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Conserved domains on  [gi|1831510791|ref|NP_001366805|]
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Mesocentin [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12363-12522 2.69e-26

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


:

Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 109.30  E-value: 2.69e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKIN-DGV 12441
Cdd:cd01450       2 DIVFLLDGSESVGPENFEKVKDFIEKLVE-KLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGgGGT 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12442 AIALyGLNAARQQFQLHG--RENATKVVILITNGKN--RGNAAAAAEDLRDMyGVQLFAVAVGS-NPEELatiKRLVGNS 12516
Cdd:cd01450      81 NTGK-ALQYALEQLFSESnaRENVPKVIIVLTDGRSddGGDPKEAAAKLKDE-GIKVFVVGVGPaDEEEL---REIASCP 155

                    ....*.
gi 1831510791 12517 NTENVI 12522
Cdd:cd01450     156 SERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
12151-12302 2.85e-19

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


:

Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 89.82  E-value: 2.85e-19
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12151 DLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISE-SRRLKGRA 12229
Cdd:smart00327     1 DVVFLLDGSGSMGGNRFELAKEFVLKLV-EQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGT 79
                             90       100       110       120       130       140       150
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510791  12230 QLGAGLREALDEL---SISGVDGVPQIVLIVKNGKASD---DYSSAVKSLKaERNVTVFVVDAGDDESQQQNSELTEED 12302
Cdd:smart00327    80 NLGAALQYALENLfskSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELK-RSGVKVFVVGVGNDVDEEELKKLASAP 157
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
993-1089 1.32e-14

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.30  E-value: 1.32e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   993 SAPQNPEVIVDPDNRVTITWQPPKYPNGEITSYNVYITGDPSlpvDQWQVFPVDDVTDPKLVLQRgaLQPETPYFVKIAA 1072
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEVEVTPGSETSYTLTG--LKPGTEYEFRVRA 76
                            90
                    ....*....|....*..
gi 1831510791  1073 VNPHGEGIHTDPKHFDT 1089
Cdd:cd00063      77 VNGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
394-478 4.79e-12

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


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.71  E-value: 4.79e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    394 PGSAPHLKSASAGRTSLTVRWEPPSiiNRPITTYTLYYTNNPQQPVKNWKKLEVKEPTREVAIPDLRPDTAYYIRVRAND 473
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPP--DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1831510791    474 PLGPG 478
Cdd:smart00060    79 GAGEG 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1824-1903 8.70e-12

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: 65.29  E-value: 8.70e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1824 STTIQILPGSQMTIACNA-TGIPLPQVKWIKAGNYEIDPSRV-DADGNHAQFSLQVANITED--TTFNCVAQNPLGHANW 1899
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVkHDNGRTTQSSLLISNVTKEdaGTYTCVVNNPGGSATL 82

                    ....
gi 1831510791  1900 TINV 1903
Cdd:pfam00047    83 STSL 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1096-1196 2.00e-11

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.44  E-value: 2.00e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGPIKSYTVyfapEYDDSDFKTWQRISVDAPdgaDHGEVTLPKeqFNPNTPYKI 1175
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV----EYREKGSGDWKEVEVTPG---SETSYTLTG--LKPGTEYEF 72
                            90       100
                    ....*....|....*....|.
gi 1831510791  1176 RISATNDLSEGPASDPVRFET 1196
Cdd:cd00063      73 RVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
581-675 2.27e-11

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.05  E-value: 2.27e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   581 PSAPERIR-YQIDGDKVTLQWEPPQITNGPMAGYDVFYTEDPSlprDQWKVHHIDDPNARTTTVLRLNEKTPYTFVIVGR 659
Cdd:cd00063       1 PSPPTNLRvTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*.
gi 1831510791   660 NRLGPGLPSAPFTATT 675
Cdd:cd00063      78 NGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1701-1803 3.66e-11

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 3.66e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1701 GPPVELRVEPDGQRSAVAQWKEPVTSDVPPIGYEIYYVRgdksveeddsAGLNDWIKISIDDPTKLTHKIQNlLLPDTDY 1780
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYRE----------KGSGDWKEVEVTPGSETSYTLTG-LKPGTEY 70
                            90       100
                    ....*....|....*....|...
gi 1831510791  1781 VFKMRAIYPDGPSVFSEPCIMKT 1803
Cdd:cd00063      71 EFRVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1287-1381 4.43e-10

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 4.43e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1287 APNEIVLLPMPNQEINVEWTSPDEVNGQITNYIIHYGEISEDGSEPATWDQVTiardDVNHKLANLEPKKTYAIRVQAVS 1366
Cdd:cd00063       3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS----ETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1831510791  1367 DRGPGVISAPQVIKT 1381
Cdd:cd00063      79 GGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
784-876 3.86e-09

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.89  E-value: 3.86e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   784 SAPLGITPTPMH-TGFDVAWKPPKVTNGRITDYVVYYSKDPDaplSDWES-KTVPADTRNLTVNVDDEDTPYVVKVQART 861
Cdd:cd00063       2 SPPTNLRVTDVTsTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1831510791   862 DDGPGIISEAYEVTT 876
Cdd:cd00063      79 GGGESPPSESVTVTT 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
311-389 4.61e-09

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: 57.59  E-value: 4.61e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   311 PQGPYEVAPGGNINISCT-SVAYPFPDIYWFKNQKVNTDG----PDQNTLRASQILIIKEIYRNE-EFTCVSDNIHGSAN 384
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSaSTGSPGPDVTWSKEGGTLIESlkvkHDNGRTTQSSLLISNVTKEDAgTYTCVVNNPGGSAT 81

                    ....*
gi 1831510791   385 RTVSI 389
Cdd:pfam00047    82 LSTSL 86
EGF_CA smart00179
Calcium-binding EGF-like domain;
12972-13013 4.76e-09

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 55.72  E-value: 4.76e-09
                             10        20        30        40
                     ....*....|....*....|....*....|....*....|....
gi 1831510791  12972 DIDECETNNGqCSEG--CVNTPGSYYCACPHGMMrdplDPFNCV 13013
Cdd:smart00179     1 DIDECASGNP-CQNGgtCVNTVGSYRCECPPGYT----DGRNCE 39
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
226-262 8.63e-09

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.94  E-value: 8.63e-09
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1831510791   226 CAADNGGCSHTCISyNDEKIECKCPRGMTLDVDEKTC 262
Cdd:pfam14670     1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1585-1694 1.34e-08

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.34e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1585 APENIQLTANKPTTISVQYEVPSIPNGNISKYIIYYTPLDDqdpdhqlgqvqtkpiSDWQNVhdmNDGVEGPRKVDIKDf 1664
Cdd:cd00063       3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---------------GDWKEV---EVTPGSETSYTLTG- 63
                            90       100       110
                    ....*....|....*....|....*....|
gi 1831510791  1665 VSTDTAYAVVVQAINDDGPGPYSNQYTIRT 1694
Cdd:cd00063      64 LKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2005-2097 8.92e-08

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 8.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  2005 PKPPSDIRFGKNNDDEQIVDFKPAVASE-PIKEYTISVWPsTDPSNVKKFTTPADVTSGVVVDGLEPDTEYNVQVAAEFY 2083
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGgPITGYVVEYRE-KGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1831510791  2084 EGEELASEPVTVKT 2097
Cdd:cd00063      80 GGESPPSESVTVTT 93
VWA super family cl47497
von Willebrand factor type A domain;
6583-6690 2.28e-06

von Willebrand factor type A domain;


The actual alignment was detected with superfamily member pfam00092:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 52.28  E-value: 2.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  6583 DIIFVLvnDGD---GAQNYDQFKKAVVGFSRKVDMSPDIIRLAVLSVGSEIAVPLPLGGYQEKEHLSSILNSFEIPPIVG 6659
Cdd:pfam00092     1 DIVFLL--DGSgsiGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGT 78
                            90       100       110
                    ....*....|....*....|....*....|....
gi 1831510791  6660 TEILSPVQ-AANQQFTSF--PRTGISKMVVIFAD 6690
Cdd:pfam00092    79 TNTGKALKyALENLFSSAagARPGAPKVVVLLTD 112
VWA super family cl47497
von Willebrand factor type A domain;
12596-12762 1.64e-05

von Willebrand factor type A domain;


The actual alignment was detected with superfamily member pfam00092:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 49.58  E-value: 1.64e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12596 ILVDITSRASADEFRRVLDHLINFFnDRMRDEQHMITINIITVNSDkvQNILSNLRA----DQLSEQLNAITQQSDDTVS 12671
Cdd:pfam00092     4 FLLDGSGSIGGDNFEKVKEFLKKLV-ESLDIGPDGTRVGLVQYSSD--VRTEFPLNDysskEELLSAVDNLRYLGGGTTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12672 pkLGAGIDALAEL---SKENYINGAIKLMLIVgSDGTSSD-DALPAAEYAnSDFQHNIIAVSVRKPATDLLSKIAGLPT- 12746
Cdd:pfam00092    81 --TGKALKYALENlfsSAAGARPGAPKVVVLL-TDGRSQDgDPEEVAREL-KSAGVTVFAVGVGNADDEELRKIASEPGe 156
                           170
                    ....*....|....*..
gi 1831510791 12747 -RVVHLDQWSAPNELFD 12762
Cdd:pfam00092   157 gHVFTVSDFEALEDLQD 173
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1212-1281 1.78e-05

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


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.11  E-value: 1.78e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1212 STYTVEPLGAATITCTATGVPQPKVHWIKANGETV------------DSATLQLYDLVKDTSA--TCVAENNAGKTQEAV 1277
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrsgSTSTLTISNVTPEDSGtyTCAATNSSGSASSGT 81

                     ....
gi 1831510791   1278 SIQV 1281
Cdd:smart00410    82 TLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
681-766 2.58e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 2.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   681 PPVVQLEPSEEMTKEpsNDEMIIECGAQGVPKPKIIWLWSGTLIEDGkeefrvydTTPTDAQDRTRSKLIAQSTTR--SG 758
Cdd:pfam13927     1 KPVITVSPSSVTVRE--GETVTLTCEATGSPPPTITWYKNGEPISSG--------STRSRSLSGSNSTLTISNVTRsdAG 70

                    ....*...
gi 1831510791   759 VATCQAVN 766
Cdd:pfam13927    71 TYTCVASN 78
RhsA super family cl34567
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
5199-5943 2.03e-04

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


The actual alignment was detected with superfamily member COG3209:

Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 49.37  E-value: 2.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5199 DGSPLPTDNTGNYVLVPSDEGATEEKPTQGSESIVHPITKPDGTPLATDSTGSFVTDDDQVIAKDEDGKP-IGPDGQVLP 5277
Cdd:COG3209      23 AGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGyVGGAAAGGG 102
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5278 TDSSGNYIYPVIGPDGQALPTDESGKTVYPVRGPDGTPLSTDASGAVIGSDGKPIPTDETGLPLNKDGSPLPTDNDGNYI 5357
Cdd:COG3209     103 ATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPAT 182
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5358 LIPADESVVKALPTDEAKEVYPIVQPDGTPLATDSSGNfvtssGDIIDIDDEGKPLGPDGQALPTDDSGNYIYPVIGPDG 5437
Cdd:COG3209     183 GVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSA-----TTATGTALGTPASVAATVTGSATGAAGAGAAVATAAT 257
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5438 QALPTDESGKTVYPIRGPDGTPLPTDASGAVIGPDGEPIPTDASGKPLSQDGSPLPTDASGNYILVPSDGEVTKTLPTDD 5517
Cdd:COG3209     258 TLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTT 337
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5518 VGNVIYPITKPDGTPLATDSTGSFVTDDGQIIEKDDEGKPLGPDGQVLSTDDSGNYIYPAVGPNGQTIPTDDTGRTVYP- 5596
Cdd:COG3209     338 TGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDg 417
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5597 ---VRGPDGTPLPTDASGAVIGPDGEPIPTDASGKPLSADGSPLPTDNNGNYVIVPTDGSTVKSHPTDDSGNTIYPVVNE 5673
Cdd:COG3209     418 gpaTAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLG 497
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5674 DGTPLSTDLSGNFLTNSGEIVDRDDEGKPLGPDGQTLPTDASGNYVYLQKVEETTKPLPTDESGNIVYPITKPDGTPLAT 5753
Cdd:COG3209     498 TDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGG 577
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5754 DSTGSFVTEDGTVIEKDDEGKPVGPDGQVLPTDESGNYIYPDVTPDGQVQPTDVSGKPVYPVRGPDGSTLPTDASGAALG 5833
Cdd:COG3209     578 ASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGTTTT 657
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5834 PDGKPIPTDSNGVPLSEDGSPLPTDNQGNYVLVPTSETVTKSMPTDDNRNVIYPITMSDGSLLSTDSTGSFVTEDGKVIE 5913
Cdd:COG3209     658 RATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGT 737
                           730       740       750
                    ....*....|....*....|....*....|
gi 1831510791  5914 KDDEGKPLGPDGQVLPTDASGNYIYPVHGQ 5943
Cdd:COG3209     738 GGTTGTLTTTSTTTTTTAGALTYTYDALGR 767
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
497-578 3.64e-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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 43.79  E-value: 3.64e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   497 VNIVEGDEIRvppmtafeIDCNVTrADPVPVLVWLHKGRPLNKGsktQHIKMKNGGVL-----------ESTQFSCVAEN 565
Cdd:pfam07679    10 VEVQEGESAR--------FTCTVT-GTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTytltisnvqpdDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1831510791   566 EAGKSTKKINVTV 578
Cdd:pfam07679    78 SAGEAEASAELTV 90
RhsA super family cl34567
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
11138-11861 5.91e-04

