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Conserved domains on  [gi|1953347750|ref|XP_038293652|]
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von Willebrand factor isoform X1 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 381-544 1.11e-47

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 168.73  E-value: 1.11e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   381 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDH-TFSVVIETVQCADDldAVCTRSVTVRLPGhhNSL 459
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPCGGG--ATCLKSVKVELNG--DEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   460 VKLKHGGGVSMDGQDIQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRG 536
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1953347750   537 DDFVTPAG 544
Cdd:smart00216  156 DDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 860-1015 3.21e-41

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 150.24  E-value: 3.21e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   860 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 939
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   940 LFDGEV-------NVKKPMKDETHFEVVES-GQYVILLLGKAL-SVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNND 1010
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 1953347750  1011 FTSSS 1015
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1695-1864 1.44e-40

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 1.44e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVD-LMQQEGGPSQ 1773
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1774 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD--VSVDSVDAAAEAARSNRVTVFPIGIGDRYsEAQLSSLAGPKAGSN 1851
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTDgrSQDGDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 1953347750 1852 MVRLQRIEDLPTV 1864
Cdd:pfam00092  159 VFTVSDFEALEDL 171
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1202-1280 4.46e-39

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


:

Pssm-ID: 465038  Cd Length: 79  Bit Score: 140.89  E-value: 4.46e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953347750 1202 VCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLL 1280
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1502-1647 5.30e-39

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.34  E-value: 5.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1581
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750 1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPHANvQELEKIG 1647
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGNADD-EELRKIA 151
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1954-2106 7.43e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.50  E-value: 7.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1954 CMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGR 2031
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2032 LVSIPYVGGDMEVNVYGTIMYEVRFnHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGT 2106
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 39-183 9.65e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.12  E-value: 9.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   39 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVSLIGGFQNGK-----RVSLSVYLGEFFdIHLFVNGTMLQGT 110
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  111 QSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGT 183
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1281-1453 1.00e-25

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: 106.38  E-value: 1.00e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1360
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1361 TSEVLKYTLFQIFGKID--RPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPE 1438
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 1953347750  1439 NKAFVFSGVDELEQR 1453
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1057-1131 1.19e-21

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 90.86  E-value: 1.19e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750  1057 QTMVDSSCRILTSD--IFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFCP 1131
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 226-296 1.04e-18

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 82.39  E-value: 1.04e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953347750   226 WEQCQLLKSAS-VFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGIVLYGWTDHSVCR 296
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2731-2812 2.86e-18

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


:

Pssm-ID: 214482  Cd Length: 82  Bit Score: 81.68  E-value: 2.86e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  2731 IIAKLQRVKVGDCKSEEeVDIHYCEGKCASKAVYSIhmEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRC 2810
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 1953347750  2811 SP 2812
Cdd:smart00041   78 EP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 656-711 2.53e-13

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 66.57  E-value: 2.53e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750  656 CPQGQVYLQCGTPCNMTCRSLSYPEeDCNEVCLEGCFCPPGLYLDERGDCVPKAQC 711
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 299-352 2.63e-12

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 2.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  299 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDE-GHCVGSAEC 352
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 583-653 8.19e-12

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 63.13  E-value: 8.19e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750   583 FAEEACALLTSSK--FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHI-AWREPGFCA 653
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2142-2203 6.91e-11

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


:

Pssm-ID: 462584  Cd Length: 68  Bit Score: 60.09  E-value: 6.91e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 2142 HCQVLL-SELFAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFC 2203
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGddecLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1150-1200 5.14e-08

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.55  E-value: 5.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1150 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1200
Cdd:cd19941      7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2435-2498 2.90e-07

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


:

Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 2.90e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2435 CVHRGTIYPVGQFWEEA-CDVCTCTDledsvmglRVAQCSQKPCEDNCLSGFTYVLHEGECCGRC 2498
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2265-2325 6.87e-07

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.28  E-value: 6.87e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953347750  2265 DGVRHQFLETWVPAhqPCQICTCLSGRKVNCTLQPCPTARaptcgPCEVARLRQNAEQCCP 2325
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2586-2648 3.50e-06

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam00093:

Pssm-ID: 450195  Cd Length: 57  Bit Score: 46.26  E-value: 3.50e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2586 CLLNGTIIGPGKSLMIDVCTTCRCTVqvgvisgFKLECRKTTCEA--CPLGYkEEKNQGECCGRC 2648
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2207-2258 7.59e-05

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.69  E-value: 7.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2207 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVM-LEGSCVPEEAC 2258
Cdd:cd19941      1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 354-398 4.98e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member smart00215:

Pssm-ID: 450195  Cd Length: 67  Bit Score: 37.93  E-value: 4.98e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1953347750   354 CVHAGQRYPPGASLLQDCHTCICRNSLWICSNEEC-PGECLVTGQS 398
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 381-544 1.11e-47

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 168.73  E-value: 1.11e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   381 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDH-TFSVVIETVQCADDldAVCTRSVTVRLPGhhNSL 459
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPCGGG--ATCLKSVKVELNG--DEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   460 VKLKHGGGVSMDGQDIQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRG 536
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1953347750   537 DDFVTPAG 544
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 392-545 1.32e-47

