VGSSVRLKCVASGNPRPDITWLKDNkplTPPEIGENKKKKWTLS-----LKNLKPEDSGKYTCHVSNRAGEINAT 87
LRR_8 pfam13855
Leucine rich repeat;
196-255 2.59e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.99  E-value: 2.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   196 TLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARNDV 255
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
41-284 3.52e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 57.40  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   41 LDLSEIPTTIPNNTRILLLSDNEIESIDKSrLKGfyFLQTLDISNNIIRHIDfeffYNLPN-LKILNIRKNRLARIPRgs 119
Cdd:PRK15370 188 LGLTTIPACIPEQITTLILDNNELKSLPEN-LQG--NIKTLYANSNQLTSIP----ATLPDtIQEMELSINRITELPE-- 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  120 HELGHLEKLDLRSNLISTVTS---EELSYLaavrsvDLSRNLISYLPKPTTSAkvnIEKLDLASNSITDIGTDHFSSFNT 196
Cdd:PRK15370 259 RLPSALQSLDLFHNKISCLPEnlpEELRYL------SVYDNSIRTLPAHLPSG---ITHLNVQSNSLTALPETLPPGLKT 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  197 LVTlklARNHITTLNQfsfSRLRKLESLDLTRNMIrevRFLAFNQLPSLQNVSLARNDVYRLDDGMFYAcegLKHLNLST 276
Cdd:PRK15370 330 LEA---GENALTSLPA---SLPPELQVLDVSKNQI---TVLPETLPPTITTLDVSRNALTNLPENLPAA---LQIMQASR 397


                 ....*...
gi 17542472  277 NRVQAVTE 284
Cdd:PRK15370 398 NNLVRLPE 405
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 511-607 3.53e-08

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: 52.27  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 511 PVEVSTLIGEKARFTCNVYGASPLSIEW--RVMENGQPrvLVQDSATFLSINRTAVVNGTFDERELaaaeLLLDNVAMTD 588
Cdd:cd05858   8 PANTSVVVGTDAEFVCKVYSDAQPHIQWlkHVEKNGSK--YGPDGLPYVEVLKTAGVNTTDKEIEV----LYLRNVTFED 81

                        90
                ....*....|....*....
gi 17542472 589 NSEYQCVARNRFGsdFSTH 607
Cdd:cd05858  82 AGEYTCLAGNSIG--ISHH 98
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
 618-707 4.09e-08

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.


Pssm-ID: 409534  Cd Length: 116  Bit Score: 52.27  E-value: 4.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 618 FTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFE-QIP-------FPAAEARRLYVTPN-DDH----IYIMNVTKEDQG 684
Cdd:cd20940   3 FIKSPLSQQRLVGDSVELHCEAVGSPIPEIQWWFEgQEPneicsqlWDGARLDRVHINATyHQHatstISIDNLTEEDTG 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 17542472 685 AYTCHATNVAGQT-----------QASANLIVFE 707
Cdd:cd20940  83 TYECRASNDPDRNhltrapkvkwiRSQANVLVLE 116
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 506-612 5.23e-08

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: 51.09  E-value: 5.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 506 KIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWrvmengqprvlVQDSATFLSINRTAVvngtfdereLAAAELLLDNVA 585
Cdd:cd20968   1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSW-----------IKGDDLIKENNRIAV---------LESGSLRIHNVQ 60

                        90       100
                ....*....|....*....|....*..
gi 17542472 586 MTDNSEYQCVARNRFGSDFSTHVKLQV 612
Cdd:cd20968  61 KEDAGQYRCVAKNSLGIAYSKPVTIEV 87
LRR_8 pfam13855
Leucine rich repeat;
339-427 6.49e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.83  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   339 RQLEELILSANSIDSLHKFALVGMSSLHKLDLSsntlavcvedgavlyntsmpflrslrftNNQLRVIPKRAFERFPALE 418
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLS----------------------------NNLLTTLSPGAFSGLPSLR 52


                  ....*....
gi 17542472   419 ELDLTDNPI 427
Cdd:pfam13855  53 YLDLSGNRL 61
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 621-705 9.77e-08

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: 50.29  E-value: 9.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 621 TPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEarRLYVTPNDDHIYIMNVtkEDQGAYTCHATNVAGQTQAS 700
Cdd:cd05728   5 VISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASEN--RIEVEAGDLRITKLSL--SDSGMYQCVAENKHGTIYAS 80


                ....*
gi 17542472 701 ANLIV 705
Cdd:cd05728  81 AELAV 85
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 623-705 1.26e-07

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: 50.02  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 623 EDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPA-AEarrlyVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASA 701
Cdd:cd05851   9 KDTYALKGQNVTLECFALGNPVPVIRWRKILEPMPAtAE-----ISMSGAVLKIFNIQPEDEGTYECEAENIKGKDKHQA 83