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


The actual alignment was detected with superfamily member COG3209:

Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 47.83  E-value: 5.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11138 SGKPIYPVFTEDGTQLPTDSTGFAIGPDGELVPTDSANGVPLSKDGSPLPTDASGNYILPDSGVTTANPTDENGYAIYPI 11217
Cdd:COG3209      37 LLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAG 116
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11218 TKPDGTLLATDSTGSYITQGGQLIEKDNTGKPIGPDGQVLPTDGSGNYVYPVVGPDGQALPTDDTGNVVYPVINADGSLL 11297
Cdd:COG3209     117 RLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPATGVGTGAVTLATGLA 196
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11298 ATDSSGSFITENGKIVAKDDEGKPISPDGQVLPTDASGNYIYPALGPDGSILPTDSNGKSIYPVRGPDGTPLPTDEFGFA 11377
Cdd:COG3209     197 GSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDA 276
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11378 IGPDGKPIPTDTSGKPLSADGSPLPTDNNGNYILVLSEGVTEHAPTDENGNVIYPVTNPDGTPLGTDSSGAFITQDGTVV 11457
Cdd:COG3209     277 STGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLT 356
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11458 KKDEDGKPIGPDGQVLPTDNSGNYIYPVIGPDGQVLPTDASGKTVHSVYGPDGTQLPTDASGSAIGPDGELVPTDVSGRP 11537
Cdd:COG3209     357 LGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTG 436
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11538 LSQDGSPLPTDNNGNYALVVSDEATTKVLPTDEGGNVIYHITKPDGSLLGTDASGDFITDHGKAVQKDDEGKPIGPDGSV 11617
Cdd:COG3209     437 TGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGA 516
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11618 LPTDTSGNYIYPITGPDGNVLPTDSNGKPVYPVFNEDGTQLPTDSTGSAIDQDGELVSTDSTSGVPLAKDGSPLPTNSAG 11697
Cdd:COG3209     517 RGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTT 596
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11698 NYVLVSSGKSQPTDEHGNVIYPITKPDGTLLATDSTGSYLTEDGQLVEIDDSGKPLGSDGQVLPIDASGNYIYPALGPDG 11777
Cdd:COG3209     597 TTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTL 676
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11778 QALPTDDAGNLVYPIVYPDGTPLATESTGNYVTENGEVVGKNTDGKPISPDGQVLPTDASGNYIYPAVGPDGQVLPT--- 11854
Cdd:COG3209     677 ATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTSTTTTTtag 756
                           730
                    ....*....|...
gi 1831510791 11855 ------DASGKLI 11861
Cdd:COG3209     757 altytyDALGRLT 769
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12363-12522 2.69e-26

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 109.30  E-value: 2.69e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKIN-DGV 12441
Cdd:cd01450       2 DIVFLLDGSESVGPENFEKVKDFIEKLVE-KLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGgGGT 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12442 AIALyGLNAARQQFQLHG--RENATKVVILITNGKN--RGNAAAAAEDLRDMyGVQLFAVAVGS-NPEELatiKRLVGNS 12516
Cdd:cd01450      81 NTGK-ALQYALEQLFSESnaRENVPKVIIVLTDGRSddGGDPKEAAAKLKDE-GIKVFVVGVGPaDEEEL---REIASCP 155

                    ....*.
gi 1831510791 12517 NTENVI 12522
Cdd:cd01450     156 SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
12363-12532 8.72e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.74  E-value: 8.72e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKINDGVA 12442
Cdd:pfam00092     1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVE-SLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12443 IALYGLNAARQQFQLH---GRENATKVVILITNGK-NRGNAAAAAEDLRDmYGVQLFAVAVGSN-PEELatiKRLVGNSN 12517
Cdd:pfam00092    80 NTGKALKYALENLFSSaagARPGAPKVVVLLTDGRsQDGDPEEVARELKS-AGVTVFAVGVGNAdDEEL---RKIASEPG 155
                           170
                    ....*....|....*
gi 1831510791 12518 TENVIEVAQSTEIDD 12532
Cdd:pfam00092   156 EGHVFTVSDFEALED 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
12363-12533 6.59e-20

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 91.36  E-value: 6.59e-20
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDTgFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKI-NDGV 12441
Cdd:smart00327     1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQ-LDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79
                             90       100       110       120       130       140       150       160
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12442 AIALyGLNAARQQF---QLHGRENATKVVILITNGK---NRGNAAAAAEDLRDmYGVQLFAVAVGSNPEElATIKRLVGN 12515
Cdd:smart00327    80 NLGA-ALQYALENLfskSAGSRRGAPKVVILITDGEsndGPKDLLKAAKELKR-SGVKVFVVGVGNDVDE-EELKKLASA 156
                            170
                     ....*....|....*...
gi 1831510791  12516 SNTENVIEVAQSTEIDDD 12533
Cdd:smart00327   157 PGGVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
12151-12302 2.85e-19

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 89.82  E-value: 2.85e-19
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12151 DLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISE-SRRLKGRA 12229
Cdd:smart00327     1 DVVFLLDGSGSMGGNRFELAKEFVLKLV-EQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGT 79
                             90       100       110       120       130       140       150
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510791  12230 QLGAGLREALDEL---SISGVDGVPQIVLIVKNGKASD---DYSSAVKSLKaERNVTVFVVDAGDDESQQQNSELTEED 12302
Cdd:smart00327    80 NLGAALQYALENLfskSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELK-RSGVKVFVVGVGNDVDEEELKKLASAP 157
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12150-12296 2.25e-17

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 83.88  E-value: 2.25e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISESRRLKGRA 12229
Cdd:cd01450       1 LDIVFLLDGSESVGPENFEKVKDFIEKLV-EKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510791 12230 Q-LGAGLREALDELSISGVD--GVPQIVLIVKNGKASDDYSSAVKSLKA-ERNVTVFVVDAGDDESQQQNS 12296
Cdd:cd01450      80 TnTGKALQYALEQLFSESNAreNVPKVIIVLTDGRSDDGGDPKEAAAKLkDEGIKVFVVGVGPADEEELRE 150
VWA pfam00092
von Willebrand factor type A domain;
12151-12293 5.76e-17

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 83.09  E-value: 5.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12151 DLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISE-SRRLKGRA 12229
Cdd:pfam00092     1 DIVFLLDGSGSIGGDNFEKVKEFLKKLV-ESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTT 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510791 12230 QLGAGLREALDEL---SISGVDGVPQIVLIVKNGKASD-DYSSAVKSLKaERNVTVFVVDAGDDESQQ 12293
Cdd:pfam00092    80 NTGKALKYALENLfssAAGARPGAPKVVVLLTDGRSQDgDPEEVARELK-SAGVTVFAVGVGNADDEE 146
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
993-1089 1.32e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.30  E-value: 1.32e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   993 SAPQNPEVIVDPDNRVTITWQPPKYPNGEITSYNVYITGDPSlpvDQWQVFPVDDVTDPKLVLQRgaLQPETPYFVKIAA 1072
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEVEVTPGSETSYTLTG--LKPGTEYEFRVRA 76
                            90
                    ....*....|....*..
gi 1831510791  1073 VNPHGEGIHTDPKHFDT 1089
Cdd:cd00063      77 VNGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
394-478 4.79e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.71  E-value: 4.79e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    394 PGSAPHLKSASAGRTSLTVRWEPPSiiNRPITTYTLYYTNNPQQPVKNWKKLEVKEPTREVAIPDLRPDTAYYIRVRAND 473
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPP--DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1831510791    474 PLGPG 478
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
394-488 6.51e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.60  E-value: 6.51e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   394 PGSAPHLKSASAGRTSLTVRWEPPSIINRPITTYTLYYTNNPQQpvkNWKKLEVKEPTR-EVAIPDLRPDTAYYIRVRAN 472
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG---DWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*.
gi 1831510791   473 DPLGPGKLGNQVQIKT 488
Cdd:cd00063      78 NGGGESPPSESVTVTT 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1824-1903 8.70e-12

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: 65.29  E-value: 8.70e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1824 STTIQILPGSQMTIACNA-TGIPLPQVKWIKAGNYEIDPSRV-DADGNHAQFSLQVANITED--TTFNCVAQNPLGHANW 1899
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVkHDNGRTTQSSLLISNVTKEdaGTYTCVVNNPGGSATL 82

                    ....
gi 1831510791  1900 TINV 1903
Cdd:pfam00047    83 STSL 86
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1096-1196 2.00e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.44  E-value: 2.00e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGPIKSYTVyfapEYDDSDFKTWQRISVDAPdgaDHGEVTLPKeqFNPNTPYKI 1175
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV----EYREKGSGDWKEVEVTPG---SETSYTLTG--LKPGTEYEF 72
                            90       100
                    ....*....|....*....|.
gi 1831510791  1176 RISATNDLSEGPASDPVRFET 1196
Cdd:cd00063      73 RVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
581-675 2.27e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.05  E-value: 2.27e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   581 PSAPERIR-YQIDGDKVTLQWEPPQITNGPMAGYDVFYTEDPSlprDQWKVHHIDDPNARTTTVLRLNEKTPYTFVIVGR 659
Cdd:cd00063       1 PSPPTNLRvTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*.
gi 1831510791   660 NRLGPGLPSAPFTATT 675
Cdd:cd00063      78 NGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1701-1803 3.66e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 3.66e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1701 GPPVELRVEPDGQRSAVAQWKEPVTSDVPPIGYEIYYVRgdksveeddsAGLNDWIKISIDDPTKLTHKIQNlLLPDTDY 1780
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYRE----------KGSGDWKEVEVTPGSETSYTLTG-LKPGTEY 70
                            90       100
                    ....*....|....*....|...
gi 1831510791  1781 VFKMRAIYPDGPSVFSEPCIMKT 1803
Cdd:cd00063      71 EFRVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1287-1381 4.43e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 4.43e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1287 APNEIVLLPMPNQEINVEWTSPDEVNGQITNYIIHYGEISEDGSEPATWDQVTiardDVNHKLANLEPKKTYAIRVQAVS 1366
Cdd:cd00063       3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS----ETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1831510791  1367 DRGPGVISAPQVIKT 1381
Cdd:cd00063      79 GGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
396-471 2.09e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 2.09e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510791   396 SAPH-LKSASAGRTSLTVRWEPPSIINRPITTYTLYYTnnPQQPVKNWKKLEVKEPTREVAIPDLRPDTAYYIRVRA 471
Cdd:pfam00041     1 SAPSnLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
12363-12512 2.14e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 63.03  E-value: 2.14e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSEnftpdefvSM---------KDAVASIVDtgfDLAPDvSKIGFVIYSDKVAVPVALGhyeDKIELLEKITD 12433
Cdd:COG1240      94 DVVLVVDASG--------SMaaenrleaaKGALLDFLD---DYRPR-DRVGLVAFGGEAEVLLPLT---RDREALKRALD 158
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12434 AEKINDGVAIALyGLNAARQQFQLHgRENATKVVILITNGKN---RGNAAAAAEDLRDMyGVQLFAVAVGSNPEELATIK 12510
Cdd:COG1240     159 ELPPGGGTPLGD-ALALALELLKRA-DPARRKVIVLLTDGRDnagRIDPLEAAELAAAA-GIRIYTIGVGTEAVDEGLLR 235

                    ..
gi 1831510791 12511 RL 12512
Cdd:COG1240     236 EI 237
fn3 pfam00041
Fibronectin type III domain;
1300-1374 3.06e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 3.06e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791  1300 EINVEWTSPDEVNGQITNYIIHYGEISEdgsePATWDQVTIARDDVNHKLANLEPKKTYAIRVQAVSDRGPGVIS 1374
Cdd:pfam00041    15 SLTVSWTPPPDGNGPITGYEVEYRPKNS----GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
784-876 3.86e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.89  E-value: 3.86e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   784 SAPLGITPTPMH-TGFDVAWKPPKVTNGRITDYVVYYSKDPDaplSDWES-KTVPADTRNLTVNVDDEDTPYVVKVQART 861
Cdd:cd00063       2 SPPTNLRVTDVTsTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1831510791   862 DDGPGIISEAYEVTT 876
Cdd:cd00063      79 GGGESPPSESVTVTT 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
311-389 4.61e-09

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: 57.59  E-value: 4.61e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   311 PQGPYEVAPGGNINISCT-SVAYPFPDIYWFKNQKVNTDG----PDQNTLRASQILIIKEIYRNE-EFTCVSDNIHGSAN 384
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSaSTGSPGPDVTWSKEGGTLIESlkvkHDNGRTTQSSLLISNVTKEDAgTYTCVVNNPGGSAT 81

                    ....*
gi 1831510791   385 RTVSI 389
Cdd:pfam00047    82 LSTSL 86
EGF_CA smart00179
Calcium-binding EGF-like domain;
12972-13013 4.76e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 55.72  E-value: 4.76e-09
                             10        20        30        40
                     ....*....|....*....|....*....|....*....|....
gi 1831510791  12972 DIDECETNNGqCSEG--CVNTPGSYYCACPHGMMrdplDPFNCV 13013
Cdd:smart00179     1 DIDECASGNP-CQNGgtCVNTVGSYRCECPPGYT----DGRNCE 39
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
993-1079 5.13e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.24  E-value: 5.13e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    993 SAPQNPEVIVDPDNRVTITWQPPKYPNGeiTSYNVYITGDPSLPVDQWQVFPVDDvTDPKLVLQRgaLQPETPYFVKIAA 1072
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTP-SSTSYTLTG--LKPGTEYEFRVRA 76

