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Conserved domains on  [gi|334191706|tpg|DAA34797|]
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TPA_inf: von Willebrand factor [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 ...
 377-540 1.16e-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: 1.16e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    377 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDH-TFSVVIETVQCADDldAVCTRSVTVRLPGhhNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPCGGG--ATCLKSVKVELNG--DEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    456 VKLKHGGGVSMDGQDIQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 334191706    533 DDFVTPAG 540
Cdd:smart00216  156 DDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 3.36e-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: 3.36e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    856 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    936 LFDGEV-------NVKKPMKDETHFEVVES-GQYVILLLGKAL-SVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 334191706   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1691-1860 1.43e-40

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 1.43e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVD-LMQQEGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1770 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD--VSVDSVDAAAEAARSNRVTVFPIGIGDRYsEAQLSSLAGPKAGSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTDgrSQDGDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 334191706  1848 MVRLQRIEDLPTV 1860
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 ...
 1198-1276 4.54e-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: 4.54e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334191706  1198 VCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1498-1643 5.29e-39

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.34  E-value: 5.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706  1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPHANvQELEKIG 1643
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGNADD-EELRKIA 151
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 7.42e-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: 7.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1950 CMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2028 LVSIPYVGGDMEVNVYGTIMYEVRFnHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 9.73e-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: 9.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    35 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVSLIGGFQNGK-----RVSLSVYLGEFFdIHLFVNGTMLQGT 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   107 QSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 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 334191706   1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1357 TSEVLKYTLFQIFGKID--RPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 334191706   1435 NKAFVFSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 1.21e-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: 1.21e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706   1053 QTMVDSSCRILTSD--IFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-292 6.74e-19

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: 83.16  E-value: 6.74e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334191706    222 WEQCQLLKSAS-VFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGVVLYGWTDHSVCR 292
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 2.89e-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: 2.89e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   2727 IIAKLQRVKVGDCKSEEeVDIHYCEGKCASKAVYSIhmEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 334191706   2807 SP 2808
Cdd:smart00041   78 EP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 2.57e-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: 2.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706  652 CPQGQVYLQCGTPCNMTCRSLSYPEeDCNEVCLEGCFCPPGLYLDERGDCVPKAQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 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 334191706  295 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDE-GHCVGSAEC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 8.18e-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: 8.18e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706    579 FAEEACALLTSSK--FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHI-AWREPGFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 7.18e-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: 7.18e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706  2138 HCQVLL-SELFAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFC 2199
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGddecLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 5.18e-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: 5.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 334191706 1146 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 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 334191706  2431 CVHRGTIYPVGQFWEEA-CDVCTCTDledsvmglRVAQCSQKPCEDNCLSGFTYVLHEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 7.07e-07

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.28  E-value: 7.07e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334191706   2261 DGVRHQFLETWVPAhqPCQICTCLSGRKVNCTLQPCPTARaptcgPCEVARLRQNAEQCCP 2321
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 ...
 2582-2644 3.57e-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: 3.57e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2582 CLLNGTIIGPGKSLMIDVCTTCRCTVqvgvisgFKLECRKTTCEA--CPLGYkEEKNQGECCGRC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 7.58e-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: 7.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706 2203 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVM-LEGSCVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 350-394 5.07e-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: 5.07e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 334191706    350 CVHAGQRYPPGASLLQDCHTCICRNSLWICSNEEC-PGECLVTGQS 394
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 ...
 377-540 1.16e-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: 1.16e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    377 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDH-TFSVVIETVQCADDldAVCTRSVTVRLPGhhNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPCGGG--ATCLKSVKVELNG--DEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    456 VKLKHGGGVSMDGQDIQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 334191706    533 DDFVTPAG 540
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.33e-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: 1.33e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   388 CLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDHT-FSVVIETVQCADDLDAVCTRSVTVRLPGHHnslVKLKHGGGVSM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706   467 DGQDIQIPLLQGDLRIQHTV--MASVRLSYGEDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRGDDFVTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 3.36e-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: 3.36e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    856 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    936 LFDGEV-------NVKKPMKDETHFEVVES-GQYVILLLGKAL-SVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 334191706   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1691-1860 1.43e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 1.43e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVD-LMQQEGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1770 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD--VSVDSVDAAAEAARSNRVTVFPIGIGDRYsEAQLSSLAGPKAGSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTDgrSQDGDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 334191706  1848 MVRLQRIEDLPTV 1860
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 ...
 1198-1276 4.54e-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: 4.54e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334191706  1198 VCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1498-1643 5.29e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.34  E-value: 5.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706  1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPHANvQELEKIG 1643
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 ...
 1497-1645 7.41e-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: 7.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRT 1576
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706 1577 NTGLALQYLSEHSFSVSQgDREQVPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANVQELEKIGWP 1645
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 ...
 1950-2102 7.42e-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: 7.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1950 CMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2028 LVSIPYVGGDMEVNVYGTIMYEVRFnHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 8.74e-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: 8.74e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   867 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFRILVGNEGCSYPSVkCKKRVTILVEGGEIELFDG---EVN 942
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706   943 VKK---PMK-DETHFEVVESGQ-YVILLLGKALSVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNNDFTSSS 1011
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 9.73e-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: 9.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    35 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVSLIGGFQNGK-----RVSLSVYLGEFFdIHLFVNGTMLQGT 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   107 QSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 6.35e-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: 6.35e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1938 ETCGCrWTCPCVCMGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHNGACSPGAkeTCMKSIEVKHDGLSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   2016 LHSD-MQMTVNGRLVSIPYVGGDMEVNVYGTIMYEVRFNHLGHI-FTFTPQNNeFQLQLSPRtFASKTYGLCGICDENGA 2093
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 334191706   2094 NDFILRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1642 2.10e-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: 2.10e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANVQELEKI 1642
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1857 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 334191706   1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQE-GGPSQ 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1770 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGpKAG 1845
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITDgesnDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLAS-APG 158