                ....
gi 17542472 702 NLIV 705
Cdd:cd05851  84 RVYV 87
LRR_8 pfam13855
Leucine rich repeat;
53-112 1.73e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 1.73e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472    53 NTRILLLSDNEIESIDKSRLKGFYFLQTLDISNNIIRHIDFEFFYNLPNLKILNIRKNRL 112
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 640-705 2.01e-07

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: 49.13  E-value: 2.01e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542472 640 TGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLIV 705
Cdd:cd05748  17 KGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 506-598 2.35e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.10  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   506 KIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVmeNGQPRVLVQDSATFLSINRtavvngtfderelaaAELLLDNVA 585
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYK--NGEPISSGSTRSRSLSGSN---------------STLTISNVT 65

                          90
                  ....*....|...
gi 17542472   586 MTDNSEYQCVARN 598
Cdd:pfam13927  66 RSDAGTYTCVASN 78
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 616-705 2.77e-07

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: 49.01  E-value: 2.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLyVTPNDDhIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:cd05764   1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTL-VYDNGT-LDILITTVKDTGAFTCIASNPAG 78

                        90
                ....*....|
gi 17542472 696 QTQASANLIV 705
Cdd:cd05764  79 EATARVELHI 88
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 628-695 3.50e-07

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: 48.75  E-value: 3.50e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472 628 LVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYvtpNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:cd05876   8 LRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQN---HNKTLQLLNVGESDDGEYVCLAENSLG 72
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 616-705 4.11e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first 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: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 48.89  E-value: 4.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDH--IYIMNVTKEDQGAYTCHATNV 693
Cdd:cd20974   1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQISFSDGRakLSIPAVTKANSGRYSLTATNG 80

                        90
                ....*....|..
gi 17542472 694 AGQTQASANLIV 705
Cdd:cd20974  81 SGQATSTAELLV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 615-705 4.48e-07

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: 48.73  E-value: 4.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 615 APKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAfeqipfpaAEARRLYVTPN-------DDH-IYIMNVTKEDQGAY 686
Cdd:cd20972   1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWF--------CEGKELQNSPDiqihqegDLHsLIIAEAFEEDTGRY 72

                        90
                ....*....|....*....
gi 17542472 687 TCHATNVAGQTQASANLIV 705
Cdd:cd20972  73 SCLATNSVGSDTTSAEIFV 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 622-705 7.13e-07

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: 47.78  E-value: 7.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAA-TGTPRPEIKWAFEQIPFPAAEARRLYVTpnDDHIYIMNVTKEDQGAYTCHATNVAGQTQ-A 699
Cdd:cd05724   4 PSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVD--DGNLLIAEARKSDEGTYKCVATNMVGEREsR 81


                ....*.
gi 17542472 700 SANLIV 705
Cdd:cd05724  82 AARLSV 87
LRR_8 pfam13855
Leucine rich repeat;
393-450 8.06e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 8.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542472   393 LRSLRFTNNQLRVIPKRAFERFPALEELDLTDNPIATIHPEAFEPLE-LKRLVMNSSSI 450
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPsLRYLDLSGNRL 61
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 622-705 8.91e-07

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: 48.03  E-value: 8.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAATGTPRPEIKW---------AFEQIPFPAAEARRLY-VTPNDDHI---YIMNVTKEDQGAYTC 688
Cdd:cd05858   8 PANTSVVVGTDAEFVCKVYSDAQPHIQWlkhvekngsKYGPDGLPYVEVLKTAgVNTTDKEIevlYLRNVTFEDAGEYTC 87

                        90
                ....*....|....*..
gi 17542472 689 HATNVAGQTQASANLIV 705
Cdd:cd05858  88 LAGNSIGISHHSAWLTV 104
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 616-705 9.04e-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: 47.58  E-value: 9.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLvgqtakFLCAATGTPRPEIKWAfeqipfpaaeARRLYVTPND------DH-IYIMNVTKEDQGAYTC 688
Cdd:cd05723   4 PSNIYAHESMDIV------FECEVTGKPTPTVKWV----------KNGDVVIPSDyfkivkEHnLQVLGLVKSDEGFYQC 67

                        90
                ....*....|....*..
gi 17542472 689 HATNVAGQTQASANLIV 705
Cdd:cd05723  68 IAENDVGNAQASAQLII 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 616-705 1.49e-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: 47.07  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEAR-RLYvtpNDDHIY----IMNVTKEDQGAYTCHA 690
Cdd:cd05892   1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRiSLY---QDNCGRicllIQNANKKDAGWYTVSA 77