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 167.93  E-value: 1.32e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  392 CLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDHT-FSVVIETVQCADDLDAVCTRSVTVRLPGHHnslVKLKHGGGVSM 470
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750  471 DGQDIQIPLLQGDLRIQHTV--MASVRLSYGEDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRGDDFVTPAGL 545
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 860-1015 3.21e-41

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 150.24  E-value: 3.21e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   860 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 939
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   940 LFDGEV-------NVKKPMKDETHFEVVES-GQYVILLLGKAL-SVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNND 1010
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 1953347750  1011 FTSSS 1015
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1695-1864 1.44e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 1.44e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVD-LMQQEGGPSQ 1773
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1774 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD--VSVDSVDAAAEAARSNRVTVFPIGIGDRYsEAQLSSLAGPKAGSN 1851
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTDgrSQDGDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 1953347750 1852 MVRLQRIEDLPTV 1864
Cdd:pfam00092  159 VFTVSDFEALEDL 171
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1202-1280 4.46e-39

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 140.89  E-value: 4.46e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953347750 1202 VCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLL 1280
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1502-1647 5.30e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.34  E-value: 5.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1581
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750 1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPHANvQELEKIG 1647
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGNADD-EELRKIA 151
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1501-1649 7.43e-39

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: 143.20  E-value: 7.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRT 1580
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 1581 NTGLALQYLSEHSFSVSQgDREQVPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANVQELEKIGWP 1649
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1954-2106 7.43e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.50  E-value: 7.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1954 CMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGR 2031
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2032 LVSIPYVGGDMEVNVYGTIMYEVRFnHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGT 2106
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 871-1015 8.59e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.12  E-value: 8.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  871 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFRILVGNEGCSYPSVkCKKRVTILVEGGEIELFDG---EVN 946
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750  947 VKK---PMK-DETHFEVVESGQ-YVILLLGKALSVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNNDFTSSS 1015
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 39-183 9.65e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.12  E-value: 9.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   39 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVSLIGGFQNGK-----RVSLSVYLGEFFdIHLFVNGTMLQGT 110
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  111 QSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGT 183
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1942-2105 6.29e-35

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.14  E-value: 6.29e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1942 ETCGCrWTCPCVCMGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHNGACSPGAkeTCMKSIEVKHDGLSVE 2019
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  2020 LHSD-MQMTVNGRLVSIPYVGGDMEVNVYGTIMYEVRFNHLGHI-FTFTPQNNeFQLQLSPRtFASKTYGLCGICDENGA 2097
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1953347750  2098 NDFILRDG 2105
Cdd:smart00216  156 DDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1502-1646 2.11e-33

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: 128.34  E-value: 2.11e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1581
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANVQELEKI 1646
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1695-1861 1.11e-32

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: 126.03  E-value: 1.11e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQE-GGPSQ 1773
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1774 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGpKAG 1849
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITDgesnDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLAS-APG 158

                           170
                    ....*....|..
gi 1953347750  1850 SNMVRLQRIEDL 1861
Cdd:smart00327  159 GVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1694-1847 8.23e-32

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: 123.17  E-value: 8.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGP-S 1772
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 1773 QIGDALSFAVRYVTSEvHGARPGASKaVVILVTDV---SVDSVDAAAEAARSNRVTVFPIGIGDrYSEAQLSSLAGPK 1847
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDGrsdDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCP 155
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 26-182 5.83e-30

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 117.89  E-value: 5.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750    26 CTKGTVGrssmARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVsLIGGFQNGKRVS--LSVYLGEFF-DIH 99
Cdd:smart00216    3 CTQEECS----PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEptfSV-LLKNVPCGGGATclKSVKVELNGdEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   100 LF-VNGTMLQGTQSISMPYASNGLYLEAE-AGYYKLSSEAYG-FVARIDGNGNFQVLLSDRYFNKTCGLCGNFNIFAEDD 176
Cdd:smart00216   78 LKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 1953347750   177 FRTQEG 182
Cdd:smart00216  158 FRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1281-1453 1.00e-25

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: 106.38  E-value: 1.00e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1360
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1361 TSEVLKYTLFQIFGKID--RPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPE 1438
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 1953347750  1439 NKAFVFSGVDELEQR 1453
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1280-1442 1.10e-23

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: 99.67  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1280 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVA 1359
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1360 STSEVLKYTLFQIFGKI-DRPEASRIALLLMASQepSRLARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIHLIEKQAPE 1438
Cdd:cd01450     81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                   ....
gi 1953347750 1439 NKAF 1442
Cdd:cd01450    158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1057-1131 1.19e-21

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 90.86  E-value: 1.19e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750  1057 QTMVDSSCRILTSD--IFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFCP 1131
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 226-296 1.04e-18

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 82.39  E-value: 1.04e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953347750   226 WEQCQLLKSAS-VFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGIVLYGWTDHSVCR 296
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2731-2812 2.86e-18

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 81.68  E-value: 2.86e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  2731 IIAKLQRVKVGDCKSEEeVDIHYCEGKCASKAVYSIhmEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRC 2810
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 1953347750  2811 SP 2812
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1064-1130 1.80e-17

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 78.96  E-value: 1.80e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953347750 1064 CRILT-SDIFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFC 1130
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 228-295 7.60e-17