                           170
                    ....*....|..
gi 334191706   1846 SNMVRLQRIEDL 1857
Cdd:smart00327  159 GVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1843 8.22e-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: 8.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1690 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGP-S 1768
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706 1769 QIGDALSFAVRYVTSEvHGARPGASKaVVILVTDV---SVDSVDAAAEAARSNRVTVFPIGIGDrYSEAQLSSLAGPK 1843
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDGrsdDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCP 155
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 22-178 6.05e-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: 6.05e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706     22 CTKGTVGrssmARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVsLIGGFQNGKRVS--LSVYLGEFF-DIH 95
Cdd:smart00216    3 CTQEECS----PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEptfSV-LLKNVPCGGGATclKSVKVELNGdEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706     96 LF-VNGTMLQGTQSISMPYASNGLYLEAE-AGYYKLSSEAYG-FVARIDGNGNFQVLLSDRYFNKTCGLCGNFNIFAEDD 172
Cdd:smart00216   78 LKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 334191706    173 FRTQEG 178
Cdd:smart00216  158 FRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 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 334191706   1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1357 TSEVLKYTLFQIFGKID--RPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 334191706   1435 NKAFVFSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 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 334191706 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVA 1355
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1356 STSEVLKYTLFQIFGKI-DRPEASRIALLLMASQepSRLARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIHLIEKQAPE 1434
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 334191706 1435 NKAF 1438
Cdd:cd01450   158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 1.21e-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: 1.21e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706   1053 QTMVDSSCRILTSD--IFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-292 6.74e-19

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: 83.16  E-value: 6.74e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334191706    222 WEQCQLLKSAS-VFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGVVLYGWTDHSVCR 292
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 2.89e-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: 2.89e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   2727 IIAKLQRVKVGDCKSEEeVDIHYCEGKCASKAVYSIhmEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 334191706   2807 SP 2808
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1060-1126 1.90e-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: 78.58  E-value: 1.90e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334191706  1060 CRILT-SDIFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFC 1126
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 6.75e-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: 6.75e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706   224 QCQLLKSASVFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGVVLYGWTDHSVC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1277-1448 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 334191706  1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYhdGSHAYIE--LKDRKRPSELRRITSQVKYAGSEV 1354
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1355 ASTSEVLKYTLFQIFGKI--DRPEASRIALLL----MASQEPSRLARNlvryvqgLKKKKVIVIPVGIGPhASLKQIHLI 1428
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKI 150

                          170       180
                   ....*....|....*....|
gi 334191706  1429 EKQAPENKAFVFSGVDELEQ 1448
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 2.57e-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: 2.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706  652 CPQGQVYLQCGTPCNMTCRSLSYPEeDCNEVCLEGCFCPPGLYLDERGDCVPKAQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 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 334191706  295 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDE-GHCVGSAEC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 2.76e-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: 2.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   295 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLD-EGHCVGSAEC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 3.26e-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: 3.26e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706   652 CPQGQVYLQCGTPCNMTCRSLSYPEEdCNEVCLEGCFCPPGLYLDERGDCVPKAQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 8.18e-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: 8.18e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706    579 FAEEACALLTSSK--FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHI-AWREPGFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1688-1862 5.69e-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: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1688 QPLDVVLLLDGSSSIPA-SYFDEMKSFTKAFISRanIGPRlTQVSVLQYGsiTTIDVPWNVAYEKVHLLSLVDLMQQEGG 1766
Cdd:COG1240    91 RGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDD--YRPR-DRVGLVAFG--GEAEVLLPLTRDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1767 pSQIGDALSFAVRYVTSEVHGARPgaskaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIG-DRYSEAQLSSLAG 1841
Cdd:COG1240   166 -TPLGDALALALELLKRADPARRK-----VIVLLTDgrdnAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE 239