                        90
                ....*....|....*
gi 17542472 691 TNVAGQTQASANLIV 705
Cdd:cd05892  78 VNEAGVVSCNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 511-612 2.87e-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: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472    511 PVEVSTLIGEKARFTCNVYGASPLSIEWRvmeNGQPRVLVQDSatflsinRTAVVNGTFDerelaaAELLLDNVAMTDNS 590
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWY---KQGGKLLAESG-------RFSVSRSGST------STLTISNVTPEDSG 64

                           90       100
                   ....*....|....*....|..
gi 17542472    591 EYQCVARNRFGSDFSThVKLQV 612
Cdd:smart00410  65 TYTCAATNSSGSASSG-TTLTV 85
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 616-695 4.51e-06

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: 45.95  E-value: 4.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFE------QIPFPAAEARRLYVTPNDDhIYIMNVTKEDQGAYTCH 689
Cdd:cd05734   2 PRFVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKHSkgsgvpQFQHIVPLNGRIQLLSNGS-LLIKHVLEEDSGYYLCK 80


                ....*.
gi 17542472 690 ATNVAG 695
Cdd:cd05734  81 VSNDVG 86
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 622-701 4.60e-06

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-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: 409454  Cd Length: 89  Bit Score: 45.74  E-value: 4.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPF---PAAEARRLyvtpNDDHIYIMNVTKEDQGAYTCHATNVAGQTQ 698
Cdd:cd05868   6 PTNLVLSPGEDGTLICRANGNPKPSISWLTNGVPIeiaPTDPSRKV----DGDTIIFSKVQERSSAVYQCNASNEYGYLL 81


                ...
gi 17542472 699 ASA 701
Cdd:cd05868  82 ANA 84
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 615-705 6.30e-06

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: 45.62  E-value: 6.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 615 APKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIK--WAFEQIPF----PAAEARRLYVTPNDDHIYIMNVTKEDQGAYTC 688
Cdd:cd04970   2 ATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGVPIdlekIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTC 81

                        90
                ....*....|....*..
gi 17542472 689 HATNVAGQTQASANLIV 705
Cdd:cd04970  82 TAQTVVDSDSASATLVV 98
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
154-395 6.88e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 50.08  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  154 LSRNLISYLPKpttSAKVNIEKLDLASNSITDIGTdhfSSFNTLVTLKLARNHITTLNQfsfsRL-RKLESLDLTRNMIR 232
Cdd:PRK15370 206 LDNNELKSLPE---NLQGNIKTLYANSNQLTSIPA---TLPDTIQEMELSINRITELPE----RLpSALQSLDLFHNKIS 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  233 EVRflafNQLPS-LQNVSLARNDVYRLDDgmfYACEGLKHLNLSTNRVQAVTEGWMFGLTSLEVLDlsyNQIQSFhisSW 311
Cdd:PRK15370 276 CLP----ENLPEeLRYLSVYDNSIRTLPA---HLPSGITHLNVQSNSLTALPETLPPGLKTLEAGE---NALTSL---PA 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  312 SHTPKLKWLSLHSNRIQSLPSgsfRVLRQLEELILSANSIDSLHKFAlvgMSSLHKLDLSSNTLAVCVEdgavlyntSMP 391
Cdd:PRK15370 343 SLPPELQVLDVSKNQITVLPE---TLPPTITTLDVSRNALTNLPENL---PAALQIMQASRNNLVRLPE--------SLP 408


                 ....
gi 17542472  392 FLRS 395
Cdd:PRK15370 409 HFRG 412
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 616-705 8.57e-06

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: 44.99  E-value: 8.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFL--CAATGTPRPEIKWAfeqipfpaaEARRLYVTPNDDHIY------IMNVTKEDQGAYT 687
Cdd:cd05852   1 PTFEFNPMKKKILAAKGGRVIieCKPKAAPKPKFSWS---------KGTELLVNNSRISIWddgsleILNITKLDEGSYT 71

                        90
                ....*....|....*...
gi 17542472 688 CHATNVAGQTQASANLIV 705
Cdd:cd05852  72 CFAENNRGKANSTGVLSV 89
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 637-703 8.90e-06

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: 44.10  E-value: 8.90e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542472 637 CAATGTPRPEIKWAFEQIPFpaAEARRLYVTPnDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANL 703
Cdd:cd05746   5 CSAQGDPEPTITWNKDGVQV--TESGKFHISP-EGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig6_Contactin-2 cd05854
Sixth immunoglobulin (Ig) domain of contactin-2; The members here are composed of the sixth ...
 615-705 1.53e-05