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 77.04  E-value: 7.60e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750  228 QCQLLKSASVFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGIVLYGWTDHSVC 295
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1281-1452 2.74e-16

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 78.86  E-value: 2.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYhdGSHAYIE--LKDRKRPSELRRITSQVKYAGSEV 1358
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1359 ASTSEVLKYTLFQIFGKI--DRPEASRIALLL----MASQEPSRLARNlvryvqgLKKKKVIVIPVGIGPhASLKQIHLI 1432
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKI 150

                          170       180
                   ....*....|....*....|
gi 1953347750 1433 EKQAPENKAFVFSGVDELEQ 1452
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 656-711 2.53e-13

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 66.57  E-value: 2.53e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750  656 CPQGQVYLQCGTPCNMTCRSLSYPEeDCNEVCLEGCFCPPGLYLDERGDCVPKAQC 711
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 299-352 2.63e-12

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 2.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  299 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDE-GHCVGSAEC 352
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 299-352 2.74e-12

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.56  E-value: 2.74e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  299 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLD-EGHCVGSAEC 352
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 656-711 3.20e-12

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.56  E-value: 3.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750  656 CPQGQVYLQCGTPCNMTCRSLSYPEEdCNEVCLEGCFCPPGLYLDERGDCVPKAQC 711
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 583-653 8.19e-12

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 63.13  E-value: 8.19e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750   583 FAEEACALLTSSK--FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHI-AWREPGFCA 653
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1692-1866 5.70e-11

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: 65.73  E-value: 5.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1692 QPLDVVLLLDGSSSIPA-SYFDEMKSFTKAFISRanIGPRlTQVSVLQYGsiTTIDVPWNVAYEKVHLLSLVDLMQQEGG 1770
Cdd:COG1240     91 RGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDD--YRPR-DRVGLVAFG--GEAEVLLPLTRDREALKRALDELPPGGG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1771 pSQIGDALSFAVRYVTSEVHGARPgaskaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIG-DRYSEAQLSSLAG 1845
Cdd:COG1240    166 -TPLGDALALALELLKRADPARRK-----VIVLLTDgrdnAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE 239

                          170       180
                   ....*....|....*....|.
gi 1953347750 1846 pKAGSNMVRLQRIEDLPTVAT 1866
Cdd:COG1240    240 -ATGGRYFRADDLSELAAIYR 259
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2142-2203 6.91e-11

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 60.09  E-value: 6.91e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 2142 HCQVLL-SELFAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFC 2203
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGddecLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 588-652 7.36e-10

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 57.00  E-value: 7.36e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750  588 CALLTSSK-FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHIA-WREPGFC 652
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2138-2204 1.52e-09

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 56.58  E-value: 1.52e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750  2138 SSSSHCQVLLSEL--FAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFCA 2204
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1150-1200 5.14e-08

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.55  E-value: 5.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1150 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1200
Cdd:cd19941      7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2435-2498 2.90e-07

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 2.90e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2435 CVHRGTIYPVGQFWEEA-CDVCTCTDledsvmglRVAQCSQKPCEDNCLSGFTYVLHEGECCGRC 2498
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2265-2325 6.87e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.28  E-value: 6.87e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953347750  2265 DGVRHQFLETWVPAhqPCQICTCLSGRKVNCTLQPCPTARaptcgPCEVARLRQNAEQCCP 2325
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2435-2498 1.01e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 47.90  E-value: 1.01e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750  2435 CVHRGTIYPVGQFW-EEACDVCTCTDLEdsvmglrVAQCSQKPCEDN--CLSGFTyVLHEGECCGRC 2498
Cdd:smart00214    1 CVHNGRVYNDGETWkPDPCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1150-1200 2.22e-06

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 2.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1150 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1200
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2586-2648 3.50e-06

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 46.26  E-value: 3.50e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2586 CLLNGTIIGPGKSLMIDVCTTCRCTVqvgvisgFKLECRKTTCEA--CPLGYkEEKNQGECCGRC 2648
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2264-2326 3.90e-06

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 46.26  E-value: 3.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953347750 2264 EDGVRHQFLETWVPAhqPCQICTCLSGrKVNCTLQPCPTAraptcgPCEVARLRQNAEQCCPE 2326
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2586-2648 4.70e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.97  E-value: 4.70e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953347750  2586 CLLNGTIIGPGKSLMIDVCTTCRCTVQVgVISGFKLECRKTTceACPLGYKeEKNQGECCGRC 2648
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2207-2258 7.59e-05

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.69  E-value: 7.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2207 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVM-LEGSCVPEEAC 2258
Cdd:cd19941      1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2207-2258 1.68e-04

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.60  E-value: 1.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2207 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVML-EGSCVPEEAC 2258
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
354-398 4.98e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 37.93  E-value: 4.98e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1953347750   354 CVHAGQRYPPGASLLQDCHTCICRNSLWICSNEEC-PGECLVTGQS 398
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 381-544 1.11e-47

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 168.73  E-value: 1.11e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   381 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDH-TFSVVIETVQCADDldAVCTRSVTVRLPGhhNSL 459
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPCGGG--ATCLKSVKVELNG--DEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   460 VKLKHGGGVSMDGQDIQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRG 536
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1953347750   537 DDFVTPAG 544
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 392-545 1.32e-47