                         170       180
                  ....*....|....*....|.
gi 334191706 1842 pKAGSNMVRLQRIEDLPTVAT 1862
Cdd:COG1240   240 -ATGGRYFRADDLSELAAIYR 259
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 7.18e-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: 7.18e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706  2138 HCQVLL-SELFAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFC 2199
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGddecLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 7.64e-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: 7.64e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706   584 CALLTSSK-FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHIA-WREPGFC 648
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2134-2200 1.53e-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: 1.53e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706   2134 SSSSHCQVLLSEL--FAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFCA 2200
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 5.18e-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: 5.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 334191706 1146 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 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 334191706  2431 CVHRGTIYPVGQFWEEA-CDVCTCTDledsvmglRVAQCSQKPCEDNCLSGFTYVLHEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 7.07e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.28  E-value: 7.07e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334191706   2261 DGVRHQFLETWVPAhqPCQICTCLSGRKVNCTLQPCPTARaptcgPCEVARLRQNAEQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 1.04e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 47.90  E-value: 1.04e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706   2431 CVHRGTIYPVGQFW-EEACDVCTCTDLEdsvmglrVAQCSQKPCEDN--CLSGFTyVLHEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWkPDPCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 2.23e-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: 2.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 334191706  1146 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 3.57e-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: 3.57e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2582 CLLNGTIIGPGKSLMIDVCTTCRCTVqvgvisgFKLECRKTTCEA--CPLGYkEEKNQGECCGRC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2260-2322 3.94e-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: 3.94e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334191706  2260 EDGVRHQFLETWVPAhqPCQICTCLSGrKVNCTLQPCPTAraptcgPCEVARLRQNAEQCCPE 2322
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 4.69e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.97  E-value: 4.69e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334191706   2582 CLLNGTIIGPGKSLMIDVCTTCRCTVQVgVISGFKLECRKTTceACPLGYKeEKNQGECCGRC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 7.58e-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: 7.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706 2203 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVM-LEGSCVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 1.70e-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: 1.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2203 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVML-EGSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
350-394 5.07e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 37.93  E-value: 5.07e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 334191706    350 CVHAGQRYPPGASLLQDCHTCICRNSLWICSNEEC-PGECLVTGQS 394
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 ...
 377-540 1.16e-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: 1.16e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    377 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDH-TFSVVIETVQCADDldAVCTRSVTVRLPGhhNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPCGGG--ATCLKSVKVELNG--DEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    456 VKLKHGGGVSMDGQDIQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 334191706    533 DDFVTPAG 540
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.33e-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: 1.33e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   388 CLVTGQSHFKSFDNRYFTFSGVCHYLLAQDCQDHT-FSVVIETVQCADDLDAVCTRSVTVRLPGHHnslVKLKHGGGVSM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706   467 DGQDIQIPLLQGDLRIQHTV--MASVRLSYGEDLQMDWDGRGRLLVTLSPAYAGKTCGLCGNYNGNRGDDFVTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 3.36e-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: 3.36e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    856 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    936 LFDGEV-------NVKKPMKDETHFEVVES-GQYVILLLGKAL-SVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 334191706   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1691-1860 1.43e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 1.43e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVD-LMQQEGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1770 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD--VSVDSVDAAAEAARSNRVTVFPIGIGDRYsEAQLSSLAGPKAGSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTDgrSQDGDPEEVARELKSAGVTVFAVGVGNAD-DEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 334191706  1848 MVRLQRIEDLPTV 1860
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 ...
 1198-1276 4.54e-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: 4.54e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334191706  1198 VCEVAGRRLAPGKKIILNPSDPEHCQICHCDGVNFTCQACREPGSLVVPPTEGPIGSTTSYVEDTPEPPLHDFHCSRLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1498-1643 5.29e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.34  E-value: 5.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706  1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPHANvQELEKIG 1643
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 ...
 1497-1645 7.41e-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: 7.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRT 1576
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706 1577 NTGLALQYLSEHSFSVSQgDREQVPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANVQELEKIGWP 1645
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 ...
 1950-2102 7.42e-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: 7.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1950 CMGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGAKETCMKSIEVKHDGLSVELHSDMQMTVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2028 LVSIPYVGGDMEVNVYGTIMYEVRFnHLGHIFTFTPQNNEFQLQLSPRTFASKTYGLCGICDENGANDFILRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 8.74e-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: 8.74e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   867 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFRILVGNEGCSYPSVkCKKRVTILVEGGEIELFDG---EVN 942
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706   943 VKK---PMK-DETHFEVVESGQ-YVILLLGKALSVVWDHRLSISVTLKRTYQEQVCGLCGNFDGIQNNDFTSSS 1011
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 9.73e-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: 9.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706    35 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVSLIGGFQNGK-----RVSLSVYLGEFFdIHLFVNGTMLQGT 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   107 QSISMPYASNGLYLEAEAGYYKLSSEAYGFVARIDGNGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFRTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 6.35e-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: 6.35e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1938 ETCGCrWTCPCVCMGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHNGACSPGAkeTCMKSIEVKHDGLSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   2016 LHSD-MQMTVNGRLVSIPYVGGDMEVNVYGTIMYEVRFNHLGHI-FTFTPQNNeFQLQLSPRtFASKTYGLCGICDENGA 2093
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 334191706   2094 NDFILRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1498-1654 4.29e-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: 4.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNrTN 1577
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIKRMPG-----DIQVVPIGVGPhANVQELEKIGwpNAPILIH 1652
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVelkqaGIEVFAVGVKN-ADEEELKQIA--SDPKELY 157