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: 44.65  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 615 APKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIK--WAFEQIPF----PAAEARRLYVTPNDDHIYIMNVTKEDQGAYTC 688
Cdd:cd05854   2 ATKITLAPSSADINQGENLTLQCHASHDPTMDLTftWSLDDFPIdldkPNGHYRRMEVKETIGDLVIVNAQLSHAGTYTC 81

                        90
                ....*....|....*..
gi 17542472 689 HATNVAGQTQASANLIV 705
Cdd:cd05854  82 TAQTVVDSASASATLVV 98
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 618-705 1.62e-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: 44.12  E-value: 1.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 618 FTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIyIMNVTKEDQGAYTCHATNVAGQT 697
Cdd:cd05867   2 WTRRPQSHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGALI-LTDVQPSDTAVYQCEARNRHGNL 80


                ....*...
gi 17542472 698 QASANLIV 705
Cdd:cd05867  81 LANAHVHV 88
LRRNT smart00013
Leucine rich repeat N-terminal domain;
29-54 1.68e-05

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 42.30  E-value: 1.68e-05
                           10        20
                   ....*....|....*....|....*.
gi 17542472     29 CHCVGNVVDCSSLDLSEIPTTIPNNT 54
Cdd:smart00013   6 CNCSGTAVDCSGRGLTEVPLDLPPDT 31
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 616-695 2.09e-05

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: 43.84  E-value: 2.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKW--AFEQIPfpaAEARRLYVTPN-----DDHIYIMNVTKEDQGAYTC 688
Cdd:cd20954   2 PRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWkkATGSTP---GEYKDLLYDPNvrilpNGTLVFGHVQKENEGHYLC 78


                ....*..
gi 17542472 689 HATNVAG 695
Cdd:cd20954  79 EAKNGIG 85
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 622-707 2.23e-05

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 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-nonNCAM), 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 the Ig1, Ig2, and Ig3 domains. 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. 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: 409451  Cd Length: 97  Bit Score: 43.88  E-value: 2.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAATGTPR-PEIKWAFEQIPFPAAEARRLYVTPNDDH---IYIMNVTKEDQGAYTCHATNVA-GQ 696
Cdd:cd05865   7 PSQGEISVGESKFFLCQVAGEAKdKDISWFSPNGEKLTPNQQRISVVRNDDYsstLTIYNANIDDAGIYKCVVSNEDeGE 86

                        90
                ....*....|.
gi 17542472 697 TQASANLIVFE 707
Cdd:cd05865  87 SEATVNVKIFQ 97
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 55-117 2.33e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 46.32  E-value: 2.33e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542472  55 RILLLSDNEIESIDKsrLKGFYFLQTLDISNNIIRHID--FEFFYNLPNLKILNIRKNRLARIPR 117
Cdd:cd21340 123 RVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEelLDLLSSWPSLRELDLTGNPVCKKPK 185
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 617-695 2.88e-05

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: 43.38  E-value: 2.88e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542472 617 KFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFpaAEARRLYVTpNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:cd20968   1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLI--KENNRIAVL-ESGSLRIHNVQKEDAGQYRCVAKNSLG 76
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 610-707 3.11e-05

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, 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 of neural cell adhesion molecule NCAM-1. NCAM-1 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-nonNCAM) 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 the Ig1, Ig2, and Ig3 domains. 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). 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: 409366  Cd Length: 95  Bit Score: 43.39  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 610 LQVyqapkfTYTPEDMPLLVGQTAKFLCAATGTPRpEIKWAFEQIPFPAAEARRLYVTPNDD---HIYIMNVTKEDQGAY 686
Cdd:cd04977   1 LQV------KIIPSYAEISVGESKFFLCKVSGDAK-NINWVSPNGEKVLTKHGNLKVVNHGSvlsSLTIYNANINDAGIY 73

                        90       100
                ....*....|....*....|..
gi 17542472 687 TCHATNVAGQT-QASANLIVFE 707
Cdd:cd04977  74 KCVATNGKGTEsEATVKLDIIQ 95
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 622-703 4.51e-05

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: 43.11  E-value: 4.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 622 PEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASA 701
Cdd:cd05747  10 PRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQF 89


                ..
gi 17542472 702 NL 703
Cdd:cd05747  90 TL 91
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 269-453 6.29e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.19  E-value: 6.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 269 LKHLNLSTNRVQAVTEGW---MFGLTS---LEVLDLSYNQIQ---SFHISSWSHTPKLKWLSLHSNRI---------QSL 330
Cdd:cd00116  53 LKELCLSLNETGRIPRGLqslLQGLTKgcgLQELDLSDNALGpdgCGVLESLLRSSSLQELKLNNNGLgdrglrllaKGL 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 331 PSGSFRvlrqLEELILSANSIDSLHKFALVG----MSSLHKLDLSSNTL-----AVCVEDGAVLYNtsmpfLRSLRFTNN 401
Cdd:cd00116 133 KDLPPA----LEKLVLGRNRLEGASCEALAKalraNRDLKELNLANNGIgdagiRALAEGLKANCN-----LEVLDLNNN 203