                     ....*..
gi 1831510791   1073 VNPHGEG 1079
Cdd:smart00060    77 VNGAGEG 83
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
226-262 8.63e-09

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.94  E-value: 8.63e-09
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1831510791   226 CAADNGGCSHTCISyNDEKIECKCPRGMTLDVDEKTC 262
Cdd:pfam14670     1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
12972-13001 1.31e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.57  E-value: 1.31e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1831510791 12972 DIDECETNNGqCSEG--CVNTPGSYYCACPHG 13001
Cdd:cd00054       1 DIDECASGNP-CQNGgtCVNTVGSYRCSCPPG 31
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1585-1694 1.34e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.34e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1585 APENIQLTANKPTTISVQYEVPSIPNGNISKYIIYYTPLDDqdpdhqlgqvqtkpiSDWQNVhdmNDGVEGPRKVDIKDf 1664
Cdd:cd00063       3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---------------GDWKEV---EVTPGSETSYTLTG- 63
                            90       100       110
                    ....*....|....*....|....*....|
gi 1831510791  1665 VSTDTAYAVVVQAINDDGPGPYSNQYTIRT 1694
Cdd:cd00063      64 LKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
993-1079 1.72e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.72e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   993 SAPQNPEVIVDPDNRVTITWQPPKYPNGEITSYNVYITgdPSLPVDQWQVFPVDDVTDPklVLQRGaLQPETPYFVKIAA 1072
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTS--VTLTG-LKPGTEYEVRVQA 75

                    ....*..
gi 1831510791  1073 VNPHGEG 1079
Cdd:pfam00041    76 VNGGGEG 82
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
12976-13003 1.89e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.17  E-value: 1.89e-08
                            10        20
                    ....*....|....*....|....*...
gi 1831510791 12976 CETNNGQCSEGCVNTPGSYYCACPHGMM 13003
Cdd:pfam14670     1 CSVNNGGCSHLCLNTPGGYTCSCPEGYE 28
fn3 pfam00041
Fibronectin type III domain;
582-668 4.18e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 4.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   582 SAPERIR-YQIDGDKVTLQWEPPQITNGPMAGYDVFYTEDpslpRDQWKVHHIDDPNARTTTVLR-LNEKTPYTFVIVGR 659
Cdd:pfam00041     1 SAPSNLTvTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK----NSGEPWNEITVPGTTTSVTLTgLKPGTEYEVRVQAV 76

                    ....*....
gi 1831510791   660 NRLGPGLPS 668
Cdd:pfam00041    77 NGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
784-869 5.83e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 5.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   784 SAPLGITPTPM-HTGFDVAWKPPKVTNGRITDYVVYYSKDPDapLSDWESKTVPADTRNLTVNVDDEDTPYVVKVQARTD 862
Cdd:pfam00041     1 SAPSNLTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNS--GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1831510791   863 DGPGIIS 869
Cdd:pfam00041    79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2005-2097 8.92e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 8.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  2005 PKPPSDIRFGKNNDDEQIVDFKPAVASE-PIKEYTISVWPsTDPSNVKKFTTPADVTSGVVVDGLEPDTEYNVQVAAEFY 2083
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGgPITGYVVEYRE-KGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1831510791  2084 EGEELASEPVTVKT 2097
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1287-1371 9.07e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.77  E-value: 9.07e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1287 APNEIVLLPMPNQEINVEWTSPDEVNGqiTNYIIHYgeISEDGSEPATWDQVTIARDDVNHKLANLEPKKTYAIRVQAVS 1366
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGY--RVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1831510791   1367 DRGPG 1371
Cdd:smart00060    79 GAGEG 83
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
12150-12290 1.22e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 1.22e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLD-YRVMKELIKNFLTEhfnLRKhQVRVGLVKYGDGAEIPVSLGdyDNEDDLVHRISESrRLKGR 12228
Cdd:COG1240      93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDD---YRP-RDRVGLVAFGGEAEVLLPLT--RDREALKRALDEL-PPGGG 165
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510791 12229 AQLGAGLREALDELSISGVDGVPQIVLIvKNGKASDDYSSAVKSLK--AERNVTVFVVDAGDDE 12290
Cdd:COG1240     166 TPLGDALALALELLKRADPARRKVIVLL-TDGRDNAGRIDPLEAAElaAAAGIRIYTIGVGTEA 228
fn3 pfam00041
Fibronectin type III domain;
1096-1189 2.24e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.42  E-value: 2.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGPIKSYTVYFAPEyddSDFKTWQRISVDapdgADHGEVTLPKeqFNPNTPYKI 1175
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK---NSGEPWNEITVP----GTTTSVTLTG--LKPGTEYEV 71
                            90
                    ....*....|....
gi 1831510791  1176 RISATNDLSEGPAS 1189
Cdd:pfam00041    72 RVQAVNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
1585-1687 5.15e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.65  E-value: 5.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1585 APENIQLTANKPTTISVQYEVPSIPNGNISKYIIYYTPLDDQDPDHqlgqvqtkpisdWQNVhdmndgVEGPRKVDIKDF 1664
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWN------------EITV------PGTTTSVTLTGL 63
                            90       100
                    ....*....|....*....|...
gi 1831510791  1665 VsTDTAYAVVVQAINDDGPGPYS 1687
Cdd:pfam00041    64 K-PGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
581-665 6.22e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.46  E-value: 6.22e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    581 PSAPERIR-YQIDGDKVTLQWEPPQITNGpmAGYDVFYTEDPSLPRDQWKVHHiDDPNARTTTVLRLNEKTPYTFVIVGR 659
Cdd:smart00060     1 PSPPSNLRvTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1831510791    660 NRLGPG 665
Cdd:smart00060    78 NGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1824-1903 1.72e-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: 50.20  E-value: 1.72e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1824 STTIQILPGSQMTIACNATGIPLPQVKWIKAGNYEIDPS-RVDADGNHAQFSLQVANIT-EDT-TFNCVAQNPLGHANWT 1900
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESgRFSVSRSGSTSTLTISNVTpEDSgTYTCAATNSSGSASSG 80

                     ...
gi 1831510791   1901 INV 1903
Cdd:smart00410    81 TTL 83
VWA pfam00092
von Willebrand factor type A domain;
6583-6690 2.28e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 52.28  E-value: 2.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  6583 DIIFVLvnDGD---GAQNYDQFKKAVVGFSRKVDMSPDIIRLAVLSVGSEIAVPLPLGGYQEKEHLSSILNSFEIPPIVG 6659
Cdd:pfam00092     1 DIVFLL--DGSgsiGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGT 78
                            90       100       110
                    ....*....|....*....|....*....|....
gi 1831510791  6660 TEILSPVQ-AANQQFTSF--PRTGISKMVVIFAD 6690
Cdd:pfam00092    79 TNTGKALKyALENLFSSAagARPGAPKVVVLLTD 112
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
6583-6690 4.94e-06

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 51.14  E-value: 4.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  6583 DIIFVLVN-DGDGAQNYDQFKKAVVGFSRKVDMSPDIIRLAVLSVGSEIAVPLPLGGYQEKEHLSSILNSFEIPPIVGTE 6661
Cdd:cd01450       2 DIVFLLDGsESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1831510791  6662 ILSPVQAANQQF--TSFPRTGISKMVVIFAD 6690
Cdd:cd01450      82 TGKALQYALEQLfsESNARENVPKVIIVLTD 112
fn3 pfam00041
Fibronectin type III domain;
1701-1796 5.81e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.81e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1701 GPPVELRVEPDGQRSAVAQWKEPVTSDVPPIGYEIYYVRGDksveeddsaGLNDWIKISIdDPTKLTHKIQNlLLPDTDY 1780
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKN---------SGEPWNEITV-PGTTTSVTLTG-LKPGTEY 69
                            90
                    ....*....|....*.
gi 1831510791  1781 VFKMRAIYPDGPSVFS 1796
Cdd:pfam00041    70 EVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
784-866 5.83e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 5.83e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    784 SAPLGITPTPM-HTGFDVAWKPPKVTNGriTDYVVYYSKDPDAPLSDWESKTVPADTRNLTVNVDDEDTPYVVKVQARTD 862
Cdd:smart00060     2 SPPSNLRVTDVtSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1831510791    863 DGPG 866
Cdd:smart00060    80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1701-1793 7.90e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 7.90e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1701 GPPVELRVEPDGQRSAVAQWKEPvtSDVPPIGYEIYYVRGDKSVEEDdsaglndWIKISiDDPTKLTHKIQNLLlPDTDY 1780
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGSE-------WKEVN-VTPSSTSYTLTGLK-PGTEY 70
                             90
                     ....*....|...
gi 1831510791   1781 VFKMRAIYPDGPS 1793
Cdd:smart00060    71 EFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
2007-2080 7.94e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 7.94e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791  2007 PPSDIRFGKNNDDEQIVDFK-PAVASEPIKEYTISVWPSTDPSNVKKFTTPADVTSgVVVDGLEPDTEYNVQVAA 2080
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTpPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQA 75
VWA pfam00092
von Willebrand factor type A domain;
12596-12762 1.64e-05

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 49.58  E-value: 1.64e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12596 ILVDITSRASADEFRRVLDHLINFFnDRMRDEQHMITINIITVNSDkvQNILSNLRA----DQLSEQLNAITQQSDDTVS 12671
Cdd:pfam00092     4 FLLDGSGSIGGDNFEKVKEFLKKLV-ESLDIGPDGTRVGLVQYSSD--VRTEFPLNDysskEELLSAVDNLRYLGGGTTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12672 pkLGAGIDALAEL---SKENYINGAIKLMLIVgSDGTSSD-DALPAAEYAnSDFQHNIIAVSVRKPATDLLSKIAGLPT- 12746
Cdd:pfam00092    81 --TGKALKYALENlfsSAAGARPGAPKVVVLL-TDGRSQDgDPEEVAREL-KSAGVTVFAVGVGNADDEELRKIASEPGe 156
                           170
                    ....*....|....*..
gi 1831510791 12747 -RVVHLDQWSAPNELFD 12762
Cdd:pfam00092   157 gHVFTVSDFEALEDLQD 173
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1212-1281 1.78e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.11  E-value: 1.78e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1212 STYTVEPLGAATITCTATGVPQPKVHWIKANGETV------------DSATLQLYDLVKDTSA--TCVAENNAGKTQEAV 1277
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrsgSTSTLTISNVTPEDSGtyTCAATNSSGSASSGT 81

                     ....
gi 1831510791   1278 SIQV 1281
Cdd:smart00410    82 TLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1096-1186 2.00e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.84  E-value: 2.00e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGpiKSYTVYFAPEYDDSDfKTWQRISVDAPDgadhGEVTLPKeqFNPNTPYKI 1175
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEG-SEWKEVNVTPSS----TSYTLTG--LKPGTEYEF 72
                             90
                     ....*....|.
gi 1831510791   1176 RISATNDLSEG 1186
Cdd:smart00060    73 RVRAVNGAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
681-766 2.58e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 2.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   681 PPVVQLEPSEEMTKEpsNDEMIIECGAQGVPKPKIIWLWSGTLIEDGkeefrvydTTPTDAQDRTRSKLIAQSTTR--SG 758
Cdd:pfam13927     1 KPVITVSPSSVTVRE--GETVTLTCEATGSPPPTITWYKNGEPISSG--------STRSRSLSGSNSTLTISNVTRsdAG 70

                    ....*...
gi 1831510791   759 VATCQAVN 766
Cdd:pfam13927    71 TYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1202-1268 2.76e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 2.76e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1202 PPTITLDPSNSTYTVEplGAATITCTATGVPQPKVHWIKANGETVD-----------SATLQLYDLVKDTSA--TCVAEN 1268
Cdd:pfam13927     1 KPVITVSPSSVTVREG--ETVTLTCEATGSPPPTITWYKNGEPISSgstrsrslsgsNSTLTISNVTRSDAGtyTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1203-1281 2.99e-05

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.62  E-value: 2.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1203 PTITLDPSNSTyTVEPLGAATITCTATGVPQPKVHWIKaNGE---------TVDSATLQLYDLVKDTSA--TCVAENNAG 1271
Cdd:cd20978       1 PKFIQKPEKNV-VVKGGQDVTLPCQVTGVPQPKITWLH-NGKplqgpmeraTVEDGTLTIINVQPEDTGyyGCVATNEIG 78
                            90
                    ....*....|
gi 1831510791  1272 KTQEAVSIQV 1281
Cdd:cd20978      79 DIYTETLLHV 88
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
1828-1895 4.20e-05

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


Pssm-ID: 409401  Cd Length: 82  Bit Score: 46.05  E-value: 4.20e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510791  1828 QILPGSQMTIACNATGIPLPQVKWIKAGNyEIDPSRVDADGNHAqfsLQVANITEDTTFNCVAQNPLG 1895
Cdd:cd05739       8 EVMPGGSVNLTCVAVGAPMPYVKWMKGGE-ELTKEDEMPVGRNV---LELTNIYESANYTCVAISSLG 71
RhsA COG3209
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
5199-5943 2.03e-04