                  ..
gi 334191706 1653 DF 1654
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 ...
 1498-1642 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 334191706 1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1577
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334191706 1578 TGLALQYLSEHSFSVSQGDR--EQVPNLVYMVTGNPASDEIKRMPGDIQ---VVPIGVGP-HANVQELEKI 1642
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQI 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1642 2.10e-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: 2.10e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANVQELEKI 1642
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1857 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 334191706   1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQE-GGPSQ 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1770 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGpKAG 1845
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITDgesnDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLAS-APG 158

                           170
                    ....*....|..
gi 334191706   1846 SNMVRLQRIEDL 1857
Cdd:smart00327  159 GVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1843 8.22e-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: 8.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1690 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGP-S 1768
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706 1769 QIGDALSFAVRYVTSEvHGARPGASKaVVILVTDV---SVDSVDAAAEAARSNRVTVFPIGIGDrYSEAQLSSLAGPK 1843
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDGrsdDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCP 155
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 22-178 6.05e-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: 6.05e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706     22 CTKGTVGrssmARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQEH---SVsLIGGFQNGKRVS--LSVYLGEFF-DIH 95
Cdd:smart00216    3 CTQEECS----PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEptfSV-LLKNVPCGGGATclKSVKVELNGdEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706     96 LF-VNGTMLQGTQSISMPYASNGLYLEAE-AGYYKLSSEAYG-FVARIDGNGNFQVLLSDRYFNKTCGLCGNFNIFAEDD 172
Cdd:smart00216   78 LKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 334191706    173 FRTQEG 178
Cdd:smart00216  158 FRTPDG 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1498-1643 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 334191706 1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNrTN 1577
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334191706 1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIkRMPGD------IQVVPIGVGpHANVQELEKIG 1643
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGVK-DADESELKMIA 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 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 334191706   1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   1357 TSEVLKYTLFQIFGKID--RPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 334191706   1435 NKAFVFSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 7.97e-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: 7.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1690 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQE-GGPS 1768
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1769 QIGDALSFAVRYVTSEVHGARpgasKAVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIGDRYSEAQLSSLAGPKA 1844
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA----RRVIILLTDgepnDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTT 156


                  ....*
gi 334191706 1845 GSNMV 1849
Cdd:cd00198   157 GGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1497-1654 9.49e-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: 9.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRY--RGgn 1574
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1575 rTNTGLALQYLSEHSFSVSQGDR---EQVPNLVYMVTGNPASDEIK------RMPGdIQVVPIGVGpHANVQELEKIGWP 1645
Cdd:cd01475    81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIASE 157


