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Conserved domains on  [gi|449083357|ref|NP_446341|]
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von Willebrand factor precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.08e-43

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: 156.76  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   388 CLVTGQSHFKSFDNRHFTFSGICQYLLARDC-QDHSFSIVIETMQCADDPDAVCTRSVSVRLSALHNSLmklKHGGGVAI 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITL---QKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   467 DGQDVQIPFLQGDLRIQHTV--MASVRLSYGEDLQMEWDGRGRLLVKLSPIYSGKTCGLCGNYNGNKGDDFLTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 2.28e-41

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 150.89  E-value: 2.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVT-GNPASDEIRRL-----PGDIQVVPIGVGSrANLQELERIS---RPIAP 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGN-ADDEELRKIAsepGEGHV 159

                          170
                   ....*....|
gi 449083357  1649 IFIQDFETLP 1658
Cdd:pfam00092  160 FTVSDFEALE 169
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 4.00e-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: 4.00e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357  1198 VCEVAGRRLASGKKITLSPNDPQHCQNCHCDGVNLTCEACQEPGGLVVPPTDAPVSSTTPYVEDTPEPPLHNFYCSKLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 1.56e-37

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: 139.46  E-value: 1.56e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    856 WNCTTHVCDATCSALGMAHYLTFDGLKYLFPGECQYVLVQDyCgGSSGTFRILVGNEGCTyPSVKCKKRVTILVDGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-C-SSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    936 LFNGEV-------NVKRPLKDESHFEMVES-GQYVILLLGQGL-SVVWDHRLSISVVLKYTYQEHVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 449083357   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1691-1862 3.07e-36

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 136.25  E-value: 3.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVD-LMQQEGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1770 IGNALAFAVRYVTSQIHGARPGASKAVVMIIMDTSLD-SVDTAVDAARSNRVAVFPIGVGDRyDEAQLRILAGPGASSNV 1848
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGHV 159

                          170
                   ....*....|....
gi 449083357  1849 VKLQQVEDLLTMVT 1862
Cdd:pfam00092  160 FTVSDFEALEDLQD 173
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 4.46e-35

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: 132.11  E-value: 4.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    35 CSLFGDGFINTFDEAMYSFAGGCSYLLAGDCQKR---SFSILGNFQDGK-----RVGLSVYLGEFFdIHLFANGTVMQGD 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   107 QSISMPYASKGLYVEHEAGYYKISSEAFGFAARIDGDGNFQ--VLMSDRHFNKTCGLCGDFNIFAEDDFRTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 1.50e-33

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: 127.87  E-value: 1.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1950 CTGSSTRHIVTFDGQNFKLTGNCSYVIFQNKEQ--DLEVVLHNGACSPGAVQTCMKTIEVKHAGLSVELRSDMEMAVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2028 PVLAPYVGGNMQVSIYGAIMYEVRFtHLGHTLTFTPQNNEFQLQLSPKTFASKMYGLCGICDENGANDFTLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 3.38e-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: 104.84  E-value: 3.38e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1357 TSEVLKYTLFQIFGKID--RPEASRVILLLTaSQEPQRMARYFTRYLQGFKKKKVILIPVGIGPHANLKQIRLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 449083357   1435 NKAFLLSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 2.00e-20

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: 87.40  E-value: 2.00e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357   1053 QTMVDSSCRILTSD--IFQGCNRLVDPEPYLDICIYDTCSCEsiGDCSCFCDTIAAYAHVCAQHG-QVVAWRKPTLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 218-292 6.39e-18

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 80.46  E-value: 6.39e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357    218 QQAMWEQCQLLKTAS-VFARCHPLVDPEPFVALCEKTLCTCVTGPECACPALLEYARTCAQEGMVLYGWADHSACR 292
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2726-2807 5.88e-15

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: 72.05  E-value: 5.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   2726 ITAKVQYIKVGDCKSEEeVDIHYCQGKCASKAVYSIdiEDLQEQCSCCWPSSTERMRVPLLCTNGSVVHHEVINAMQCRC 2805
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 449083357   2806 SP 2807
Cdd:smart00041   78 EP 79
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 1.53e-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: 65.05  E-value: 1.53e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357    579 FAEEACALLTSSK--FETCHHAVSPLPYLQNCRYDVCSCADSQDCLCSAVANYAAACARKGVHI-GWREPDFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 2.08e-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: 63.88  E-value: 2.08e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  295 CPAGMEYKECVSPCTRTCQSLPINEVCQQQCVDGCGCPEGELLDED-RCVQSSDC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 2.18e-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: 63.88  E-value: 2.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357  652 CPQGQVYLQCGNSCNMTCRSLSLPdEECSEVCLEGCFCPPGLYQDERGDCVPKAQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 2.72e-12

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: 63.94  E-value: 2.72e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357  2138 HCQVLLSAS-FAECHKVIAPATFHTICQQDSCH----QERVCEVIASYAHLCRTNGVCV-DWRTTDFC 2199
Cdd:pfam08742    1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 1.98e-07

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 49.82  E-value: 1.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   2431 CVHRGTVYPVGQFWEEG-CDTCTCTDMEdtvvglrVAQCSQKPCEDS--CQPGFSyVLHEGECCGKC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 2.43e-07

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: 49.62  E-value: 2.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 449083357 1146 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDAQDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2257-2321 2.99e-06

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 46.74  E-value: 2.99e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   2257 CVGDdGVRHQFLETWVPDhqPCQICMCLSGRKINCTAQPCPTARaptcgPCEVARLKQSADLCCP 2321
Cdd:smart00214    1 CVHN-GRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2581-2643 1.78e-05