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542472 402 QLR----VIPKRAFERFPALEELDLTDNPI-----ATIHPEAFEPLE-LKRLVMNSSSILCD 453
Cdd:cd00116 204 GLTdegaSALAETLASLKSLEVLNLGDNNLtdagaAALASALLSPNIsLLTLSLSCNDITDD 265
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 644-691 6.51e-05

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 42.31  E-value: 6.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17542472 644 RPEIKWAFEQIPFPAAEARrlyvTPNDDHIYIMNVTKEDQGAYTCHAT 691
Cdd:cd05757  29 LPPIQWYKDCKPLQGDKRF----IPKGSKLLIQNVTEEDAGNYTCKFT 72
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 503-612 9.51e-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: 42.15  E-value: 9.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 503 PRakIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWrvMENGQPrvLVQDSATFLSiNRTAVVNGTfdereLAAAELLLD 582
Cdd:cd07693   1 PR--IVEHPSDLIVSKGDPATLNCKAEGRPTPTIQW--LKNGQP--LETDKDDPRS-HRIVLPSGS-----LFFLRVVHG 68

                        90       100       110
                ....*....|....*....|....*....|
gi 17542472 583 NVAMTDNSEYQCVARNRFGSDFSTHVKLQV 612
Cdd:cd07693  69 RKGRSDEGVYVCVAHNSLGEAVSRNASLEV 98
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 508-601 9.79e-05

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: 42.05  E-value: 9.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 508 VRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVmeNGQPrvlVQDsatfLSINRTAVVNGTfderelaaaELLLDNVAMT 587
Cdd:cd04978   3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRL--NGVP---IEP----APEDMRRTVDGR---------TLIFSNLQPN 64

                        90
                ....*....|....
gi 17542472 588 DNSEYQCVARNRFG 601
Cdd:cd04978  65 DTAVYQCNASNVHG 78
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 508-602 1.01e-04

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: 41.61  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 508 VRQPVEVSTLIGEKARFTCNVYGASPLSIEWRvMENGQprvlvqdsatfLSINRTavvngtfdeRELAAAELLLDNVAMT 587
Cdd:cd05725   1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWR-KEDGE-----------LPKGRY---------EILDDHSLKIRKVTAG 59

                        90
                ....*....|....*
gi 17542472 588 DNSEYQCVARNRFGS 602
Cdd:cd05725  60 DMGSYTCVAENMVGK 74
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 522-608 1.89e-04

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: 40.39  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 522 ARFTCNVYGASPLSIEWRVmeNGQPrvlvqDSATFLSINRTAVVNGTfderelaaaeLLLDNVAMTDNSEYQCVARNRFG 601
Cdd:cd00096   1 VTLTCSASGNPPPTITWYK--NGKP-----LPPSSRDSRRSELGNGT----------LTISNVTLEDSGTYTCVASNSAG 63


                ....*..
gi 17542472 602 SDFSTHV 608
Cdd:cd00096  64 GSASASV 70
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 616-716 1.92e-04

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: 41.48  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAG 695
Cdd:cd05762   2 PQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLG 81

                        90       100
                ....*....|....*....|.
gi 17542472 696 QTQASANLIVFENffhyPESP 716
Cdd:cd05762  82 SRQAQVNLTVVDK----PDPP 98
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 627-703 1.99e-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: 41.03  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   627 LLVGQTAKFLC-AATGTPRPEIKWAFE--QIPFPaaearRLYVTPNDDH----IYIMNVTKEDQGAYTCHATNVAGQTQA 699
Cdd:pfam00047   8 VLEGDSATLTCsASTGSPGPDVTWSKEggTLIES-----LKVKHDNGRTtqssLLISNVTKEDAGTYTCVVNNPGGSATL 82


                  ....
gi 17542472   700 SANL 703
Cdd:pfam00047  83 STSL 86
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 630-705 2.08e-04

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: 41.22  E-value: 2.08e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542472 630 GQTAKFLCAATGTPRPEIKWAFEQI-PFPAAEARRLYVTPnDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLIV 705
Cdd:cd20969  17 GHTVQFVCRADGDPPPAILWLSPRKhLVSAKSNGRLTVFP-DGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 49-286 2.58e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.40  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  49 TIPNNTRILLLSDNEI-----ESIDKSrLKGFYFLQTLDISNNiirHIDFEFFYNLPNlkilNIRKNRlariprgshelg 123
Cdd:COG5238 205 TQNTTVTTLWLKRNPIgdegaEILAEA-LKGNKSLTTLDLSNN---QIGDEGVIALAE----ALKNNT------------ 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 124 HLEKLDLRSNLISTVTSEELSYLaavrsvdLSRNlisylpkpttsakVNIEKLDLASNSITDIGT----DHFSSFNTLVT 199
Cdd:COG5238 265 TVETLYLSGNQIGAEGAIALAKA-------LQGN-------------TTLTSLDLSVNRIGDEGAialaEGLQGNKTLHT 324