                  ....*....
gi 334191706 1646 naPILIHDF 1654
Cdd:cd01475   158 --PLADHVF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 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 334191706 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVA 1355
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1356 STSEVLKYTLFQIFGKI-DRPEASRIALLLMASQepSRLARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIHLIEKQAPE 1434
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 334191706 1435 NKAF 1438
Cdd:cd01450   158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 1.21e-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: 1.21e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706   1053 QTMVDSSCRILTSD--IFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1691-1840 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 334191706 1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQI 1770
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334191706 1771 GDALSFAVRYVTSEVHGARPGASKaVVILVTD-VSVDSVDAAAEAARSNRVTVFPIGIGDRySEAQLSSLA 1840
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 ...
 1691-1842 8.50e-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: 8.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQI 1770
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334191706 1771 GDALSFAVRYVTSEVHGARPGASKaVVILVTD-VSVDSVDAAAEAARSNRVTVFPIGIGDrYSEAQLSSLAGP 1842
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 ...
 1690-1831 1.95e-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: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1690 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPSQ 1769
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706 1770 IGDALSFAVRYVTSEVHGARPGASKaVVILVTD-VSVDSVD--AAAEAARSNRVTVFPIGIGDRY 1831
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 ...
 1497-1642 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 334191706 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGnRT 1576
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706 1577 NTGLALQYLSEHSFSVSQGDREQVPNLVYMVT-----GNPASDEIKRMP--GDIQVVPIGVGPHAN----VQELEKI 1642
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITdgeshDDPLLKDVIPQAerEGIIRYAIGVGGHFQrensREELKTI 156
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1642 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 334191706 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSEAQSKGEVLQQVRDIRYRGGNRT 1576
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706 1577 NTGLALQYLSEHsfsVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMpgDIQVVPIGVGPHANVQELEKI 1642
Cdd:cd00198    81 NIGAALRLALEL---LKSAKRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEI 151
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-292 6.74e-19

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: 83.16  E-value: 6.74e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334191706    222 WEQCQLLKSAS-VFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGVVLYGWTDHSVCR 292
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1689-1889 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 334191706 1689 PLDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGGPS 1768
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1769 QIGDALSFAVRYVTSEVHGARPGASKA--VVILVTD-VSVDSVDAAAEAARSNRVTVFPIGIGdRYSEAQLSSLAGPKAG 1845
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVprVGIVVTDgRPQDDVSEVAAKARALGIEMFAVGVG-RADEEELREIASEPLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 334191706 1846 SNmvrLQRIEDLPTVATLGNSFFHKLCSGFDrVCVDEDGNEKRP 1889
Cdd:cd01475   161 DH---VFYVEDFSTIEELTKKFQGKICVVPD-LCATLSHVCQQV 200
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 2.89e-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: 2.89e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706   2727 IIAKLQRVKVGDCKSEEeVDIHYCEGKCASKAVYSIhmEDVQDQCSCCSPTQTEPMQVPLRCTNGSLIYHEILNAMQCRC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 334191706   2807 SP 2808
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1060-1126 1.90e-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: 78.58  E-value: 1.90e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334191706  1060 CRILT-SDIFQDCNRLVDPEPFLDICIYDTCSCEsiGDCTCFCDTIAAYAHVCAQHG-KVVAWRTATFC 1126
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 6.75e-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: 6.75e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706   224 QCQLLKSASVFARCHPLVDPEPFVALCERTLCTCVQGMECPCAVLLEYARACAQQGVVLYGWTDHSVC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1277-1448 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 334191706  1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYhdGSHAYIE--LKDRKRPSELRRITSQVKYAGSEV 1354
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706  1355 ASTSEVLKYTLFQIFGKI--DRPEASRIALLL----MASQEPSRLARNlvryvqgLKKKKVIVIPVGIGPhASLKQIHLI 1428
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKI 150

                          170       180
                   ....*....|....*....|
gi 334191706  1429 EKQAPENKAFVFSGVDELEQ 1448
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1690-1841 6.10e-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: 6.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1690 LDVVLLLDGSSSIPASYFDEMKsFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVA--YEKVHLLSLVDLMQQEGGP 1767
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKK-YIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPkhNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706 1768 SQIGDALSFAVRYVTsEVHGARPGASKAVVILVTDVSVDSVDAAAEAARSN-RVTVFPIGIGDRYS--EAQLSSLAG 1841
Cdd:cd01476    80 TATGAAIEVALQQLD-PSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDPGTvdTEELHSITG 155
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1497-1643 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 334191706 1497 LDVVFVLEGSDKIGEAnFNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVT--VEYTFSEAQSKGEVLQQVRDIRYRGGN 1574
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706 1575 rTNTGLALQYLSEHsFSVSQGDREQVPNLVYMVTGNPASDEIKRM-------PGdIQVVPIGVGPHANV--QELEKIG 1643
Cdd:cd01476    80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQarilravPN-IETFAVGTGDPGTVdtEELHSIT 154
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1497-1638 6.96e-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: 6.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1497 LDVVFVLEGSDKIGEAN-FNKSREFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFSE--AQSKGEVLQQVRDIR---Y 1570
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslyY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706 1571 RGGNrTNTGLALQYLSEHSFSvSQGDREQVPNLVYMVT-GNPASD--------EIKRMPGDIQVvpIGVGPHANVQE 1638
Cdd:cd01471    81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEE 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 1.59e-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: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVA 1355
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1356 STSEVLKYTLfQIFGKIDRPEASRIaLLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIHLIEKQAPEN 1435
Cdd:cd00198    81 NIGAALRLAL-ELLKSAKRPNARRV-IILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGG 158