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 49.37  E-value: 2.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5199 DGSPLPTDNTGNYVLVPSDEGATEEKPTQGSESIVHPITKPDGTPLATDSTGSFVTDDDQVIAKDEDGKP-IGPDGQVLP 5277
Cdd:COG3209      23 AGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGyVGGAAAGGG 102
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5278 TDSSGNYIYPVIGPDGQALPTDESGKTVYPVRGPDGTPLSTDASGAVIGSDGKPIPTDETGLPLNKDGSPLPTDNDGNYI 5357
Cdd:COG3209     103 ATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPAT 182
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5358 LIPADESVVKALPTDEAKEVYPIVQPDGTPLATDSSGNfvtssGDIIDIDDEGKPLGPDGQALPTDDSGNYIYPVIGPDG 5437
Cdd:COG3209     183 GVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSA-----TTATGTALGTPASVAATVTGSATGAAGAGAAVATAAT 257
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5438 QALPTDESGKTVYPIRGPDGTPLPTDASGAVIGPDGEPIPTDASGKPLSQDGSPLPTDASGNYILVPSDGEVTKTLPTDD 5517
Cdd:COG3209     258 TLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTT 337
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5518 VGNVIYPITKPDGTPLATDSTGSFVTDDGQIIEKDDEGKPLGPDGQVLSTDDSGNYIYPAVGPNGQTIPTDDTGRTVYP- 5596
Cdd:COG3209     338 TGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDg 417
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5597 ---VRGPDGTPLPTDASGAVIGPDGEPIPTDASGKPLSADGSPLPTDNNGNYVIVPTDGSTVKSHPTDDSGNTIYPVVNE 5673
Cdd:COG3209     418 gpaTAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLG 497
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5674 DGTPLSTDLSGNFLTNSGEIVDRDDEGKPLGPDGQTLPTDASGNYVYLQKVEETTKPLPTDESGNIVYPITKPDGTPLAT 5753
Cdd:COG3209     498 TDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGG 577
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5754 DSTGSFVTEDGTVIEKDDEGKPVGPDGQVLPTDESGNYIYPDVTPDGQVQPTDVSGKPVYPVRGPDGSTLPTDASGAALG 5833
Cdd:COG3209     578 ASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGTTTT 657
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5834 PDGKPIPTDSNGVPLSEDGSPLPTDNQGNYVLVPTSETVTKSMPTDDNRNVIYPITMSDGSLLSTDSTGSFVTEDGKVIE 5913
Cdd:COG3209     658 RATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGT 737
                           730       740       750
                    ....*....|....*....|....*....|
gi 1831510791  5914 KDDEGKPLGPDGQVLPTDASGNYIYPVHGQ 5943
Cdd:COG3209     738 GGTTGTLTTTSTTTTTTAGALTYTYDALGR 767
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
311-391 2.15e-04

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


Pssm-ID: 409401  Cd Length: 82  Bit Score: 44.12  E-value: 2.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   311 PQGPYEVAPGGNINISCTSVAYPFPDIYWFKNQKVNTDGPDQNTLRasQILIIKEIYRNEEFTCVSDNIHGSANRTVSIV 390
Cdd:cd05739       3 PPSNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDEMPVGR--NVLELTNIYESANYTCVAISSLGMIEATAQVT 80

                    .
gi 1831510791   391 V 391
Cdd:cd05739      81 V 81
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
312-391 3.52e-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: 43.65  E-value: 3.52e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    312 QGPYEVAPGGNINISCTSVAYPFPDIYWFKN--QKVNTDG---PDQNTLRASqiLIIKEIYRNEE--FTCVSDNIHGSAN 384
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQggKLLAESGrfsVSRSGSTST--LTISNVTPEDSgtYTCAATNSSGSAS 78

                     ....*..
gi 1831510791    385 RTVSIVV 391
Cdd:smart00410    79 SGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
497-578 3.64e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.79  E-value: 3.64e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   497 VNIVEGDEIRvppmtafeIDCNVTrADPVPVLVWLHKGRPLNKGsktQHIKMKNGGVL-----------ESTQFSCVAEN 565
Cdd:pfam07679    10 VEVQEGESAR--------FTCTVT-GTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTytltisnvqpdDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1831510791   566 EAGKSTKKINVTV 578
Cdd:pfam07679    78 SAGEAEASAELTV 90
RhsA COG3209
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
11138-11861 5.91e-04

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 47.83  E-value: 5.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11138 SGKPIYPVFTEDGTQLPTDSTGFAIGPDGELVPTDSANGVPLSKDGSPLPTDASGNYILPDSGVTTANPTDENGYAIYPI 11217
Cdd:COG3209      37 LLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAG 116
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11218 TKPDGTLLATDSTGSYITQGGQLIEKDNTGKPIGPDGQVLPTDGSGNYVYPVVGPDGQALPTDDTGNVVYPVINADGSLL 11297
Cdd:COG3209     117 RLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPATGVGTGAVTLATGLA 196
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11298 ATDSSGSFITENGKIVAKDDEGKPISPDGQVLPTDASGNYIYPALGPDGSILPTDSNGKSIYPVRGPDGTPLPTDEFGFA 11377
Cdd:COG3209     197 GSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDA 276
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11378 IGPDGKPIPTDTSGKPLSADGSPLPTDNNGNYILVLSEGVTEHAPTDENGNVIYPVTNPDGTPLGTDSSGAFITQDGTVV 11457
Cdd:COG3209     277 STGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLT 356
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11458 KKDEDGKPIGPDGQVLPTDNSGNYIYPVIGPDGQVLPTDASGKTVHSVYGPDGTQLPTDASGSAIGPDGELVPTDVSGRP 11537
Cdd:COG3209     357 LGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTG 436
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11538 LSQDGSPLPTDNNGNYALVVSDEATTKVLPTDEGGNVIYHITKPDGSLLGTDASGDFITDHGKAVQKDDEGKPIGPDGSV 11617
Cdd:COG3209     437 TGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGA 516
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11618 LPTDTSGNYIYPITGPDGNVLPTDSNGKPVYPVFNEDGTQLPTDSTGSAIDQDGELVSTDSTSGVPLAKDGSPLPTNSAG 11697
Cdd:COG3209     517 RGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTT 596
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11698 NYVLVSSGKSQPTDEHGNVIYPITKPDGTLLATDSTGSYLTEDGQLVEIDDSGKPLGSDGQVLPIDASGNYIYPALGPDG 11777
Cdd:COG3209     597 TTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTL 676
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11778 QALPTDDAGNLVYPIVYPDGTPLATESTGNYVTENGEVVGKNTDGKPISPDGQVLPTDASGNYIYPAVGPDGQVLPT--- 11854
Cdd:COG3209     677 ATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTSTTTTTtag 756
                           730
                    ....*....|...
gi 1831510791 11855 ------DASGKLI 11861
Cdd:COG3209     757 altytyDALGRLT 769
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
517-578 1.39e-03

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 1.39e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510791   517 CNVTRADPVPVLVWLHKGRPLNKgSKTQHIKMKNG-----------GVLESTQFSCVAENEAGKSTKKINVTV 578
Cdd:cd05750      21 CEATSENPSPRYRWFKDGKELNR-KRPKNIKIRNKkknselqinkaKLEDSGEYTCVVENILGKDTVTGNVTV 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2005-2086 2.88e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.06  E-value: 2.88e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   2005 PKPPSDIRFGKNNDDEQIVDFKPaVASEPIKEYTISVWP--STDPSNVKKFTTPADVTSgVVVDGLEPDTEYNVQVAAEF 2082
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEP-PPDDGITGYIVGYRVeyREEGSEWKEVNVTPSSTS-YTLTGLKPGTEYEFRVRAVN 78

                     ....
gi 1831510791   2083 YEGE 2086
Cdd:smart00060    79 GAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1585-1684 8.98e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.52  E-value: 8.98e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1585 APENIQLTANKPTTISVQYEVPSIPNGNisKYIIYYTPLDDQDPDhqlgqvqtkpisDWQNVHdmndGVEGPRKVDIKDF 1664
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGS------------EWKEVN----VTPSSTSYTLTGL 64
                             90       100
                     ....*....|....*....|
gi 1831510791   1665 VStDTAYAVVVQAINDDGPG 1684
Cdd:smart00060    65 KP-GTEYEFRVRAVNGAGEG 83
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12363-12522 2.69e-26

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 109.30  E-value: 2.69e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKIN-DGV 12441
Cdd:cd01450       2 DIVFLLDGSESVGPENFEKVKDFIEKLVE-KLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGgGGT 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12442 AIALyGLNAARQQFQLHG--RENATKVVILITNGKN--RGNAAAAAEDLRDMyGVQLFAVAVGS-NPEELatiKRLVGNS 12516
Cdd:cd01450      81 NTGK-ALQYALEQLFSESnaRENVPKVIIVLTDGRSddGGDPKEAAAKLKDE-GIKVFVVGVGPaDEEEL---REIASCP 155

                    ....*.
gi 1831510791 12517 NTENVI 12522
Cdd:cd01450     156 SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
12363-12532 8.72e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.74  E-value: 8.72e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKINDGVA 12442
Cdd:pfam00092     1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVE-SLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12443 IALYGLNAARQQFQLH---GRENATKVVILITNGK-NRGNAAAAAEDLRDmYGVQLFAVAVGSN-PEELatiKRLVGNSN 12517
Cdd:pfam00092    80 NTGKALKYALENLFSSaagARPGAPKVVVLLTDGRsQDGDPEEVARELKS-AGVTVFAVGVGNAdDEEL---RKIASEPG 155
                           170
                    ....*....|....*
gi 1831510791 12518 TENVIEVAQSTEIDD 12532
Cdd:pfam00092   156 EGHVFTVSDFEALED 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
12363-12533 6.59e-20

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 91.36  E-value: 6.59e-20
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDTgFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKI-NDGV 12441
Cdd:smart00327     1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQ-LDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79
                             90       100       110       120       130       140       150       160
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12442 AIALyGLNAARQQF---QLHGRENATKVVILITNGK---NRGNAAAAAEDLRDmYGVQLFAVAVGSNPEElATIKRLVGN 12515
Cdd:smart00327    80 NLGA-ALQYALENLfskSAGSRRGAPKVVILITDGEsndGPKDLLKAAKELKR-SGVKVFVVGVGNDVDE-EELKKLASA 156
                            170
                     ....*....|....*...
gi 1831510791  12516 SNTENVIEVAQSTEIDDD 12533
Cdd:smart00327   157 PGGVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
12151-12302 2.85e-19

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 89.82  E-value: 2.85e-19
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  12151 DLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISE-SRRLKGRA 12229
Cdd:smart00327     1 DVVFLLDGSGSMGGNRFELAKEFVLKLV-EQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGT 79
                             90       100       110       120       130       140       150
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510791  12230 QLGAGLREALDEL---SISGVDGVPQIVLIVKNGKASD---DYSSAVKSLKaERNVTVFVVDAGDDESQQQNSELTEED 12302
Cdd:smart00327    80 NLGAALQYALENLfskSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELK-RSGVKVFVVGVGNDVDEEELKKLASAP 157
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12150-12296 2.25e-17

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 83.88  E-value: 2.25e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISESRRLKGRA 12229
Cdd:cd01450       1 LDIVFLLDGSESVGPENFEKVKDFIEKLV-EKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510791 12230 Q-LGAGLREALDELSISGVD--GVPQIVLIVKNGKASDDYSSAVKSLKA-ERNVTVFVVDAGDDESQQQNS 12296
Cdd:cd01450      80 TnTGKALQYALEQLFSESNAreNVPKVIIVLTDGRSDDGGDPKEAAAKLkDEGIKVFVVGVGPADEEELRE 150
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12363-12522 3.38e-17

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 83.38  E-value: 3.38e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDTgFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKINDG-V 12441
Cdd:cd00198       2 DIVFLLDVSGSMGGEKLDKAKEALKALVSS-LSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGgT 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12442 AIALyGLNAARQQFQLHGRENATKVVILITNGKN---RGNAAAAAEDLRDMyGVQLFAVAVGSNPEElATIKRLVGNSNT 12518
Cdd:cd00198      81 NIGA-ALRLALELLKSAKRPNARRVIILLTDGEPndgPELLAEAARELRKL-GITVYTIGIGDDANE-DELKEIADKTTG 157

                    ....
gi 1831510791 12519 ENVI 12522
Cdd:cd00198     158 GAVF 161
VWA pfam00092
von Willebrand factor type A domain;
12151-12293 5.76e-17

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 83.09  E-value: 5.76e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12151 DLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISE-SRRLKGRA 12229
Cdd:pfam00092     1 DIVFLLDGSGSIGGDNFEKVKEFLKKLV-ESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTT 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510791 12230 QLGAGLREALDEL---SISGVDGVPQIVLIVKNGKASD-DYSSAVKSLKaERNVTVFVVDAGDDESQQ 12293
Cdd:pfam00092    80 NTGKALKYALENLfssAAGARPGAPKVVVLLTDGRSQDgDPEEVARELK-SAGVTVFAVGVGNADDEE 146
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
12150-12302 1.07e-16

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 81.84  E-value: 1.07e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLDYRVMKELIKNFLTEhFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISESR-RLKGR 12228
Cdd:cd00198       1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSS-LSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGG 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510791 12229 AQLGAGLREALDELSISGVDGVPQIVLIVKNGKASDDYSSAVKSLKA--ERNVTVFVVDAGDDESQQQNSELTEED 12302
Cdd:cd00198      80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARElrKLGITVYTIGIGDDANEDELKEIADKT 155
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
12363-12509 2.11e-15