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 200 LKLARNHITT-----LNQfSFSRLRKLESLDLTRNMIREVRFLAFNQL----PSLQNVSLARNDVYrlDDGmfyACEGLK 270
Cdd:COG5238 325 LNLAYNGIGAqgaiaLAK-ALQENTTLHSLDLSDNQIGDEGAIALAKYlegnTTLRELNLGKNNIG--KQG---AEALID 398

                       250
                ....*....|....*.
gi 17542472 271 HLNlsTNRVQAVTEGW 286
Cdd:COG5238 399 ALQ--TNRLHTLILDG 412
LRR_9 pfam14580
Leucine-rich repeat;
290-376 2.94e-04

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 42.44  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   290 LTSLEVLDLSYNQIQSfhISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKF-ALVGMSSLHKL 368
Cdd:pfam14580  41 LDQFDTIDFSDNEIRK--LDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLdPLASLKKLTFL 118


                  ....*...
gi 17542472   369 DLSSNTLA 376
Cdd:pfam14580 119 SLLRNPVT 126
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 510-612 3.33e-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: 40.54  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 510 QPVEVSTLIGEKARFTCNVYGASPLSIEWRvmENGqprvlvqdsatflsinrtAVVNGTFDER--ELAAAELLLDNVAMT 587
Cdd:cd05722   7 EPSDIVAMRGGPVVLNCSAESDPPPKIEWK--KDG------------------VLLNLVSDERrqQLPNGSLLITSVVHS 66

                        90       100       110
                ....*....|....*....|....*....|.
gi 17542472 588 -----DNSEYQCVARN-RFGSDFSTHVKLQV 612
Cdd:cd05722  67 khnkpDEGFYQCVAQNeSLGSIVSRTARVTV 97
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 514-612 4.31e-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: 40.07  E-value: 4.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 514 VSTLIGEKARFTCNVYGASPLSIEWrvMENGQPrvlVQDSAtflsiNRTAVVNGTfderelaaaeLLLDNVAMTDNSEYQ 593
Cdd:cd20978  11 VVVKGGQDVTLPCQVTGVPQPKITW--LHNGKP---LQGPM-----ERATVEDGT----------LTIINVQPEDTGYYG 70

                        90
                ....*....|....*....
gi 17542472 594 CVARNRFGsDFSTHVKLQV 612
Cdd:cd20978  71 CVATNEIG-DIYTETLLHV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 719-788 5.59e-04

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: 39.80  E-value: 5.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542472    719 SPMLIKKRDALKIDCSCDLiSSRQRMVWKRQQQVILFLK---KAKFSDNDQILTLTQTTFSDSGEYSCELWVD 788
Cdd:smart00410   2 PSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNS 73
LRRNT pfam01462
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
 29-51 6.08e-04

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 396168 [Multi-domain]  Cd Length: 28  Bit Score: 37.99  E-value: 6.08e-04
                          10        20
                  ....*....|....*....|...
gi 17542472    29 CHCVGNVVDCSSLDLSEIPTTIP 51
Cdd:pfam01462   6 CHCSATVVNCSDRGLTAVPRDLP 28
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 519-601 6.16e-04

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: 39.49  E-value: 6.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 519 GEKARFTCNVYGASPLSIEWRVmeNGQPrvlvqdsatflsinrtavVNGTFDE--RELAAAELLLDNVAMTDNSEYQCVA 596
Cdd:cd05867  14 GETARLDCQVEGIPTPNITWSI--NGAP------------------IEGTDPDprRHVSSGALILTDVQPSDTAVYQCEA 73


                ....*
gi 17542472 597 RNRFG 601
Cdd:cd05867  74 RNRHG 78
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 78-233 6.95e-04

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 42.73  E-value: 6.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472  78 LQTLDISNNIIRHIDFEffynlpnlkilnirknRLARIPRgshELGHLEKLDLRSNlisTVTSEELSYLAAvrsvdlsrn 157
Cdd:cd00116 167 LKELNLANNGIGDAGIR----------------ALAEGLK---ANCNLEVLDLNNN---GLTDEGASALAE--------- 215