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 167.93  E-value: 1.32e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  392 CLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDHT-FSVVIETVQCADDLDAVCTRSVTVRLPGHHnslVKLKHGGGVSM 470
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750  471 DGQDIQIPLLQGDLRIQHTV--MASVRLSYGEDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRGDDFVTPAGL 545
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 860-1015 3.21e-41

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 150.24  E-value: 3.21e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   860 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 939
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   940 LFDGEV-------NVKKPMKDETHFEVVES-GQYVILLLGKAL-SVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNND 1010
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 1953347750  1011 FTSSS 1015
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1695-1864 1.44e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 1.44e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVD-LMQQEGGPSQ 1773
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1774 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD--VSVDSVDAAAEAARSNRVTVFPIGIGDRYsEAQLSSLAGPKAGSN 1851
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTDgrSQDGDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 1953347750 1852 MVRLQRIEDLPTV 1864
Cdd:pfam00092  159 VFTVSDFEALEDL 171
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1202-1280 4.46e-39

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 140.89  E-value: 4.46e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953347750 1202 VCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLL 1280
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1502-1647 5.30e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.34  E-value: 5.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1581
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750 1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPHANvQELEKIG 1647
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGNADD-EELRKIA 151
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1501-1649 7.43e-39

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: 143.20  E-value: 7.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRT 1580
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 1581 NTGLALQYLSEHSFSVSQgDREQVPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANVQELEKIGWP 1649
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1954-2106 7.43e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.50  E-value: 7.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1954 CMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGR 2031
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2032 LVSIPYVGGDMEVNVYGTIMYEVRFnHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGT 2106
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 871-1015 8.59e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.12  E-value: 8.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  871 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFRILVGNEGCSYPSVkCKKRVTILVEGGEIELFDG---EVN 946
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750  947 VKK---PMK-DETHFEVVESGQ-YVILLLGKALSVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNNDFTSSS 1015
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 39-183 9.65e-37

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 137.12  E-value: 9.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   39 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVSLIGGFQNGK-----RVSLSVYLGEFFdIHLFVNGTMLQGT 110
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  111 QSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGT 183
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1942-2105 6.29e-35

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.14  E-value: 6.29e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1942 ETCGCrWTCPCVCMGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHNGACSPGAkeTCMKSIEVKHDGLSVE 2019
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  2020 LHSD-MQMTVNGRLVSIPYVGGDMEVNVYGTIMYEVRFNHLGHI-FTFTPQNNeFQLQLSPRtFASKTYGLCGICDENGA 2097
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1953347750  2098 NDFILRDG 2105
Cdd:smart00216  156 DDFRTPDG 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1502-1658 4.30e-34

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: 129.66  E-value: 4.30e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNrTN 1581
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIKRMPG-----DIQVVPIGVGPhANVQELEKIGwpNAPILIH 1656
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVelkqaGIEVFAVGVKN-ADEEELKQIA--SDPKELY 157


                   ..
gi 1953347750 1657 DF 1658
Cdd:cd01472    158 VF 159
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1502-1646 1.79e-33

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: 128.21  E-value: 1.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1581
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953347750 1582 TGLALQYLSEHSFSVSQGDR--EQVPNLVYMVTGNPASDEIKRMPGDIQ---VVPIGVGP-HANVQELEKI 1646
Cdd:cd01481     82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQI 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1502-1646 2.11e-33

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: 128.34  E-value: 2.11e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1581
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANVQELEKI 1646
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1695-1861 1.11e-32

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: 126.03  E-value: 1.11e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQE-GGPSQ 1773
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1774 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGpKAG 1849
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITDgesnDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLAS-APG 158

                           170
                    ....*....|..
gi 1953347750  1850 SNMVRLQRIEDL 1861
Cdd:smart00327  159 GVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1694-1847 8.23e-32

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: 123.17  E-value: 8.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGP-S 1772
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 1773 QIGDALSFAVRYVTSEvHGARPGASKaVVILVTDV---SVDSVDAAAEAARSNRVTVFPIGIGDrYSEAQLSSLAGPK 1847
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDGrsdDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCP 155
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 26-182 5.83e-30

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 117.89  E-value: 5.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750    26 CTKGTVGrssmARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVsLIGGFQNGKRVS--LSVYLGEFF-DIH 99
Cdd:smart00216    3 CTQEECS----PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEptfSV-LLKNVPCGGGATclKSVKVELNGdEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750   100 LF-VNGTMLQGTQSISMPYASNGLYLEAE-AGYYKLSSEAYG-FVARIDGNGNFQVLLSDRYFNKTCGLCGNFNIFAEDD 176
Cdd:smart00216   78 LKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 1953347750   177 FRTQEG 182
Cdd:smart00216  158 FRTPDG 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1502-1647 1.58e-28

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: 113.92  E-value: 1.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNrTN 1581
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1582 TGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIkRMPGD------IQVVPIGVGpHANVQELEKIG 1647
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGVK-DADESELKMIA 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1281-1453 1.00e-25