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 78.04  E-value: 2.11e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKINDGVA 12442
Cdd:cd01472       2 DIVFLVDGSESIGLSNFNLVKDFVKRVVE-RLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510791 12443 IALyGLNAARQQF---QLHGRENATKVVILITNGKNRGNAAAAAEDLRDMyGVQLFAVAVGS-NPEELATI 12509
Cdd:cd01472      81 TGK-ALKYVRENLfteASGSREGVPKVLVVITDGKSQDDVEEPAVELKQA-GIEVFAVGVKNaDEEELKQI 149
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
993-1089 1.32e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 73.30  E-value: 1.32e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   993 SAPQNPEVIVDPDNRVTITWQPPKYPNGEITSYNVYITGDPSlpvDQWQVFPVDDVTDPKLVLQRgaLQPETPYFVKIAA 1072
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEVEVTPGSETSYTLTG--LKPGTEYEFRVRA 76
                            90
                    ....*....|....*..
gi 1831510791  1073 VNPHGEGIHTDPKHFDT 1089
Cdd:cd00063      77 VNGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
394-478 4.79e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 65.71  E-value: 4.79e-12
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    394 PGSAPHLKSASAGRTSLTVRWEPPSiiNRPITTYTLYYTNNPQQPVKNWKKLEVKEPTREVAIPDLRPDTAYYIRVRAND 473
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEPPP--DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1831510791    474 PLGPG 478
Cdd:smart00060    79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
394-488 6.51e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.60  E-value: 6.51e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   394 PGSAPHLKSASAGRTSLTVRWEPPSIINRPITTYTLYYTNNPQQpvkNWKKLEVKEPTR-EVAIPDLRPDTAYYIRVRAN 472
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG---DWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*.
gi 1831510791   473 DPLGPGKLGNQVQIKT 488
Cdd:cd00063      78 NGGGESPPSESVTVTT 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
1824-1903 8.70e-12

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: 65.29  E-value: 8.70e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1824 STTIQILPGSQMTIACNA-TGIPLPQVKWIKAGNYEIDPSRV-DADGNHAQFSLQVANITED--TTFNCVAQNPLGHANW 1899
Cdd:pfam00047     3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVkHDNGRTTQSSLLISNVTKEdaGTYTCVVNNPGGSATL 82

                    ....
gi 1831510791  1900 TINV 1903
Cdd:pfam00047    83 STSL 86
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
12362-12509 1.07e-11

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 67.42  E-value: 1.07e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12362 SDVIIVLDSSENfTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYS--DKVAVPVALGHYEDKIELLEKITDAEKIND 12439
Cdd:cd01476       1 LDLLFVLDSSGS-VRGKFEKYKKYIERIVE-GLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGG 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510791 12440 GVAIALyGLNAARQQFQ-LHG-RENATKVVILITNGKNRGNAAAAAEDLRDMYGVQLFAVAVGSNP----EELATI 12509
Cdd:cd01476      79 TTATGA-AIEVALQQLDpSEGrREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPGtvdtEELHSI 153
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1096-1196 2.00e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.44  E-value: 2.00e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGPIKSYTVyfapEYDDSDFKTWQRISVDAPdgaDHGEVTLPKeqFNPNTPYKI 1175
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV----EYREKGSGDWKEVEVTPG---SETSYTLTG--LKPGTEYEF 72
                            90       100
                    ....*....|....*....|.
gi 1831510791  1176 RISATNDLSEGPASDPVRFET 1196
Cdd:cd00063      73 RVRAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
581-675 2.27e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.05  E-value: 2.27e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   581 PSAPERIR-YQIDGDKVTLQWEPPQITNGPMAGYDVFYTEDPSlprDQWKVHHIDDPNARTTTVLRLNEKTPYTFVIVGR 659
Cdd:cd00063       1 PSPPTNLRvTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
                            90
                    ....*....|....*.
gi 1831510791   660 NRLGPGLPSAPFTATT 675
Cdd:cd00063      78 NGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1701-1803 3.66e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 3.66e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1701 GPPVELRVEPDGQRSAVAQWKEPVTSDVPPIGYEIYYVRgdksveeddsAGLNDWIKISIDDPTKLTHKIQNlLLPDTDY 1780
Cdd:cd00063       2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYRE----------KGSGDWKEVEVTPGSETSYTLTG-LKPGTEY 70
                            90       100
                    ....*....|....*....|...
gi 1831510791  1781 VFKMRAIYPDGPSVFSEPCIMKT 1803
Cdd:cd00063      71 EFRVRAVNGGGESPPSESVTVTT 93
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
12363-12551 5.82e-11

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 67.02  E-value: 5.82e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDTgFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAEKINDGVA 12442
Cdd:cd01475       4 DLVFLIDSSRSVRPENFELVKQFLNQIIDS-LDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12443 IAL---YGLNAARQQFQ--LHGRENATKVVILITNGKNRGNAAAAAEDLRDMyGVQLFAVAVGSNPEElaTIKRLVGNSN 12517
Cdd:cd01475      83 TGLaiqYAMNNAFSEAEgaRPGSERVPRVGIVVTDGRPQDDVSEVAAKARAL-GIEMFAVGVGRADEE--ELREIASEPL 159
                           170       180       190
                    ....*....|....*....|....*....|....
gi 1831510791 12518 TENVIEVAQSTEIDDDAAALLKAVCGNTSPKNSE 12551
Cdd:cd01475     160 ADHVFYVEDFSTIEELTKKFQGKICVVPDLCATL 193
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
12151-12288 4.09e-10

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 62.80  E-value: 4.09e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12151 DLLLVIDSSNNIKVLdYRVMKELIKNfLTEHFNLRKHQVRVGLVKY-GDGAE-IPVSLGDYDNEDDLVHRISESRRLKGR 12228
Cdd:cd01476       2 DLLFVLDSSGSVRGK-FEKYKKYIER-IVEGLEIGPTATRVALITYsGRGRQrVRFNLPKHNDGEELLEKVDNLRFIGGT 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510791 12229 AQLGAGLREALDELSIS-GV-DGVPQIVLIVKNGKASDDYSSAVKSLKAERNVTVFVVDAGD 12288
Cdd:cd01476      80 TATGAAIEVALQQLDPSeGRrEGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGD 141
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1287-1381 4.43e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 4.43e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1287 APNEIVLLPMPNQEINVEWTSPDEVNGQITNYIIHYGEISEDGSEPATWDQVTiardDVNHKLANLEPKKTYAIRVQAVS 1366
Cdd:cd00063       3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGS----ETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1831510791  1367 DRGPGVISAPQVIKT 1381
Cdd:cd00063      79 GGGESPPSESVTVTT 93
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
12150-12292 7.83e-10

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 62.25  E-value: 7.83e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKvldyRVMKELIKNFLT---EHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDL---VHRIsesr 12223
Cdd:cd01472       1 ADIVFLVDGSESIG----LSNFNLVKDFVKrvvERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVleaVKNL---- 72
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510791 12224 RLKGRA-QLGAGLREALDEL--SISGV-DGVPQIVLIVKNGKASDDYSSAVKSLKAERNVTVFVVDAGDDESQ 12292
Cdd:cd01472      73 RYIGGGtNTGKALKYVRENLftEASGSrEGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEE 145
fn3 pfam00041
Fibronectin type III domain;
396-471 2.09e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.20  E-value: 2.09e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510791   396 SAPH-LKSASAGRTSLTVRWEPPSIINRPITTYTLYYTnnPQQPVKNWKKLEVKEPTREVAIPDLRPDTAYYIRVRA 471
Cdd:pfam00041     1 SAPSnLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
12363-12512 2.14e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 63.03  E-value: 2.14e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSEnftpdefvSM---------KDAVASIVDtgfDLAPDvSKIGFVIYSDKVAVPVALGhyeDKIELLEKITD 12433
Cdd:COG1240      94 DVVLVVDASG--------SMaaenrleaaKGALLDFLD---DYRPR-DRVGLVAFGGEAEVLLPLT---RDREALKRALD 158
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12434 AEKINDGVAIALyGLNAARQQFQLHgRENATKVVILITNGKN---RGNAAAAAEDLRDMyGVQLFAVAVGSNPEELATIK 12510
Cdd:COG1240     159 ELPPGGGTPLGD-ALALALELLKRA-DPARRKVIVLLTDGRDnagRIDPLEAAELAAAA-GIRIYTIGVGTEAVDEGLLR 235

                    ..
gi 1831510791 12511 RL 12512
Cdd:COG1240     236 EI 237
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
12362-12538 2.67e-09

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 60.83  E-value: 2.67e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12362 SDVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHY---EDKIELLEKITDAEkin 12438
Cdd:cd01469       1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMK-KLDIGPTKTQFGLVQYSESFRTEFTLNEYrtkEEPLSLVKHISQLL--- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12439 dGVAIALYGLNAARQQ---FQLHGRENATKVVILITNGKNRGNA-AAAAEDLRDMYGVQLFAVAVG---SNPEELATIKR 12511
Cdd:cd01469      77 -GLTNTATAIQYVVTElfsESNGARKDATKVLVVITDGESHDDPlLKDVIPQAEREGIIRYAIGVGghfQRENSREELKT 155
                           170       180
                    ....*....|....*....|....*..
gi 1831510791 12512 LVGNSNTENVIEVaqsteidDDAAALL 12538
Cdd:cd01469     156 IASKPPEEHFFNV-------TDFAALK 175
fn3 pfam00041
Fibronectin type III domain;
1300-1374 3.06e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 3.06e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791  1300 EINVEWTSPDEVNGQITNYIIHYGEISEdgsePATWDQVTIARDDVNHKLANLEPKKTYAIRVQAVSDRGPGVIS 1374
Cdd:pfam00041    15 SLTVSWTPPPDGNGPITGYEVEYRPKNS----GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
784-876 3.86e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.89  E-value: 3.86e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   784 SAPLGITPTPMH-TGFDVAWKPPKVTNGRITDYVVYYSKDPDaplSDWES-KTVPADTRNLTVNVDDEDTPYVVKVQART 861
Cdd:cd00063       2 SPPTNLRVTDVTsTSVTLSWTPPEDDGGPITGYVVEYREKGS---GDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                            90
                    ....*....|....*
gi 1831510791   862 DDGPGIISEAYEVTT 876
Cdd:cd00063      79 GGGESPPSESVTVTT 93
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
311-389 4.61e-09

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: 57.59  E-value: 4.61e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   311 PQGPYEVAPGGNINISCT-SVAYPFPDIYWFKNQKVNTDG----PDQNTLRASQILIIKEIYRNE-EFTCVSDNIHGSAN 384
Cdd:pfam00047     2 APPTVTVLEGDSATLTCSaSTGSPGPDVTWSKEGGTLIESlkvkHDNGRTTQSSLLISNVTKEDAgTYTCVVNNPGGSAT 81

                    ....*
gi 1831510791   385 RTVSI 389
Cdd:pfam00047    82 LSTSL 86
EGF_CA smart00179
Calcium-binding EGF-like domain;
12972-13013 4.76e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 55.72  E-value: 4.76e-09
                             10        20        30        40
                     ....*....|....*....|....*....|....*....|....
gi 1831510791  12972 DIDECETNNGqCSEG--CVNTPGSYYCACPHGMMrdplDPFNCV 13013
Cdd:smart00179     1 DIDECASGNP-CQNGgtCVNTVGSYRCECPPGYT----DGRNCE 39
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
993-1079 5.13e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 57.24  E-value: 5.13e-09
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    993 SAPQNPEVIVDPDNRVTITWQPPKYPNGeiTSYNVYITGDPSLPVDQWQVFPVDDvTDPKLVLQRgaLQPETPYFVKIAA 1072
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTP-SSTSYTLTG--LKPGTEYEFRVRA 76

                     ....*..
gi 1831510791   1073 VNPHGEG 1079
Cdd:smart00060    77 VNGAGEG 83
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
226-262 8.63e-09

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.94  E-value: 8.63e-09
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1831510791   226 CAADNGGCSHTCISyNDEKIECKCPRGMTLDVDEKTC 262
Cdd:pfam14670     1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
12150-12305 1.04e-08

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 59.29  E-value: 1.04e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLDYRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISESRRLKGRA 12229
Cdd:cd01469       1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVM-KKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12230 QLGAGLREALDEL---SISGVDGVPQIVLIVKNGKASDDY--SSAVKSLKAErNVTVFVVDAGDdesQQQNSELTEEDKT 12304
Cdd:cd01469      80 NTATAIQYVVTELfseSNGARKDATKVLVVITDGESHDDPllKDVIPQAERE-GIIRYAIGVGG---HFQRENSREELKT 155

                    .
gi 1831510791 12305 I 12305
Cdd:cd01469     156 I 156
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
12972-13001 1.31e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.57  E-value: 1.31e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1831510791 12972 DIDECETNNGqCSEG--CVNTPGSYYCACPHG 13001
Cdd:cd00054       1 DIDECASGNP-CQNGgtCVNTVGSYRCSCPPG 31
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
1585-1694 1.34e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.34e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1585 APENIQLTANKPTTISVQYEVPSIPNGNISKYIIYYTPLDDqdpdhqlgqvqtkpiSDWQNVhdmNDGVEGPRKVDIKDf 1664
Cdd:cd00063       3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGS---------------GDWKEV---EVTPGSETSYTLTG- 63
                            90       100       110
                    ....*....|....*....|....*....|
gi 1831510791  1665 VSTDTAYAVVVQAINDDGPGPYSNQYTIRT 1694
Cdd:cd00063      64 LKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
12363-12509 1.37e-08