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 158 lisylpkpTTSAKVNIEKLDLASNSITDIGTDHFSSFN-----TLVTLKLARNHITTLNQFSFSRLRK----LESLDLTR 228
Cdd:cd00116 216 --------TLASLKSLEVLNLGDNNLTDAGAAALASALlspniSLLTLSLSCNDITDDGAKDLAEVLAekesLLELDLRG 287


                ....*
gi 17542472 229 NMIRE 233
Cdd:cd00116 288 NKFGE 292
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 629-705 7.11e-04

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: 39.40  E-value: 7.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 629 VGQTAKFLCAATGTPRP-EIKWAFEQIPFP---AAEARRLyvTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLI 704
Cdd:cd20959  16 VGMRAQLHCGVPGGDLPlNIRWTLDGQPISddlGITVSRL--GRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLT 93


                .
gi 17542472 705 V 705
Cdd:cd20959  94 V 94
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 511-603 8.37e-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: 39.10  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   511 PVEVSTLIGEKARFTCNV-YGASPLSIEWRVmeNGQprVLVQDSATFLSINRTAVvngtfderelaaAELLLDNVAMTDN 589
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSK--EGG--TLIESLKVKHDNGRTTQ------------SSLLISNVTKEDA 66

                          90
                  ....*....|....
gi 17542472   590 SEYQCVARNRFGSD 603
Cdd:pfam00047  67 GTYTCVVNNPGGSA 80
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 616-705 1.00e-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: 38.99  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 616 PKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFpAAEARRLYVTPNDD--HIYIMNVTKEDQGAYTCHATNV 693
Cdd:cd20975   1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPV-RPDQRRFAEEAEGGlcRLRILAAERGDAGFYTCKAVNE 79

                        90
                ....*....|..
gi 17542472 694 AGQTQASANLIV 705
Cdd:cd20975  80 YGARQCEARLEV 91
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 637-695 1.06e-03

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: 38.93  E-value: 1.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542472 637 CAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMN---VTKEDQGAYTCHATNVAG 695
Cdd:cd05733  23 CEAKGNPQPTFRWTKDGKFFDPAKDPRVSMRRRSGTLVIDNhngGPEDYQGEYQCYASNELG 84
IgI_1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the ...
 627-707 1.11e-03

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. 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: 409452  Cd Length: 93  Bit Score: 38.88  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 627 LLVGQTAKFLCAATGTPRpEIKWAFEQIPFPAAEARrlYVTPND---DHIYIMNVTKEDQGAYTCHATNVAGQTQASAnl 703
Cdd:cd05866  12 LSVGESKFFTCTAIGEPE-SIDWYNPQGEKIVSSQR--VVVQKEgvrSRLTIYNANIEDAGIYRCQATDAKGQTQEAT-- 86


                ....
gi 17542472 704 IVFE 707
Cdd:cd05866  87 VVLE 90
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
 620-707 1.18e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (also known as Flt-1), VEGFR-2 (also known as KDR or Flk-1) and VEGFR-3 (also known as Flt-4). VEGF_A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth.


Pssm-ID: 409448  Cd Length: 102  Bit Score: 39.35  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 620 YTPEDMPLLVGQTAKFLCAATgTP---RPEIKWAF--EQIPFPAAEARRLYVTPNDDHIY-----IMNVTKEDQGAYTCH 689
Cdd:cd05862   6 SPPKPVELLVGEKLVLNCTAR-TElnvGVDFQWDYpgKKEQRRASVRRRRKQQSSEATEFsstltIDNVTLSDKGLYTCA 84

                        90
                ....*....|....*...
gi 17542472 690 ATNVAGQTQASANLIVFE 707
Cdd:cd05862  85 ASSGPMFKKNSTSVIVHE 102
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 628-705 1.26e-03

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: 38.54  E-value: 1.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472 628 LVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAearRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLIV 705
Cdd:cd05731   8 LRGGVLLLECIAEGLPTPDIRWIKLGGELPKG---RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 640-700 1.44e-03

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: 38.67  E-value: 1.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542472 640 TGTPRPEIKWAFEQIPFPAAEAR-RLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd05894  20 SGEPAPTVTWSRGDKAFTATEGRvRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHAS 81
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 507-602 1.70e-03

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: 38.68  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 507 IVRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVMENGQPRVLVQDSATFLSINRTAVvngtfderelaaAELLLDNVAM 586
Cdd:cd05765   3 LVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQVPGKENLIMRPNHVRGNVVVTNI------------GQLVIYNAQP 70

                        90
                ....*....|....*.
gi 17542472 587 TDNSEYQCVARNRFGS 602
Cdd:cd05765  71 QDAGLYTCTARNSGGL 86
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 645-691 2.06e-03