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: 106.38  E-value: 1.00e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1360
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  1361 TSEVLKYTLFQIFGKID--RPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPE 1438
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 1953347750  1439 NKAFVFSGVDELEQR 1453
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1694-1853 7.98e-24

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: 100.33  E-value: 7.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQE-GGPS 1772
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1773 QIGDALSFAVRYVTSEVHGARpgasKAVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGPKA 1848
Cdd:cd00198     81 NIGAALRLALELLKSAKRPNA----RRVIILLTDgepnDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTT 156


                   ....*
gi 1953347750 1849 GSNMV 1853
Cdd:cd00198    157 GGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1501-1658 9.50e-24

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: 102.08  E-value: 9.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRY--RGgn 1578
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1579 rTNTGLALQYLSEHSFSVSQGDR---EQVPNLVYMVTGNPASDEIK------RMPGdIQVVPIGVGpHANVQELEKIGWP 1649
Cdd:cd01475     81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIASE 157


                   ....*....
gi 1953347750 1650 naPILIHDF 1658
Cdd:cd01475    158 --PLADHVF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1280-1442 1.10e-23

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: 99.67  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1280 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVA 1359
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1360 STSEVLKYTLFQIFGKI-DRPEASRIALLLMASQepSRLARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIHLIEKQAPE 1438
Cdd:cd01450     81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                   ....
gi 1953347750 1439 NKAF 1442
Cdd:cd01450    158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1057-1131 1.19e-21

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 90.86  E-value: 1.19e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750  1057 QTMVDSSCRILTSD--IFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFCP 1131
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1695-1844 3.34e-21

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: 92.68  E-value: 3.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQI 1774
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953347750 1775 GDALSFAVRYVTSEVHGARPGASKaVVILVTD-VSVDSVDAAAEAARSNRVTVFPIGIGDRySEAQLSSLA 1844
Cdd:cd01472     82 GKALKYVRENLFTEASGSREGVPK-VLVVITDgKSQDDVEEPAVELKQAGIEVFAVGVKNA-DEEELKQIA 150
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1695-1846 8.51e-21

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: 91.58  E-value: 8.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQI 1774
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953347750 1775 GDALSFAVRYVTSEVHGARPGASKaVVILVTD-VSVDSVDAAAEAARSNRVTVFPIGIGDrYSEAQLSSLAGP 1846
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPGVPK-VVILITDgKSQDDVELPARVLRNLGVNVFAVGVKD-ADESELKMIASK 152
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1694-1835 1.96e-20

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: 91.26  E-value: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQ 1773
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 1774 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD-VSVDSVD--AAAEAARSNRVTVFPIGIGDRY 1835
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATK-VLVVITDgESHDDPLlkDVIPQAEREGIIRYAIGVGGHF 144
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1501-1646 2.09e-19

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: 88.18  E-value: 2.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGnRT 1580
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750 1581 NTGLALQYLSEHSFSVSQGDREQVPNLVYMVT-----GNPASDEIKRMP--GDIQVVPIGVGPHAN----VQELEKI 1646
Cdd:cd01469     80 NTATAIQYVVTELFSESNGARKDATKVLVVITdgeshDDPLLKDVIPQAerEGIIRYAIGVGGHFQrensREELKTI 156
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1501-1646 2.28e-19

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: 87.62  E-value: 2.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRT 1580
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750 1581 NTGLALQYLSEHsfsVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMpgDIQVVPIGVGPHANVQELEKI 1646
Cdd:cd00198     81 NIGAALRLALEL---LKSAKRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEI 151
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 226-296 1.04e-18

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 82.39  E-value: 1.04e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953347750   226 WEQCQLLKSAS-VFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGIVLYGWTDHSVCR 296
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1693-1893 2.40e-18

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: 86.67  E-value: 2.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1693 PLDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPS 1772
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1773 QIGDALSFAVRYVTSEVHGARPGASKA--VVILVTD-VSVDSVDAAAEAARSNRVTVFPIGIGdRYSEAQLSSLAGPKAG 1849
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSERVprVGIVVTDgRPQDDVSEVAAKARALGIEMFAVGVG-RADEEELREIASEPLA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1953347750 1850 SNmvrLQRIEDLPTVATLGNSFFHKLCSGFDrVCVDEDGNEKRP 1893
Cdd:cd01475    161 DH---VFYVEDFSTIEELTKKFQGKICVVPD-LCATLSHVCQQV 200
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2731-2812 2.86e-18

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 81.68  E-value: 2.86e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750  2731 IIAKLQRVKVGDCKSEEeVDIHYCEGKCASKAVYSIhmEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRC 2810
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 1953347750  2811 SP 2812
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1064-1130 1.80e-17

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 78.96  E-value: 1.80e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953347750 1064 CRILT-SDIFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFC 1130
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 228-295 7.60e-17

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 77.04  E-value: 7.60e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750  228 QCQLLKSASVFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGIVLYGWTDHSVC 295
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1281-1452 2.74e-16

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 78.86  E-value: 2.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYhdGSHAYIE--LKDRKRPSELRRITSQVKYAGSEV 1358
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1359 ASTSEVLKYTLFQIFGKI--DRPEASRIALLL----MASQEPSRLARNlvryvqgLKKKKVIVIPVGIGPhASLKQIHLI 1432
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKI 150