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 58.45  E-value: 1.37e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDtGFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKITDAE----KIN 12438
Cdd:cd01482       2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVE-AFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPykggNTR 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791 12439 DGVAialygLNAARQQFQLHG---RENATKVVILITNGKNRGNAAAAAEDLRDMyGVQLFAVAV-GSNPEELATI 12509
Cdd:cd01482      81 TGKA-----LTHVREKNFTPDagaRPGVPKVVILITDGKSQDDVELPARVLRNL-GVNVFAVGVkDADESELKMI 149
fn3 pfam00041
Fibronectin type III domain;
993-1079 1.72e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.72e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   993 SAPQNPEVIVDPDNRVTITWQPPKYPNGEITSYNVYITgdPSLPVDQWQVFPVDDVTDPklVLQRGaLQPETPYFVKIAA 1072
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYR--PKNSGEPWNEITVPGTTTS--VTLTG-LKPGTEYEVRVQA 75

                    ....*..
gi 1831510791  1073 VNPHGEG 1079
Cdd:pfam00041    76 VNGGGEG 82
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
12976-13003 1.89e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 54.17  E-value: 1.89e-08
                            10        20
                    ....*....|....*....|....*...
gi 1831510791 12976 CETNNGQCSEGCVNTPGSYYCACPHGMM 13003
Cdd:pfam14670     1 CSVNNGGCSHLCLNTPGGYTCSCPEGYE 28
fn3 pfam00041
Fibronectin type III domain;
582-668 4.18e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.73  E-value: 4.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   582 SAPERIR-YQIDGDKVTLQWEPPQITNGPMAGYDVFYTEDpslpRDQWKVHHIDDPNARTTTVLR-LNEKTPYTFVIVGR 659
Cdd:pfam00041     1 SAPSNLTvTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK----NSGEPWNEITVPGTTTSVTLTgLKPGTEYEVRVQAV 76

                    ....*....
gi 1831510791   660 NRLGPGLPS 668
Cdd:pfam00041    77 NGGGEGPPS 85
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
12363-12535 4.19e-08

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 57.78  E-value: 4.19e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVD-----TGFDLAPDVSKIGFVIYSDKVAV-PVALGHYEDKIELLEKITDAEK 12436
Cdd:cd01480       4 DITFVLDSSESVGLQNFDITKNFVKRVAErflkdYYRKDPAGSWRVGVVQYSDQQEVeAGFLRDIRNYTSLKEAVDNLEY 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12437 INDGV----AIAlyglnAARQQFQLHGRENATKVVILITNGKNRGNAAAAAED---LRDMYGVQLFAVAVGS-NPEELAT 12508
Cdd:cd01480      84 IGGGTftdcALK-----YATEQLLEGSHQKENKFLLVITDGHSDGSPDGGIEKavnEADHLGIKIFFVAVGSqNEEPLSR 158
                           170       180
                    ....*....|....*....|....*...
gi 1831510791 12509 IKRLVGNS-NTENVIEVAQSTEIDDDAA 12535
Cdd:cd01480     159 IACDGKSAlYRENFAELLWSFFIDDETA 186
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
12148-12301 5.36e-08

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 58.17  E-value: 5.36e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12148 SHIDLLLVIDSSNNIKVLDYRVMKELIkNFLTEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISESRRLKG 12227
Cdd:cd01475       1 GPTDLVFLIDSSRSVRPENFELVKQFL-NQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLET 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12228 RAQLGAGLREALD------ELSISGVDGVPQIVLIVKNGKASDDYSSAVKSLKAeRNVTVFVVDAG---DDESQQQNSEL 12298
Cdd:cd01475      80 GTMTGLAIQYAMNnafseaEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARA-LGIEMFAVGVGradEEELREIASEP 158

                    ...
gi 1831510791 12299 TEE 12301
Cdd:cd01475     159 LAD 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
12151-12294 5.67e-08

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 56.56  E-value: 5.67e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12151 DLLLVIDSSNNIKVLDYRVMKELIKNfLTEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRIsESRRLKGRAQ 12230
Cdd:cd01481       2 DIVFLIDGSDNVGSGNFPAIRDFIER-IVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAV-RRLRLRGGSQ 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510791 12231 LGAGlrEALDEL------SISGV---DGVPQIVLIVKNGKASDDYSSAVKSLKAERNVTVFVVDAGDDESQQQ 12294
Cdd:cd01481      80 LNTG--SALDYVvknlftKSAGSrieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQ 150
fn3 pfam00041
Fibronectin type III domain;
784-869 5.83e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 5.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   784 SAPLGITPTPM-HTGFDVAWKPPKVTNGRITDYVVYYSKDPDapLSDWESKTVPADTRNLTVNVDDEDTPYVVKVQARTD 862
Cdd:pfam00041     1 SAPSNLTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNS--GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

                    ....*..
gi 1831510791   863 DGPGIIS 869
Cdd:pfam00041    79 GGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2005-2097 8.92e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 8.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  2005 PKPPSDIRFGKNNDDEQIVDFKPAVASE-PIKEYTISVWPsTDPSNVKKFTTPADVTSGVVVDGLEPDTEYNVQVAAEFY 2083
Cdd:cd00063       1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGgPITGYVVEYRE-KGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                            90
                    ....*....|....
gi 1831510791  2084 EGEELASEPVTVKT 2097
Cdd:cd00063      80 GGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1287-1371 9.07e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.77  E-value: 9.07e-08
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1287 APNEIVLLPMPNQEINVEWTSPDEVNGqiTNYIIHYgeISEDGSEPATWDQVTIARDDVNHKLANLEPKKTYAIRVQAVS 1366
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGY--RVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                     ....*
gi 1831510791   1367 DRGPG 1371
Cdd:smart00060    79 GAGEG 83
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
12150-12290 1.22e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 1.22e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLD-YRVMKELIKNFLTEhfnLRKhQVRVGLVKYGDGAEIPVSLGdyDNEDDLVHRISESrRLKGR 12228
Cdd:COG1240      93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDD---YRP-RDRVGLVAFGGEAEVLLPLT--RDREALKRALDEL-PPGGG 165
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510791 12229 AQLGAGLREALDELSISGVDGVPQIVLIvKNGKASDDYSSAVKSLK--AERNVTVFVVDAGDDE 12290
Cdd:COG1240     166 TPLGDALALALELLKRADPARRKVIVLL-TDGRDNAGRIDPLEAAElaAAAGIRIYTIGVGTEA 228
fn3 pfam00041
Fibronectin type III domain;
1096-1189 2.24e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.42  E-value: 2.24e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGPIKSYTVYFAPEyddSDFKTWQRISVDapdgADHGEVTLPKeqFNPNTPYKI 1175
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPK---NSGEPWNEITVP----GTTTSVTLTG--LKPGTEYEV 71
                            90
                    ....*....|....
gi 1831510791  1176 RISATNDLSEGPAS 1189
Cdd:pfam00041    72 RVQAVNGGGEGPPS 85
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
12363-12509 2.74e-07

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 54.64  E-value: 2.74e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSENFTPDEFVSMKDAVASIVDTgFDLAPDVSKIGFVIYSDKVAVPVALGHYEDKIELLEKI-----TDAEKI 12437
Cdd:cd01481       2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQS-LDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVrrlrlRGGSQL 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510791 12438 NDGVAIALYGLNAARQQFQLHGRENATKVVILITNGKNRGNAAAAAEDLRDmYGVQLFAVAV-GSNPEELATI 12509
Cdd:cd01481      81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKR-AGIVPFAIGArNADLAELQQI 152
fn3 pfam00041
Fibronectin type III domain;
1585-1687 5.15e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.65  E-value: 5.15e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1585 APENIQLTANKPTTISVQYEVPSIPNGNISKYIIYYTPLDDQDPDHqlgqvqtkpisdWQNVhdmndgVEGPRKVDIKDF 1664
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWN------------EITV------PGTTTSVTLTGL 63
                            90       100
                    ....*....|....*....|...
gi 1831510791  1665 VsTDTAYAVVVQAINDDGPGPYS 1687
Cdd:pfam00041    64 K-PGTEYEVRVQAVNGGGEGPPS 85
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
12151-12284 5.33e-07

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 53.83  E-value: 5.33e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12151 DLLLVIDSSNNIKvldyRVMKELIKNFL---TEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYDNEDDLVHRISESRRLKG 12227
Cdd:cd01482       2 DIVFLVDGSWSIG----RSNFNLVRSFLssvVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG 77
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12228 RAQLGAGLREALDEL--SISGV-DGVPQIVLIVKNGKASDDYSSAVKSLKAErNVTVFVV 12284
Cdd:cd01482      78 NTRTGKALTHVREKNftPDAGArPGVPKVVILITDGKSQDDVELPARVLRNL-GVNVFAV 136
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
581-665 6.22e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.46  E-value: 6.22e-07
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    581 PSAPERIR-YQIDGDKVTLQWEPPQITNGpmAGYDVFYTEDPSLPRDQWKVHHiDDPNARTTTVLRLNEKTPYTFVIVGR 659
Cdd:smart00060     1 PSPPSNLRvTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVN-VTPSSTSYTLTGLKPGTEYEFRVRAV 77

                     ....*.
gi 1831510791    660 NRLGPG 665
Cdd:smart00060    78 NGAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
304-378 1.18e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.26  E-value: 1.18e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510791   304 PPRIYIEPQgPYEVAPGGNINISCTSVAYPFPDIYWFKNQKVNTDGPDQ--NTLRASQILIIKEIYRNEE--FTCVSDN 378
Cdd:pfam13927     1 KPVITVSPS-SVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRsrSLSGSNSTLTISNVTRSDAgtYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1824-1903 1.72e-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: 50.20  E-value: 1.72e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1824 STTIQILPGSQMTIACNATGIPLPQVKWIKAGNYEIDPS-RVDADGNHAQFSLQVANIT-EDT-TFNCVAQNPLGHANWT 1900
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESgRFSVSRSGSTSTLTISNVTpEDSgTYTCAATNSSGSASSG 80

                     ...
gi 1831510791   1901 INV 1903
Cdd:smart00410    81 TTL 83
VWA pfam00092
von Willebrand factor type A domain;
6583-6690 2.28e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 52.28  E-value: 2.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  6583 DIIFVLvnDGD---GAQNYDQFKKAVVGFSRKVDMSPDIIRLAVLSVGSEIAVPLPLGGYQEKEHLSSILNSFEIPPIVG 6659
Cdd:pfam00092     1 DIVFLL--DGSgsiGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGT 78
                            90       100       110
                    ....*....|....*....|....*....|....
gi 1831510791  6660 TEILSPVQ-AANQQFTSF--PRTGISKMVVIFAD 6690
Cdd:pfam00092    79 TNTGKALKyALENLFSSAagARPGAPKVVVLLTD 112
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
984-1278 3.53e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.01  E-value: 3.53e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   984 HVFIVNKPGSAPQNPEVIVDPDNRVTITWQPPkyPNGEITSYNVYITGDPSLPVDQwqvfpVDDVTDPKLVLQrgALQPE 1063
Cdd:COG3401     225 SVTTPTTPPSAPTGLTATADTPGSVTLSWDPV--TESDATGYRVYRSNSGDGPFTK-----VATVTTTSYTDT--GLTNG 295
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1064 TPYFVKIAAVNPHGEGIHTDPKHFDTVSGAPIDAPTDVLPSVSIDNTVNITWSPPTQPlgPIKSYTVYfapeYDDSDFKT 1143
Cdd:COG3401     296 TTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDA--DVTGYNVY----RSTSGGGT 369
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1144 WQRIsvdapdGADHGEVTLPKEQFNPNTPYKIRISATN-DLSEGPASDPVRFETGSGeiPPTITLDPSNSTYTVEPLGAA 1222
Cdd:COG3401     370 YTKI------AETVTTTSYTDTGLTPGTTYYYKVTAVDaAGNESAPSEEVSATTASA--ASGESLTASVDAVPLTDVAGA 441
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510791  1223 TITCTATGVPQPKVHWIKANGETVDSATLQLYDLVKDTSATCVAENNAGKTQEAVS 1278
Cdd:COG3401     442 TAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
6583-6690 4.94e-06

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 51.14  E-value: 4.94e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  6583 DIIFVLVN-DGDGAQNYDQFKKAVVGFSRKVDMSPDIIRLAVLSVGSEIAVPLPLGGYQEKEHLSSILNSFEIPPIVGTE 6661
Cdd:cd01450       2 DIVFLLDGsESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1831510791  6662 ILSPVQAANQQF--TSFPRTGISKMVVIFAD 6690
Cdd:cd01450      82 TGKALQYALEQLfsESNARENVPKVIIVLTD 112
fn3 pfam00041
Fibronectin type III domain;
1701-1796 5.81e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.81e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1701 GPPVELRVEPDGQRSAVAQWKEPVTSDVPPIGYEIYYVRGDksveeddsaGLNDWIKISIdDPTKLTHKIQNlLLPDTDY 1780
Cdd:pfam00041     1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKN---------SGEPWNEITV-PGTTTSVTLTG-LKPGTEY 69
                            90
                    ....*....|....*.
gi 1831510791  1781 VFKMRAIYPDGPSVFS 1796
Cdd:pfam00041    70 EVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
784-866 5.83e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 5.83e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    784 SAPLGITPTPM-HTGFDVAWKPPKVTNGriTDYVVYYSKDPDAPLSDWESKTVPADTRNLTVNVDDEDTPYVVKVQARTD 862
Cdd:smart00060     2 SPPSNLRVTDVtSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                     ....
gi 1831510791    863 DGPG 866
Cdd:smart00060    80 AGEG 83
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
12150-12287 6.71e-06