                  ...
gi 334191706 1436 KAF 1438
Cdd:cd00198   159 AVF 161
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 2.57e-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: 2.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706  652 CPQGQVYLQCGTPCNMTCRSLSYPEeDCNEVCLEGCFCPPGLYLDERGDCVPKAQC 707
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 ...
 1691-1867 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 334191706 1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITTIDVPWNVAYEKVHLLSLVDLMQQEGG-PSQ 1769
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1770 IGDALSFAVRYVTSEVHGAR--PGASKAVVILVTDVSVDSVDAAAEAARSNRvtVFPIGIGDRyseaqlsslagpkaGSN 1847
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAG--IVPFAIGAR--------------NAD 145

                         170       180
                  ....*....|....*....|
gi 334191706 1848 MVRLQRIEDLPTVATLGNSF 1867
Cdd:cd01481   146 LAELQQIAFDPSFVFQVSDF 165
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 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 334191706  295 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLDE-GHCVGSAEC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 2.76e-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: 2.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706   295 CPAGMEYKECVSPCTRTCQSLHVKEVCQEQCVDGCSCPEGQLLD-EGHCVGSAEC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 3.26e-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: 3.26e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706   652 CPQGQVYLQCGTPCNMTCRSLSYPEEdCNEVCLEGCFCPPGLYLDERGDCVPKAQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 8.18e-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: 8.18e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706    579 FAEEACALLTSSK--FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHI-AWREPGFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1688-1862 5.69e-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: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1688 QPLDVVLLLDGSSSIPA-SYFDEMKSFTKAFISRanIGPRlTQVSVLQYGsiTTIDVPWNVAYEKVHLLSLVDLMQQEGG 1766
Cdd:COG1240    91 RGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDD--YRPR-DRVGLVAFG--GEAEVLLPLTRDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1767 pSQIGDALSFAVRYVTSEVHGARPgaskaVVILVTD----VSVDSVDAAAEAARSNRVTVFPIGIG-DRYSEAQLSSLAG 1841
Cdd:COG1240   166 -TPLGDALALALELLKRADPARRK-----VIVLLTDgrdnAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE 239

                         170       180
                  ....*....|....*....|.
gi 334191706 1842 pKAGSNMVRLQRIEDLPTVAT 1862
Cdd:COG1240   240 -ATGGRYFRADDLSELAAIYR 259
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 7.18e-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: 7.18e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706  2138 HCQVLL-SELFAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFC 2199
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGddecLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 7.64e-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: 7.64e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706   584 CALLTSSK-FEPCHRAVGPQPYVQNCRYDVCSCSDGRDCLCSAVANYAAACARRGVHIA-WREPGFC 648
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2134-2200 1.53e-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: 1.53e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334191706   2134 SSSSHCQVLLSEL--FAECHKVLAPATFYAMCQPDSCHPKK----VCEAIALYAHLCRTKGVCV-DWRRANFCA 2200
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1276-1349 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 334191706 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKY 1349
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 ...
 1689-1840 7.42e-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: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1689 PLDVVLLLDGSSSIPASYFDEMKSFTKAFISR------ANIGPRLTQVSVLQY-GSITTIDVPWNVAYEKVHLLSLVDLM 1761
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1762 QQEGGPSQIGDALsfavRYVTSEVHGARPGASKAVVILVTDVSVDSVDA-----AAEAARSNRVTVFPIGIGDRYSEaQL 1836
Cdd:cd01480    82 EYIGGGTFTDCAL----KYATEQLLEGSHQKENKFLLVITDGHSDGSPDggiekAVNEADHLGIKIFFVAVGSQNEE-PL 156


                  ....
gi 334191706 1837 SSLA 1840
Cdd:cd01480   157 SRIA 160
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1277-1425 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 334191706 1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAs 1356
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334191706 1357 TSEVLKYTLFQIFGKIDRPEAS--RIALLLMASQEPSRLARNLVRyvqgLKKKKVIVIPVGIGPHAS--LKQI 1425
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 ...
 1497-1587 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 334191706 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRM------DVGQDRIHVTVLQYSYMVTVEYTF-SEAQSKGEVLQQVRDIR 1569
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLE 82