                          170       180
                   ....*....|....*....|
gi 1953347750 1433 EKQAPENKAFVFSGVDELEQ 1452
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1694-1845 6.11e-16

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: 77.82  E-value: 6.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSIPASYFDEMKsFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVA--YEKVHLLSLVDLMQQEGGP 1771
Cdd:cd01476      1 LDLLFVLDSSGSVRGKFEKYKK-YIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPkhNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750 1772 SQIGDALSFAVRYVTsEVHGARPGASKAVVILVTDVSVDSVDAAAEAARSN-RVTVFPIGIGDRYS--EAQLSSLAG 1845
Cdd:cd01476     80 TATGAAIEVALQQLD-PSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDPGTvdTEELHSITG 155
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1501-1647 2.91e-15

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: 75.90  E-value: 2.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEAnFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVT--VEYTFSEAQSKGEVLQQVRDIRYRGGN 1578
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 1579 rTNTGLALQYLSEHsFSVSQGDREQVPNLVYMVTGNPASDEIKRM-------PGdIQVVPIGVGPHANV--QELEKIG 1647
Cdd:cd01476     80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQarilravPN-IETFAVGTGDPGTVdtEELHSIT 154
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1501-1642 6.97e-15

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: 75.50  E-value: 6.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEAN-FNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSE--AQSKGEVLQQVRDIR---Y 1574
Cdd:cd01471      1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslyY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750 1575 RGGNrTNTGLALQYLSEHSFSvSQGDREQVPNLVYMVT-GNPASD--------EIKRMPGDIQVvpIGVGPHANVQE 1642
Cdd:cd01471     81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEE 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1280-1442 1.60e-13

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: 70.67  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1280 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVA 1359
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1360 STSEVLKYTLfQIFGKIDRPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPEN 1439
Cdd:cd00198     81 NIGAALRLAL-ELLKSAKRPNARRV-IILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGG 158


                   ...
gi 1953347750 1440 KAF 1442
Cdd:cd00198    159 AVF 161
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 656-711 2.53e-13

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 66.57  E-value: 2.53e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750  656 CPQGQVYLQCGTPCNMTCRSLSYPEeDCNEVCLEGCFCPPGLYLDERGDCVPKAQC 711
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1695-1871 1.86e-12

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: 67.73  E-value: 1.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGG-PSQ 1773
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1774 IGDALSFAVRYVTSEVHGAR--PGASKAVVILVTDVSVDSVDAAAEAARSNRvtVFPIGIGDRyseaqlsslagpkaGSN 1851
Cdd:cd01481     82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAG--IVPFAIGAR--------------NAD 145

                          170       180
                   ....*....|....*....|
gi 1953347750 1852 MVRLQRIEDLPTVATLGNSF 1871
Cdd:cd01481    146 LAELQQIAFDPSFVFQVSDF 165
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 299-352 2.63e-12

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 2.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  299 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDE-GHCVGSAEC 352
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 299-352 2.74e-12

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.56  E-value: 2.74e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750  299 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLD-EGHCVGSAEC 352
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 656-711 3.20e-12

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.56  E-value: 3.20e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750  656 CPQGQVYLQCGTPCNMTCRSLSYPEEdCNEVCLEGCFCPPGLYLDERGDCVPKAQC 711
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 583-653 8.19e-12

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 63.13  E-value: 8.19e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750   583 FAEEACALLTSSK--FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHI-AWREPGFCA 653
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1692-1866 5.70e-11

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: 65.73  E-value: 5.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1692 QPLDVVLLLDGSSSIPA-SYFDEMKSFTKAFISRanIGPRlTQVSVLQYGsiTTIDVPWNVAYEKVHLLSLVDLMQQEGG 1770
Cdd:COG1240     91 RGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDD--YRPR-DRVGLVAFG--GEAEVLLPLTRDREALKRALDELPPGGG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1771 pSQIGDALSFAVRYVTSEVHGARPgaskaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIG-DRYSEAQLSSLAG 1845
Cdd:COG1240    166 -TPLGDALALALELLKRADPARRK-----VIVLLTDgrdnAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE 239

                          170       180
                   ....*....|....*....|.
gi 1953347750 1846 pKAGSNMVRLQRIEDLPTVAT 1866
Cdd:COG1240    240 -ATGGRYFRADDLSELAAIYR 259
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2142-2203 6.91e-11

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 60.09  E-value: 6.91e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 2142 HCQVLL-SELFAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFC 2203
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGddecLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 588-652 7.36e-10

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 57.00  E-value: 7.36e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750  588 CALLTSSK-FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHIA-WREPGFC 652
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2138-2204 1.52e-09

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 56.58  E-value: 1.52e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750  2138 SSSSHCQVLLSEL--FAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFCA 2204
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1280-1353 1.56e-09

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: 60.48  E-value: 1.56e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953347750 1280 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKY 1353
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEY 76
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1693-1844 7.43e-09