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 51.23  E-value: 6.71e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLD-YRVMKELIKNFLtEHFNLRKHQVRVGLVKYGDGAEIPVSLGDYD--NEDDLVHRISESRRL- 12225
Cdd:cd01471       1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFV-QNLNISPDEINLYLVTFSTNAKELIRLSSPNstNKDLALNAIRALLSLy 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510791 12226 --KGRAQLGAGLREALDELSIS--GVDGVPQIVLIVKNGKASDDYSS--AVKSLKaERNVTVFVVDAG 12287
Cdd:cd01471      80 ypNGSTNTTSALLVVEKHLFDTrgNRENAPQLVIIMTDGIPDSKFRTlkEARKLR-ERGVIIAVLGVG 146
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
12975-13013 6.82e-06

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 46.70  E-value: 6.82e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1831510791 12975 ECETNNGqCSEG--CVNTPGSYYCACPHGMMRDpldpFNCV 13013
Cdd:cd00053       1 ECAASNP-CSNGgtCVNTPGSYRCVCPPGYTGD----RSCE 36
VWA_2 pfam13519
von Willebrand factor type A domain;
12152-12256 7.40e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.83  E-value: 7.40e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12152 LLLVIDSSNNIKVLDYRV-MKELIKNFLTEHFNLRKHQvRVGLVKYGDGAEIPVSLGdyDNEDDLVHRISESRRLKGRAQ 12230
Cdd:pfam13519     1 LVFVLDTSGSMRNGDYGPtRLEAAKDAVLALLKSLPGD-RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGGGTN 77
                            90       100
                    ....*....|....*....|....*.
gi 1831510791 12231 LGAGLREALDELSISGVDGVPQIVLI 12256
Cdd:pfam13519    78 LAAALQLARAALKHRRKNQPRRIVLI 103
EGF_CA pfam07645
Calcium-binding EGF domain;
12972-13001 7.66e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 46.46  E-value: 7.66e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1831510791 12972 DIDECETNNGQCSEG--CVNTPGSYYCACPHG 13001
Cdd:pfam07645     1 DVDECATGTHNCPANtvCVNTIGSFECRCPDG 32
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1701-1793 7.90e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 7.90e-06
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1701 GPPVELRVEPDGQRSAVAQWKEPvtSDVPPIGYEIYYVRGDKSVEEDdsaglndWIKISiDDPTKLTHKIQNLLlPDTDY 1780
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGSE-------WKEVN-VTPSSTSYTLTGLK-PGTEY 70
                             90
                     ....*....|...
gi 1831510791   1781 VFKMRAIYPDGPS 1793
Cdd:smart00060    71 EFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
2007-2080 7.94e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 7.94e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791  2007 PPSDIRFGKNNDDEQIVDFK-PAVASEPIKEYTISVWPSTDPSNVKKFTTPADVTSgVVVDGLEPDTEYNVQVAA 2080
Cdd:pfam00041     2 APSNLTVTDVTSTSLTVSWTpPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTS-VTLTGLKPGTEYEVRVQA 75
EGF smart00181
Epidermal growth factor-like domain;
12975-13003 1.42e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 45.97  E-value: 1.42e-05
                             10        20        30
                     ....*....|....*....|....*....|
gi 1831510791  12975 ECETNNGqCSEG-CVNTPGSYYCACPHGMM 13003
Cdd:smart00181     1 ECASGGP-CSNGtCINTPGSYTCSCPPGYT 29
VWA pfam00092
von Willebrand factor type A domain;
12596-12762 1.64e-05

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 49.58  E-value: 1.64e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12596 ILVDITSRASADEFRRVLDHLINFFnDRMRDEQHMITINIITVNSDkvQNILSNLRA----DQLSEQLNAITQQSDDTVS 12671
Cdd:pfam00092     4 FLLDGSGSIGGDNFEKVKEFLKKLV-ESLDIGPDGTRVGLVQYSSD--VRTEFPLNDysskEELLSAVDNLRYLGGGTTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12672 pkLGAGIDALAEL---SKENYINGAIKLMLIVgSDGTSSD-DALPAAEYAnSDFQHNIIAVSVRKPATDLLSKIAGLPT- 12746
Cdd:pfam00092    81 --TGKALKYALENlfsSAAGARPGAPKVVVLL-TDGRSQDgDPEEVAREL-KSAGVTVFAVGVGNADDEELRKIASEPGe 156
                           170
                    ....*....|....*..
gi 1831510791 12747 -RVVHLDQWSAPNELFD 12762
Cdd:pfam00092   157 gHVFTVSDFEALEDLQD 173
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
1212-1281 1.78e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.11  E-value: 1.78e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1212 STYTVEPLGAATITCTATGVPQPKVHWIKANGETV------------DSATLQLYDLVKDTSA--TCVAENNAGKTQEAV 1277
Cdd:smart00410     2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrsgSTSTLTISNVTPEDSGtyTCAATNSSGSASSGT 81

                     ....
gi 1831510791   1278 SIQV 1281
Cdd:smart00410    82 TLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1096-1186 2.00e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.84  E-value: 2.00e-05
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1096 DAPTDVLPSVSIDNTVNITWSPPTQPLGpiKSYTVYFAPEYDDSDfKTWQRISVDAPDgadhGEVTLPKeqFNPNTPYKI 1175
Cdd:smart00060     2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEG-SEWKEVNVTPSS----TSYTLTG--LKPGTEYEF 72
                             90
                     ....*....|.
gi 1831510791   1176 RISATNDLSEG 1186
Cdd:smart00060    73 RVRAVNGAGEG 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
681-766 2.58e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 2.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   681 PPVVQLEPSEEMTKEpsNDEMIIECGAQGVPKPKIIWLWSGTLIEDGkeefrvydTTPTDAQDRTRSKLIAQSTTR--SG 758
Cdd:pfam13927     1 KPVITVSPSSVTVRE--GETVTLTCEATGSPPPTITWYKNGEPISSG--------STRSRSLSGSNSTLTISNVTRsdAG 70

                    ....*...
gi 1831510791   759 VATCQAVN 766
Cdd:pfam13927    71 TYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1202-1268 2.76e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 2.76e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1202 PPTITLDPSNSTYTVEplGAATITCTATGVPQPKVHWIKANGETVD-----------SATLQLYDLVKDTSA--TCVAEN 1268
Cdd:pfam13927     1 KPVITVSPSSVTVREG--ETVTLTCEATGSPPPTITWYKNGEPISSgstrsrslsgsNSTLTISNVTRSDAGtyTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
1203-1281 2.99e-05

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.62  E-value: 2.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1203 PTITLDPSNSTyTVEPLGAATITCTATGVPQPKVHWIKaNGE---------TVDSATLQLYDLVKDTSA--TCVAENNAG 1271
Cdd:cd20978       1 PKFIQKPEKNV-VVKGGQDVTLPCQVTGVPQPKITWLH-NGKplqgpmeraTVEDGTLTIINVQPEDTGyyGCVATNEIG 78
                            90
                    ....*....|
gi 1831510791  1272 KTQEAVSIQV 1281
Cdd:cd20978      79 DIYTETLLHV 88
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
1828-1895 4.20e-05

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


Pssm-ID: 409401  Cd Length: 82  Bit Score: 46.05  E-value: 4.20e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510791  1828 QILPGSQMTIACNATGIPLPQVKWIKAGNyEIDPSRVDADGNHAqfsLQVANITEDTTFNCVAQNPLG 1895
Cdd:cd05739       8 EVMPGGSVNLTCVAVGAPMPYVKWMKGGE-ELTKEDEMPVGRNV---LELTNIYESANYTCVAISSLG 71
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1836-1895 4.76e-05

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 45.40  E-value: 4.76e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510791  1836 TIACNATGIPLPQVKWIKAGNYEIDPSRVDADGNHAQFSLQVANIT-EDT-TFNCVAQNPLG 1895
Cdd:cd00096       2 TLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTlEDSgTYTCVASNSAG 63
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
1810-1892 5.42e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.63  E-value: 5.42e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1810 PYIQIStgdngvegSTTIQILPGSQMTIACNATGIPLPQVKWIKAGNYEIDPSRVDADGNHAQFSLQVANIT-EDT-TFN 1887
Cdd:pfam13927     2 PVITVS--------PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTrSDAgTYT 73

                    ....*
gi 1831510791  1888 CVAQN 1892
Cdd:pfam13927    74 CVASN 78
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
1824-1903 9.25e-05

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 45.09  E-value: 9.25e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1824 STTIQILPGSQMTIACNATGIPLPQVKWIKAGNyEIDPSRVDADgnHAQFSLQVANITE--DTTFNCVAQNPLGHANWTI 1901
Cdd:cd05731       2 ESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGG-ELPKGRTKFE--NFNKTLKIENVSEadSGEYQCTASNTMGSARHTI 78

                    ..
gi 1831510791  1902 NV 1903
Cdd:cd05731      79 SV 80
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
6583-6692 1.04e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 47.18  E-value: 1.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  6583 DIIFVLvndgD-----GAQNYDQFKKAVVGFSRKVDMSPDIIRLAVLSVGSEIAVPLPLGGYQEKEHLSSILNSFEIPPI 6657
Cdd:cd00198       2 DIVFLL----DvsgsmGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG 77
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1831510791  6658 VGTEILSPVQAANQQFTSFPRTGISKMVVIFADNE 6692
Cdd:cd00198      78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGE 112
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
1202-1281 1.84e-04

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: 44.54  E-value: 1.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1202 PPTITLDPSNSTYTVEPLGAATITCTATGVPQPKVHWIKaNGETV-----------DSATLQLYDLVKDTSA--TCVAEN 1268
Cdd:cd05730       1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTK-DGEPIesgeekysfneDGSEMTILDVDKLDEAeyTCIAEN 79
                            90
                    ....*....|...
gi 1831510791  1269 NAGKTQEAVSIQV 1281
Cdd:cd05730      80 KAGEQEAEIHLKV 92
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
1824-1903 1.84e-04

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: 44.13  E-value: 1.84e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1824 STTIQILPGSQMTIACNATGIPLPQVKWIKAgNYEIDPSRVDAdGNHAQfSLQVANITE--DTTFNCVAQNPLGHANWTI 1901
Cdd:cd05876       2 SSSLVALRGQSLVLECIAEGLPTPTVKWLRP-SGPLPPDRVKY-QNHNK-TLQLLNVGEsdDGEYVCLAENSLGSARHAY 78

                    ..
gi 1831510791  1902 NV 1903
Cdd:cd05876      79 YV 80
RhsA COG3209
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
5199-5943 2.03e-04

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 49.37  E-value: 2.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5199 DGSPLPTDNTGNYVLVPSDEGATEEKPTQGSESIVHPITKPDGTPLATDSTGSFVTDDDQVIAKDEDGKP-IGPDGQVLP 5277
Cdd:COG3209      23 AGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGyVGGAAAGGG 102
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5278 TDSSGNYIYPVIGPDGQALPTDESGKTVYPVRGPDGTPLSTDASGAVIGSDGKPIPTDETGLPLNKDGSPLPTDNDGNYI 5357
Cdd:COG3209     103 ATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPAT 182
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5358 LIPADESVVKALPTDEAKEVYPIVQPDGTPLATDSSGNfvtssGDIIDIDDEGKPLGPDGQALPTDDSGNYIYPVIGPDG 5437
Cdd:COG3209     183 GVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSA-----TTATGTALGTPASVAATVTGSATGAAGAGAAVATAAT 257
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5438 QALPTDESGKTVYPIRGPDGTPLPTDASGAVIGPDGEPIPTDASGKPLSQDGSPLPTDASGNYILVPSDGEVTKTLPTDD 5517
Cdd:COG3209     258 TLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTT 337
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5518 VGNVIYPITKPDGTPLATDSTGSFVTDDGQIIEKDDEGKPLGPDGQVLSTDDSGNYIYPAVGPNGQTIPTDDTGRTVYP- 5596
Cdd:COG3209     338 TGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDg 417
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5597 ---VRGPDGTPLPTDASGAVIGPDGEPIPTDASGKPLSADGSPLPTDNNGNYVIVPTDGSTVKSHPTDDSGNTIYPVVNE 5673
Cdd:COG3209     418 gpaTAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLG 497
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5674 DGTPLSTDLSGNFLTNSGEIVDRDDEGKPLGPDGQTLPTDASGNYVYLQKVEETTKPLPTDESGNIVYPITKPDGTPLAT 5753
Cdd:COG3209     498 TDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGG 577
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5754 DSTGSFVTEDGTVIEKDDEGKPVGPDGQVLPTDESGNYIYPDVTPDGQVQPTDVSGKPVYPVRGPDGSTLPTDASGAALG 5833
Cdd:COG3209     578 ASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGTTTT 657
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  5834 PDGKPIPTDSNGVPLSEDGSPLPTDNQGNYVLVPTSETVTKSMPTDDNRNVIYPITMSDGSLLSTDSTGSFVTEDGKVIE 5913
Cdd:COG3209     658 RATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGT 737
                           730       740       750
                    ....*....|....*....|....*....|
gi 1831510791  5914 KDDEGKPLGPDGQVLPTDASGNYIYPVHGQ 5943
Cdd:COG3209     738 GGTTGTLTTTSTTTTTTAGALTYTYDALGR 767
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
311-391 2.15e-04

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


Pssm-ID: 409401  Cd Length: 82  Bit Score: 44.12  E-value: 2.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   311 PQGPYEVAPGGNINISCTSVAYPFPDIYWFKNQKVNTDGPDQNTLRasQILIIKEIYRNEEFTCVSDNIHGSANRTVSIV 390
Cdd:cd05739       3 PPSNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDEMPVGR--NVLELTNIYESANYTCVAISSLGMIEATAQVT 80