                          90
                  ....*....|....*...
gi 334191706 1570 YRGGNrTNTGLALQYLSE 1587
Cdd:cd01480    83 YIGGG-TFTDCALKYATE 99
VWA_2 pfam13519
von Willebrand factor type A domain;
1692-1800 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 334191706  1692 VVLLLDGSSSIPA-----SYFDEMKSFTKAFISRANIgprlTQVSVLQYGSITTIDVPWNVAYEkvHLLSLVDLMQQEGG 1766
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTKDRA--KILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 334191706  1767 PSQIGDALSFAVRYVtsevhGARPGASKAVVILV 1800
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 ...
 1277-1397 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 334191706 1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEvAS 1356
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 334191706 1357 TSEVLKYTLFQIF--GKIDRPEASRIALLLM--ASQ----EPSRLARNL 1397
Cdd:cd01482    81 TGKALTHVREKNFtpDAGARPGVPKVVILITdgKSQddveLPARVLRNL 129
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 5.18e-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: 5.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 334191706 1146 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1196
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 ...
 1277-1381 8.56e-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: 8.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGSEVAS 1356
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100
                  ....*....|....*....|....*
gi 334191706 1357 TSEVLKYTLFQIFgkiDRPEASRIA 1381
Cdd:cd01481    82 TGSALDYVVKNLF---TKSAGSRIE 103
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 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 334191706  2431 CVHRGTIYPVGQFWEEA-CDVCTCTDledsvmglRVAQCSQKPCEDNCLSGFTYVLHEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1690-1841 3.33e-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: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1690 LDVVLLLDGSSSI-PASYFDEMKSFTKAFISRANIGPRLTQVSVLQYGSITT--IDVPWNVAYEKVHLLSLV-DL--MQQ 1763
Cdd:cd01471     1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKelIRLSSPNSTNKDLALNAIrALlsLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1764 EGGPSQIGDALSfAVRYVTSEVHGARPGASKAVVILvTDVSVDSVDAAAEAARSNR-----VTVFPIGIGDRYSEAQlsS 1838
Cdd:cd01471    81 PNGSTNTTSALL-VVEKHLFDTRGNRENAPQLVIIM-TDGIPDSKFRTLKEARKLRergviIAVLGVGQGVNHEENR--S 156


                  ...
gi 334191706 1839 LAG 1841
Cdd:cd01471   157 LVG 159
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1276-1445 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 334191706 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSELRRITSQVKYAGsEVA 1355
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLL-GLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1356 STSEVLKYTLFQIF--GKIDRPEASRIALLLM--ASQEPSRLARNLvryvQGLKKKKVIVIPVGIGPH----ASLKQIHL 1427
Cdd:cd01469    80 NTATAIQYVVTELFseSNGARKDATKVLVVITdgESHDDPLLKDVI----PQAEREGIIRYAIGVGGHfqreNSREELKT 155