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: 7.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1693 PLDVVLLLDGSSSIPASYFDEMKSFTKAFISR------ANIGPRLTQVSVLQY-GSITTIDVPWNVAYEKVHLLSLVDLM 1765
Cdd:cd01480      2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1766 QQEGGPSQIGDALsfavRYVTSEVHGARPGASKAVVILVTDVSVDSVDA-----AAEAARSNRVTVFPIGIGDRYSEaQL 1840
Cdd:cd01480     82 EYIGGGTFTDCAL----KYATEQLLEGSHQKENKFLLVITDGHSDGSPDggiekAVNEADHLGIKIFFVAVGSQNEE-PL 156


                   ....
gi 1953347750 1841 SSLA 1844
Cdd:cd01480    157 SRIA 160
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1281-1429 1.14e-08

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: 56.85  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAs 1360
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953347750 1361 TSEVLKYTLFQIFGKIDRPEAS--RIALLLMASQEPSRLARNLVRyvqgLKKKKVIVIPVGIGPHAS--LKQI 1429
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQDDVEEPAVE----LKQAGIEVFAVGVKNADEeeLKQI 149
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1501-1591 2.25e-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: 56.24  E-value: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1501 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRM------DVGQDRIHVTVLQYSYMVTVEYTF-SEAQSKGEVLQQVRDIR 1573
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLE 82

                           90
                   ....*....|....*...
gi 1953347750 1574 YRGGNrTNTGLALQYLSE 1591
Cdd:cd01480     83 YIGGG-TFTDCALKYATE 99
VWA_2 pfam13519
von Willebrand factor type A domain;
1696-1804 3.36e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.45  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1696 VVLLLDGSSSIPA-----SYFDEMKSFTKAFISRANIgprlTQVSVLQYGSITTIDVPWNVAYEkvHLLSLVDLMQQEGG 1770
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTKDRA--KILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1953347750 1771 PSQIGDALSFAVRYVtsevhGARPGASKAVVILV 1804
Cdd:pfam13519   75 GTNLAAALQLARAAL-----KHRRKNQPRRIVLI 103
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1281-1401 3.79e-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: 55.37  E-value: 3.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEvAS 1360
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1953347750 1361 TSEVLKYTLFQIF--GKIDRPEASRIALLLM--ASQ----EPSRLARNL 1401
Cdd:cd01482     81 TGKALTHVREKNFtpDAGARPGVPKVVILITdgKSQddveLPARVLRNL 129
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1150-1200 5.14e-08

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.55  E-value: 5.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1150 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1200
Cdd:cd19941      7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1281-1385 8.57e-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: 54.25  E-value: 8.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1281 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1360
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                           90       100
                   ....*....|....*....|....*
gi 1953347750 1361 TSEVLKYTLFQIFgkiDRPEASRIA 1385
Cdd:cd01481     82 TGSALDYVVKNLF---TKSAGSRIE 103
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2435-2498 2.90e-07

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 2.90e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2435 CVHRGTIYPVGQFWEEA-CDVCTCTDledsvmglRVAQCSQKPCEDNCLSGFTYVLHEGECCGRC 2498
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1694-1845 3.34e-07

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: 53.16  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSI-PASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITT--IDVPWNVAYEKVHLLSLV-DL--MQQ 1767
Cdd:cd01471      1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKelIRLSSPNSTNKDLALNAIrALlsLYY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1768 EGGPSQIGDALSfAVRYVTSEVHGARPGASKAVVILvTDVSVDSVDAAAEAARSNR-----VTVFPIGIGDRYSEAQlsS 1842
Cdd:cd01471     81 PNGSTNTTSALL-VVEKHLFDTRGNRENAPQLVIIM-TDGIPDSKFRTLKEARKLRergviIAVLGVGQGVNHEENR--S 156


                   ...
gi 1953347750 1843 LAG 1845
Cdd:cd01471    157 LVG 159
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1280-1449 5.09e-07

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: 52.36  E-value: 5.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1280 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGsEVA 1359
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLL-GLT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1360 STSEVLKYTLFQIF--GKIDRPEASRIALLLM--ASQEPSRLARNLvryvQGLKKKKVIVIPVGIGPH----ASLKQIHL 1431
Cdd:cd01469     80 NTATAIQYVVTELFseSNGARKDATKVLVVITdgESHDDPLLKDVI----PQAEREGIIRYAIGVGGHfqreNSREELKT 155

                          170
                   ....*....|....*...
gi 1953347750 1432 IEKQAPEnkAFVFSGVDE 1449
Cdd:cd01469    156 IASKPPE--EHFFNVTDF 171
VWC smart00214
von Willebrand factor (vWF) type C domain;
2265-2325 6.87e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.28  E-value: 6.87e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953347750  2265 DGVRHQFLETWVPAhqPCQICTCLSGRKVNCTLQPCPTARaptcgPCEVARLRQNAEQCCP 2325
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2435-2498 1.01e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 47.90  E-value: 1.01e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953347750  2435 CVHRGTIYPVGQFW-EEACDVCTCTDLEdsvmglrVAQCSQKPCEDN--CLSGFTyVLHEGECCGRC 2498
Cdd:smart00214    1 CVHNGRVYNDGETWkPDPCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1150-1200 2.22e-06

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 2.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1150 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1200
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2586-2648 3.50e-06