                    .
gi 1831510791   391 V 391
Cdd:cd05739      81 V 81
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
317-391 3.37e-04

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.60  E-value: 3.37e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510791   317 VAPGGNINISCTSVAYPFPDIYWFKNQKVNTDGPDQnTLRASQILIIKEIYRNEE--FTCVSDNIHGSANRTVSIVV 391
Cdd:cd04969      14 AAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRI-CILPDGSLKIKNVTKSDEgkYTCFAVNFFGKANSTGSLSV 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
312-391 3.52e-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: 43.65  E-value: 3.52e-04
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791    312 QGPYEVAPGGNINISCTSVAYPFPDIYWFKN--QKVNTDG---PDQNTLRASqiLIIKEIYRNEE--FTCVSDNIHGSAN 384
Cdd:smart00410     1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQggKLLAESGrfsVSRSGSTST--LTISNVTPEDSgtYTCAATNSSGSAS 78

                     ....*..
gi 1831510791    385 RTVSIVV 391
Cdd:smart00410    79 SGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
497-578 3.64e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.79  E-value: 3.64e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   497 VNIVEGDEIRvppmtafeIDCNVTrADPVPVLVWLHKGRPLNKGsktQHIKMKNGGVL-----------ESTQFSCVAEN 565
Cdd:pfam07679    10 VEVQEGESAR--------FTCTVT-GTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTytltisnvqpdDSGKYTCVATN 77
                            90
                    ....*....|...
gi 1831510791   566 EAGKSTKKINVTV 578
Cdd:pfam07679    78 SAGEAEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1222-1276 3.69e-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: 43.09  E-value: 3.69e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510791  1222 ATITCTATGVPQPKVHWIKANGE-----------TVDSATLQLYDLVKDTSA--TCVAENNAGKTQEA 1276
Cdd:cd00096       1 VTLTCSASGNPPPTITWYKNGKPlppssrdsrrsELGNGTLTISNVTLEDSGtyTCVASNSAGGSASA 68
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
12363-12502 5.08e-04

VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 45.40  E-value: 5.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12363 DVIIVLDSSEN------FTPDEFVSMKDAVASIVDTgfdlaPDVSKIGFVIYSDKvAVPVA--LGHYEDKIELLE--KIT 12432
Cdd:cd01467       4 DIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFIDR-----RENDRIGLVVFAGA-AFTQAplTLDRESLKELLEdiKIG 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791 12433 DAEK---INDGVAIALYGLNAARQQfqlhgrenaTKVVILITNGKNRGNAA--AAAEDLRDMYGVQLFAVAVGSN 12502
Cdd:cd01467      78 LAGQgtaIGDAIGLAIKRLKNSEAK---------ERVIVLLTDGENNAGEIdpATAAELAKNKGVRIYTIGVGKS 143
RhsA COG3209
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
11138-11861 5.91e-04

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 47.83  E-value: 5.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11138 SGKPIYPVFTEDGTQLPTDSTGFAIGPDGELVPTDSANGVPLSKDGSPLPTDASGNYILPDSGVTTANPTDENGYAIYPI 11217
Cdd:COG3209      37 LLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAG 116
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11218 TKPDGTLLATDSTGSYITQGGQLIEKDNTGKPIGPDGQVLPTDGSGNYVYPVVGPDGQALPTDDTGNVVYPVINADGSLL 11297
Cdd:COG3209     117 RLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPATGVGTGAVTLATGLA 196
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11298 ATDSSGSFITENGKIVAKDDEGKPISPDGQVLPTDASGNYIYPALGPDGSILPTDSNGKSIYPVRGPDGTPLPTDEFGFA 11377
Cdd:COG3209     197 GSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDA 276
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11378 IGPDGKPIPTDTSGKPLSADGSPLPTDNNGNYILVLSEGVTEHAPTDENGNVIYPVTNPDGTPLGTDSSGAFITQDGTVV 11457
Cdd:COG3209     277 STGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLT 356
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11458 KKDEDGKPIGPDGQVLPTDNSGNYIYPVIGPDGQVLPTDASGKTVHSVYGPDGTQLPTDASGSAIGPDGELVPTDVSGRP 11537
Cdd:COG3209     357 LGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTG 436
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11538 LSQDGSPLPTDNNGNYALVVSDEATTKVLPTDEGGNVIYHITKPDGSLLGTDASGDFITDHGKAVQKDDEGKPIGPDGSV 11617
Cdd:COG3209     437 TGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGA 516
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11618 LPTDTSGNYIYPITGPDGNVLPTDSNGKPVYPVFNEDGTQLPTDSTGSAIDQDGELVSTDSTSGVPLAKDGSPLPTNSAG 11697
Cdd:COG3209     517 RGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTT 596
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11698 NYVLVSSGKSQPTDEHGNVIYPITKPDGTLLATDSTGSYLTEDGQLVEIDDSGKPLGSDGQVLPIDASGNYIYPALGPDG 11777
Cdd:COG3209     597 TTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTL 676
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 11778 QALPTDDAGNLVYPIVYPDGTPLATESTGNYVTENGEVVGKNTDGKPISPDGQVLPTDASGNYIYPAVGPDGQVLPT--- 11854
Cdd:COG3209     677 ATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTSTTTTTtag 756
                           730
                    ....*....|...
gi 1831510791 11855 ------DASGKLI 11861
Cdd:COG3209     757 altytyDALGRLT 769
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
1206-1282 7.76e-04

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


Pssm-ID: 409401  Cd Length: 82  Bit Score: 42.58  E-value: 7.76e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1206 TLDPSNSTytVEPLGAATITCTATGVPQPKVHWIKANGE-------TVDSATLQLYDLVKDTSATCVAENNAGkTQEAVS 1278
Cdd:cd05739       1 SIPPSNHE--VMPGGSVNLTCVAVGAPMPYVKWMKGGEEltkedemPVGRNVLELTNIYESANYTCVAISSLG-MIEATA 77

                    ....
gi 1831510791  1279 iQVT 1282
Cdd:cd05739      78 -QVT 80
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
1832-1900 9.15e-04

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: 42.48  E-value: 9.15e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510791  1832 GSQMTIACNATGIPLPQVKWIKAGNYE-IDPSRVDADGNHaqfSLQVANI-TEDT-TFNCVAQNPLGHANWT 1900
Cdd:cd20952      14 GGTVVLNCQATGEPVPTISWLKDGVPLlGKDERITTLENG---SLQIKGAeKSDTgEYTCVALNLSGEATWS 82
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
517-578 1.39e-03

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.11  E-value: 1.39e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510791   517 CNVTRADPVPVLVWLHKGRPLNKgSKTQHIKMKNG-----------GVLESTQFSCVAENEAGKSTKKINVTV 578
Cdd:cd05750      21 CEATSENPSPRYRWFKDGKELNR-KRPKNIKIRNKkknselqinkaKLEDSGEYTCVVENILGKDTVTGNVTV 92
I-set pfam07679
Immunoglobulin I-set domain;
1827-1895 1.61e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.86  E-value: 1.61e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510791  1827 IQILPGSQMTIACNATGIPLPQVKWIKAGNyEIDPS---RVDADGNHAQFSLQVANITEDTTFNCVAQNPLG 1895
Cdd:pfam07679    10 VEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSdrfKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
1222-1281 1.65e-03

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


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 41.69  E-value: 1.65e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510791  1222 ATITCTATGVPQPKVHWIKANGETV---------DSATLQ-LYDLVKDTSA-TCVAENNAGKTQEAVSIQV 1281
Cdd:cd05764      18 ATLRCKARGDPEPAIHWISPEGKLIsnssrtlvyDNGTLDiLITTVKDTGAfTCIASNPAGEATARVELHI 88
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
1825-1905 2.29e-03

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: 41.47  E-value: 2.29e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1825 TTIQILPGSQMTIACNATGIPLPQVKWIKAG-NYEIDPSRVDADGNHAQFSLQVANITEDTTFNCVAQNPLGHANWTINV 1903
Cdd:cd20976       9 KDLEAVEGQDFVAQCSARGKPVPRITWIRNAqPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWV 88

                    ..
gi 1831510791  1904 NL 1905
Cdd:cd20976      89 TV 90
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
304-391 2.37e-03

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 41.40  E-value: 2.37e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   304 PPriYIEPQGPYEVAPGGNINISCTSVAYPFPDIYWFKN---------QKVNTDGpdqntlrasqILIIKEIYRNE---E 371
Cdd:cd20958       1 PP--FIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDgrrlplnhrQRVFPNG----------TLVIENVQRSSdegE 68
                            90       100
                    ....*....|....*....|.
gi 1831510791   372 FTCVSDNIHG-SANRTVSIVV 391
Cdd:cd20958      69 YTCTARNQQGqSASRSVFVKV 89
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
2005-2086 2.88e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.06  E-value: 2.88e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   2005 PKPPSDIRFGKNNDDEQIVDFKPaVASEPIKEYTISVWP--STDPSNVKKFTTPADVTSgVVVDGLEPDTEYNVQVAAEF 2082
Cdd:smart00060     1 PSPPSNLRVTDVTSTSVTLSWEP-PPDDGITGYIVGYRVeyREEGSEWKEVNVTPSSTS-YTLTGLKPGTEYEFRVRAVN 78

                     ....
gi 1831510791   2083 YEGE 2086
Cdd:smart00060    79 GAGE 82
I-set pfam07679
Immunoglobulin I-set domain;
1221-1281 3.10e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.09  E-value: 3.10e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791  1221 AATITCTATGVPQPKVHWIKaNGETV------------DSATLQLYDLVKDTSA--TCVAENNAGKTQEAVSIQV 1281
Cdd:pfam07679    17 SARFTCTVTGTPDPEVSWFK-DGQPLrssdrfkvtyegGTYTLTISNVQPDDSGkyTCVATNSAGEAEASAELTV 90
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
514-578 4.55e-03

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 40.45  E-value: 4.55e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510791   514 EIDCNVTrADPVPVLVWLHKGRPLNKGSKTQHIKmKNGGVLESTQ------FSCVAENEAGKSTKKINVTV 578
Cdd:cd20978      20 TLPCQVT-GVPQPKITWLHNGKPLQGPMERATVE-DGTLTIINVQpedtgyYGCVATNEIGDIYTETLLHV 88
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
12150-12293 5.09e-03

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 42.76  E-value: 5.09e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791 12150 IDLLLVIDSSNNIKVLDY----RVMKELIKNFLT-EHFNLRKHQVRVGLVKYGDGAE-IPVSLGDYDNEDDLVHRISESR 12223
Cdd:cd01480       3 VDITFVLDSSESVGLQNFditkNFVKRVAERFLKdYYRKDPAGSWRVGVVQYSDQQEvEAGFLRDIRNYTSLKEAVDNLE 82
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510791 12224 RLKGRAQLGAGLREALDELSISGVDGVPQIVLIVKNGKAsdDYSSAVKSLKA-----ERNVTVFVVDAGDDESQQ 12293
Cdd:cd01480      83 YIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHS--DGSPDGGIEKAvneadHLGIKIFFVAVGSQNEEP 155
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
1210-1281 6.95e-03

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 39.89  E-value: 6.95e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791  1210 SNSTYTVEPLGAATITCTATGVPQPKVHWIKANGETV--------DSATLQLYDLVK--DTSATCVAENNAGKTQEAVSI 1279
Cdd:cd05876       1 SSSSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPpdrvkyqnHNKTLQLLNVGEsdDGEYVCLAENSLGSARHAYYV 80

                    ..
gi 1831510791  1280 QV 1281
Cdd:cd05876      81 TV 82
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
523-578 7.21e-03

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.79  E-value: 7.21e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510791   523 DPVPVLVWLHKGRPLNkgSKTQHIKMKNGGVLE--------STQFSCVAENEAGKSTKKINVTV 578
Cdd:cd20952      26 EPVPTISWLKDGVPLL--GKDERITTLENGSLQikgaeksdTGEYTCVALNLSGEATWSAVLDV 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
304-391 7.49e-03

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: 39.87  E-value: 7.49e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   304 PPRIYIEPQGpYEVAPGGNINISCTSVAYPFPDIYWFKNQKVNTDGPDQNTLRASQI--LIIKEIYRNE--EFTCVSDNI 379
Cdd:cd20972       1 PPQFIQKLRS-QEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLhsLIIAEAFEEDtgRYSCLATNS 79
                            90
                    ....*....|..
gi 1831510791   380 HGSANRTVSIVV 391
Cdd:cd20972      80 VGSDTTSAEIFV 91
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
12970-13001 8.44e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 42.37  E-value: 8.44e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1831510791 12970 CYDIDECETNNGQCSEGCVNTPGSYYCACPHG 13001
Cdd:cd01475     184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEG 215
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
1585-1684 8.98e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.52  E-value: 8.98e-03
                             10        20        30        40        50        60        70        80
                     ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510791   1585 APENIQLTANKPTTISVQYEVPSIPNGNisKYIIYYTPLDDQDPDhqlgqvqtkpisDWQNVHdmndGVEGPRKVDIKDF 1664
Cdd:smart00060     3 PPSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGS------------EWKEVN----VTPSSTSYTLTGL 64
                             90       100
                     ....*....|....*....|
gi 1831510791   1665 VStDTAYAVVVQAINDDGPG 1684
Cdd:smart00060    65 KP-GTEYEFRVRAVNGAGEG 83
 
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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