                         170
                  ....*....|....*...
gi 334191706 1428 IEKQAPEnkAFVFSGVDE 1445
Cdd:cd01469   156 IASKPPE--EHFFNVTDF 171
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 7.07e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.28  E-value: 7.07e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334191706   2261 DGVRHQFLETWVPAhqPCQICTCLSGRKVNCTLQPCPTARaptcgPCEVARLRQNAEQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 1.04e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 47.90  E-value: 1.04e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334191706   2431 CVHRGTIYPVGQFW-EEACDVCTCTDLEdsvmglrVAQCSQKPCEDN--CLSGFTyVLHEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWkPDPCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 2.23e-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: 2.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 334191706  1146 YNSCAPACPITCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCIDPEDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 3.57e-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: 3.57e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2582 CLLNGTIIGPGKSLMIDVCTTCRCTVqvgvisgFKLECRKTTCEA--CPLGYkEEKNQGECCGRC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1276-1417 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 334191706 1276 LDLVFLLDGSSKLSE-DEFEVLKVFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKD--RKRPSELRRITSQVK--YA 1350
Cdd:cd01471     1 LDLYLLVDGSGSIGYsNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslYY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334191706 1351 GSEVASTSEVLKYTLFQIF-GKIDRPEASRIAlLLMASQEPSRLARNLvRYVQGLKKKKVIVIPVGIG 1417
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFdTRGNRENAPQLV-IIMTDGIPDSKFRTL-KEARKLRERGVIIAVLGVG 146
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2260-2322 3.94e-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: 3.94e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334191706  2260 EDGVRHQFLETWVPAhqPCQICTCLSGrKVNCTLQPCPTAraptcgPCEVARLRQNAEQCCPE 2322
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 4.69e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.97  E-value: 4.69e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334191706   2582 CLLNGTIIGPGKSLMIDVCTTCRCTVQVgVISGFKLECRKTTceACPLGYKeEKNQGECCGRC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1691-1840 4.65e-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: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1691 DVVLLLDGSSSIPASYFDEMKSFTKAFISRANigPRLtQVSVLQYGSITTIDVPWNVAYEkvhLLSLVDLMQQ---EGGp 1767
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTEVVEDLPLTADDG---LEDAIEFLSGlfaGGG- 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334191706 1768 SQIGDALSFAVRYVTsevhgaRPGASKAVVILVTD--VSVDSVDAAAEA-ARSNRVTVFPIGIGDRYSEAQLSSLA 1840
Cdd:COG2425   193 TDIAPALRAALELLE------EPDYRNADIVLITDgeAGVSPEELLREVrAKESGVRLFTVAIGDAGNPGLLEALA 262
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1687-1842 5.32e-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: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1687 SQPLDVVLLLDGSSSIPASYFDEMKSFTKAFIS--RANIGPRLT-QVSVLQYGSITTIDVPWnVAYEKVHLLSLVDlmqq 1763
Cdd:COG4245     3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDelRQDPYALETvEVSVITFDGEAKVLLPL-TDLEDFQPPDLSA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1764 eGGPSQIGDALSFA-------VRYVTSEVHGARpgasKAVVILVTD--VSVDSVDAAAEAARS----NRVTVFPIGIGDR 1830
Cdd:COG4245    78 -SGGTPLGAALELLldlierrVQKYTAEGKGDW----RPVVFLITDgePTDSDWEAALQRLKDgeaaKKANIFAIGVGPD 152

                         170
                  ....*....|..
gi 334191706 1831 YSEAQLSSLAGP 1842
Cdd:COG4245   153 ADTEVLKQLTDP 164
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1498-1620 6.11e-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: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1498 DVVFVLEGSDKIGEANFNKS-REFMEEVIQRMDVGQDRIHVTVLQYSYMVTVEYTFS--EAQSKGEVLQQVRDIR--YRG 1572
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeERYDKNELLKKINDLKnsYRS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 334191706 1573 GNRTNTGLALQYlSEHSFSVSQGDREQVPNLVYMVT-GNPASDEIKRMP 1620
Cdd:cd01473    82 GGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTdGNDTSASKKELQ 129
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 7.58e-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: 7.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706 2203 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVM-LEGSCVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 1.70e-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: 1.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334191706  2203 CPPSLVYNHCEHGCPRLCE--GNTSSCGDQPSEGCFCPPNQVML-EGSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1690-1828 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 334191706 1690 LDVVLLLDGSSSIPASYFDEMKSFTKAFISRANIGPrLTQVSVlqYGSITTIDVPWNVAyekvhlLSLVDLMQQE----- 1764
Cdd:cd01464     4 LPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDP-YALESV--EISVITFDSAARVI------VPLTPLESFQpprlt 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334191706 1765 -GGPSQIGDALSFAVRYVTSEV---HGARPGASKAVVILVTD-VSVDSVDAAAEA---ARSNRVTVFPIGIG 1828
Cdd:cd01464    75 aSGGTSMGAALELALDCIDRRVqryRADQKGDWRPWVFLLTDgEPTDDLTAAIERikeARDSKGRIVACAVG 146
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1277-1445 4.59e-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: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1277 DLVFLLDGSSKLSEDEF--EVLKvFVVGMMEHLHISQKRIRVAVVEYHDGSHAYIELKDRKRPSE---LRRITSQVKYAG 1351
Cdd:cd01473     2 DLTLILDESASIGYSNWrkDVIP-FTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKnelLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334191706 1352 SEVAS-TSEVLKYTLFQIFGKIDRPEAS-RIALLLMASQEPSRLARNLVRYVQGLKKKKVIVIPVGIGphaslkqihlie 1429
Cdd:cd01473    81 SGGETyIVEALKYGLKNYTKHGNRRKDApKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVG------------ 148

                         170
                  ....*....|....*.
gi 334191706 1430 kQAPENKAFVFSGVDE 1445
Cdd:cd01473   149 -AASENKLKLLAGCDI 163
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
350-394 5.07e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 37.93  E-value: 5.07e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 334191706    350 CVHAGQRYPPGASLLQDCHTCICRNSLWICSNEEC-PGECLVTGQS 394
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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