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 46.26  E-value: 3.50e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2586 CLLNGTIIGPGKSLMIDVCTTCRCTVqvgvisgFKLECRKTTCEA--CPLGYkEEKNQGECCGRC 2648
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1280-1421 3.59e-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: 50.08  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1280 LDLVFLLDGSSKLSE-DEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKD--RKRPSELRRITSQVK--YA 1354
Cdd:cd01471      1 LDLYLLVDGSGSIGYsNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslYY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953347750 1355 GSEVASTSEVLKYTLFQIF-GKIDRPEASRIAlLLMASQEPSRLARNLvRYVQGLKKKKVIVIPVGIG 1421
Cdd:cd01471     81 PNGSTNTTSALLVVEKHLFdTRGNRENAPQLV-IIMTDGIPDSKFRTL-KEARKLRERGVIIAVLGVG 146
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2264-2326 3.90e-06

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 46.26  E-value: 3.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953347750 2264 EDGVRHQFLETWVPAhqPCQICTCLSGrKVNCTLQPCPTAraptcgPCEVARLRQNAEQCCPE 2326
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2586-2648 4.70e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.97  E-value: 4.70e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953347750  2586 CLLNGTIIGPGKSLMIDVCTTCRCTVQVgVISGFKLECRKTTceACPLGYKeEKNQGECCGRC 2648
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1695-1844 4.66e-05

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 47.75  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1695 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANigPRLtQVSVLQYGSITTIDVPWNVAYEkvhLLSLVDLMQQ---EGGp 1771
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTEVVEDLPLTADDG---LEDAIEFLSGlfaGGG- 192

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953347750 1772 SQIGDALSFAVRYVTsevhgaRPGASKAVVILVTD--VSVDSVDAAAEA-ARSNRVTVFPIGIGDRYSEAQLSSLA 1844
Cdd:COG2425    193 TDIAPALRAALELLE------EPDYRNADIVLITDgeAGVSPEELLREVrAKESGVRLFTVAIGDAGNPGLLEALA 262
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1691-1846 5.33e-05

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.84  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1691 SQPLDVVLLLDGSSSIPASYFDEMKSFTKAFIS--RANIGPRLT-QVSVLQYGSITTIDVPWnVAYEKVHLLSLVDlmqq 1767
Cdd:COG4245      3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDelRQDPYALETvEVSVITFDGEAKVLLPL-TDLEDFQPPDLSA---- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1768 eGGPSQIGDALSFA-------VRYVTSEVHGARpgasKAVVILVTD--VSVDSVDAAAEAARS----NRVTVFPIGIGDR 1834
Cdd:COG4245     78 -SGGTPLGAALELLldlierrVQKYTAEGKGDW----RPVVFLITDgePTDSDWEAALQRLKDgeaaKKANIFAIGVGPD 152

                          170
                   ....*....|..
gi 1953347750 1835 YSEAQLSSLAGP 1846
Cdd:COG4245    153 ADTEVLKQLTDP 164
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1502-1624 6.12e-05

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 46.54  E-value: 6.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1502 DVVFVLEGSDKIGEANFNKS-REFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFS--EAQSKGEVLQQVRDIR--YRG 1576
Cdd:cd01473      2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeERYDKNELLKKINDLKnsYRS 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1953347750 1577 GNRTNTGLALQYlSEHSFSVSQGDREQVPNLVYMVT-GNPASDEIKRMP 1624
Cdd:cd01473     82 GGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTdGNDTSASKKELQ 129
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2207-2258 7.59e-05

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.69  E-value: 7.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2207 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVM-LEGSCVPEEAC 2258
Cdd:cd19941      1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2207-2258 1.68e-04

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.60  E-value: 1.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953347750 2207 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVML-EGSCVPEEAC 2258
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1694-1832 3.63e-03

VWA subfamily: 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 have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 40.79  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1694 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPrLTQVSVlqYGSITTIDVPWNVAyekvhlLSLVDLMQQE----- 1768
Cdd:cd01464      4 LPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDP-YALESV--EISVITFDSAARVI------VPLTPLESFQpprlt 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953347750 1769 -GGPSQIGDALSFAVRYVTSEV---HGARPGASKAVVILVTD-VSVDSVDAAAEA---ARSNRVTVFPIGIG 1832
Cdd:cd01464     75 aSGGTSMGAALELALDCIDRRVqryRADQKGDWRPWVFLLTDgEPTDDLTAAIERikeARDSKGRIVACAVG 146
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1281-1449 4.60e-03

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 40.76  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1281 DLVFLLDGSSKLSEDEF--EVLKvFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSE---LRRITSQVKYAG 1355
Cdd:cd01473      2 DLTLILDESASIGYSNWrkDVIP-FTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKnelLKKINDLKNSYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953347750 1356 SEVAS-TSEVLKYTLFQIFGKIDRPEAS-RIALLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGphaslkqihlie 1433
Cdd:cd01473     81 SGGETyIVEALKYGLKNYTKHGNRRKDApKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVG------------ 148

                          170
                   ....*....|....*.
gi 1953347750 1434 kQAPENKAFVFSGVDE 1449
Cdd:cd01473    149 -AASENKLKLLAGCDI 163
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
354-398 4.98e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 37.93  E-value: 4.98e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1953347750   354 CVHAGQRYPPGASLLQDCHTCICRNSLWICSNEEC-PGECLVTGQS 398
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
 
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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