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 38.21  E-value: 2.06e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17542472 645 PEIKWAFEQIPFPAAEARrlYVTPNDDhIYIMNVTKEDQGAYTCHAT 691
Cdd:cd20994  31 PKVQWYKDCKPLLLDDKR--FAGLESD-LLIFNVTVQDQGNYTCHTS 74
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 579-609 2.10e-03

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: 37.77  E-value: 2.10e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 17542472 579 LLLDNVAMTDNSEYQCVARNRFGS---DFSTHVK 609
Cdd:cd05731  50 LKIENVSEADSGEYQCTASNTMGSarhTISVTVE 83
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 630-695 2.24e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; 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.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 38.30  E-value: 2.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542472 630 GQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIM-NVTKEDQGAYTCHATNVAG 695
Cdd:cd05857  19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMeSVVPSDKGNYTCVVENEYG 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 722-786 2.48e-03

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: 37.94  E-value: 2.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542472   722 LIKKRDALKIDCSCDLISSRQRMVWKRQQQVILFLKKAKFSDNDQI---LTLTQTTFSDSGEYSCELW 786
Cdd:pfam00047   7 TVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTqssLLISNVTKEDAGTYTCVVN 74
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 205-318 2.74e-03

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 38.68  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   205 NHITTLNQFSFSRLRKLESLDLTRNmIREVRFLAFNQLpSLQNVSLaRNDVYRLDDGMFYACEGLKHLNLSTNrvqaVTE 284
Cdd:pfam13306  20 SSLTSIGEYAFSNCTSLKSITLPSS-LTSIGSYAFYNC-SLTSITI-PSSLTSIGEYAFSNCSNLKSITLPSN----LTS 92

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17542472   285 --GWMFGLTSLEVLDLSYNqIQSFHISSWSHTPKLK 318
Cdd:pfam13306  93 igSYAFSNCSLKSITIPSS-VTTIGSYAFSNCSNLK 127
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 621-705 3.99e-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: 37.09  E-value: 3.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 621 TPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEArrlyvtpnddhIYIMNVTKEDQGAYTCHATNVAGQTQAS 700
Cdd:cd20948   1 SPSDTYYLSGENLNLSCHAASNPPAQYSWTINGTFQTSSQE-----------LFLPAITENNEGTYTCSAHNSLTGKNIS 69


                ....*
gi 17542472 701 ANLIV 705
Cdd:cd20948  70 LVLSV 74
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 291-427 4.23e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 40.54  E-value: 4.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 291 TSLEVLDLSYNQI----QSFHISSWSHTPKLKWLSLHSNRI---------QSLPSGsfrvlRQLEELILSANSID----- 352
Cdd:COG5238 208 TTVTTLWLKRNPIgdegAEILAEALKGNKSLTTLDLSNNQIgdegvialaEALKNN-----TTVETLYLSGNQIGaegai 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472 353 SLHKfALVGMSSLHKLDLSSNTLAvcvEDGAV-----LYNTSMpfLRSLRFTNNQLRVIPKR----AFERFPALEELDLT 423
Cdd:COG5238 283 ALAK-ALQGNTTLTSLDLSVNRIG---DEGAIalaegLQGNKT--LHTLNLAYNGIGAQGAIalakALQENTTLHSLDLS 356


                ....
gi 17542472 424 DNPI 427
Cdd:COG5238 357 DNQI 360
PLN03150 PLN03150
hypothetical protein; Provisional
 269-327 4.70e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.57  E-value: 4.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542472  269 LKHLNLSTNRVQAVTEGWMFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRI 327
Cdd:PLN03150 444 LQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 78-112 4.76e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.68  E-value: 4.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 17542472    78 LQTLDISNNIIRhiDFEFFYNLPNLKILNIRKNRL 112
Cdd:pfam12799   3 LEVLDLSNNQIT--DIPPLAKLPNLETLDLSGNNK 35
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 629-692 5.18e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409450  Cd Length: 89  Bit Score: 36.83  E-value: 5.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542472 629 VGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVtpnddHIYIMNVTKEDQGAYTCHATN 692
Cdd:cd05864  16 VGERVRIPVKYLGYPPPEIKWYKNGIPIESNHTIKAGH-----VLTIMEVTEKDAGNYTVVLTN 74
LRR_9 pfam14580
Leucine-rich repeat;
176-274 8.90e-03

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 38.21  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542472   176 LDLASNSITDIgtDHFSSFNTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMIRE-VRFLAFNQLPSLQNVSLARND 254
Cdd:pfam14580  47 IDFSDNEIRKL--DGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQElGDLDPLASLKKLTFLSLLRNP 124

                          90       100
                  ....*....|....*....|
gi 17542472   255 VYRLDDGMFYACEGLKHLNL 274
Cdd:pfam14580 125 VTNKPHYRLYVIYKVPQLRL 144
 
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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