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: 44.34  E-value: 1.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2581 CLLNGTIIGPGKSVMVDLCTTCRCIvqrgaifRFKLECRKTTCEA--CPVGyREEKSQSECCGRC 2643
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNP-RLEIPPGECCPVC 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 1.57e-04

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: 41.53  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357 2203 CPPSLIYNHCERGCPRYCD--GNTSFCGDHPSEGCFCPQHQVL-LEGSCVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 4.11e-03

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: 37.68  E-value: 4.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 449083357  788 CAKTCQNYDL--ECmSLGCVSGCLCPPGMVRHEN-RCVALERC 827
Cdd:cd19941    14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.08e-43

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: 156.76  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   388 CLVTGQSHFKSFDNRHFTFSGICQYLLARDC-QDHSFSIVIETMQCADDPDAVCTRSVSVRLSALHNSLmklKHGGGVAI 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITL---QKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   467 DGQDVQIPFLQGDLRIQHTV--MASVRLSYGEDLQMEWDGRGRLLVKLSPIYSGKTCGLCGNYNGNKGDDFLTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 2.37e-43

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: 156.41  E-value: 2.37e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    377 WICSNEECPGECLVTGQSHFKSFDNRHFTFSGICQYLLARDCQDH-SFSIVIETMQCadDPDAVCTRSVSVRlsaLHNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVE---LNGDE 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    456 MKLKHGGG-VAIDGQDVQIPFLQGDLRIQHTV---MASVRLSYGeDLQMEWDGRGRLLVKLSPIYSGKTCGLCGNYNGNK 531
Cdd:smart00216   76 IELKDDNGkVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 449083357    532 GDDFLTPAG 540
Cdd:smart00216  155 EDDFRTPDG 163
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 2.28e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 150.89  E-value: 2.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVT-GNPASDEIRRL-----PGDIQVVPIGVGSrANLQELERIS---RPIAP 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGN-ADDEELRKIAsepGEGHV 159

                          170
                   ....*....|
gi 449083357  1649 IFIQDFETLP 1658
Cdd:pfam00092  160 FTVSDFEALE 169
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 4.00e-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: 4.00e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357  1198 VCEVAGRRLASGKKITLSPNDPQHCQNCHCDGVNLTCEACQEPGGLVVPPTDAPVSSTTPYVEDTPEPPLHNFYCSKLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1643 7.00e-38

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: 140.50  E-value: 7.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRT 1576
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357 1577 NTGQALQYLSEHSFSPSQgDREQAPNLVYMVT-GNP--------ASDEIRRLpgDIQVVPIGVGSrANLQELERIS 1643
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIA 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 1.56e-37

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: 139.46  E-value: 1.56e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    856 WNCTTHVCDATCSALGMAHYLTFDGLKYLFPGECQYVLVQDyCgGSSGTFRILVGNEGCTyPSVKCKKRVTILVDGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-C-SSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    936 LFNGEV-------NVKRPLKDESHFEMVES-GQYVILLLGQGL-SVVWDHRLSISVVLKYTYQEHVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 449083357   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1691-1862 3.07e-36

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 136.25  E-value: 3.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVD-LMQQEGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1770 IGNALAFAVRYVTSQIHGARPGASKAVVMIIMDTSLD-SVDTAVDAARSNRVAVFPIGVGDRyDEAQLRILAGPGASSNV 1848
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGHV 159

                          170
                   ....*....|....
gi 449083357  1849 VKLQQVEDLLTMVT 1862
Cdd:pfam00092  160 FTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1657 5.29e-36

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: 135.66  E-value: 5.29e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVT-GNP---------ASDEIRRLPgdIQVVPIGVGSRANLQELERISRPIA 1647
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|
gi 449083357   1648 PIFIQDFETL 1657
Cdd:smart00327  159 GVYVFLPELL 168
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 4.46e-35

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: 132.11  E-value: 4.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    35 CSLFGDGFINTFDEAMYSFAGGCSYLLAGDCQKR---SFSILGNFQDGK-----RVGLSVYLGEFFdIHLFANGTVMQGD 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   107 QSISMPYASKGLYVEHEAGYYKISSEAFGFAARIDGDGNFQ--VLMSDRHFNKTCGLCGDFNIFAEDDFRTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 3.34e-34

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: 129.80  E-value: 3.34e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   867 CSALGMAHYLTFDGLKYLFPGECQYVLVQDYCGGSSGTFRILVGNEGCTYPSVkCKKRVTILVDGGEIEL-------FNG 939
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLqkggtvlVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357   940 EVnVKRPLKDES-HFEMVESGQ-YVILLLGQGLSVVWDHRLSISVVLKYTYQEHVCGLCGNFDGIQNNDFTSSS 1011
Cdd:pfam00094   80 QK-VSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 1.50e-33

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: 127.87  E-value: 1.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1950 CTGSSTRHIVTFDGQNFKLTGNCSYVIFQNKEQ--DLEVVLHNGACSPGAVQTCMKTIEVKHAGLSVELRSDMEMAVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2028 PVLAPYVGGNMQVSIYGAIMYEVRFtHLGHTLTFTPQNNEFQLQLSPKTFASKMYGLCGICDENGANDFTLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1859 9.30e-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: 123.72  E-value: 9.30e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQE-GGPSQ 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1770 IGNALAFAVRYVTSQIHGARPGASKAVVMI---IMDTSLDSVDTAVDAARSNRVAVFPIGVGDRYDEAQLRILAGPGASS 1846
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILItdgESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|...
gi 449083357   1847 NVVKLQQVEDLLT 1859
Cdd:smart00327  161 YVFLPELLDLLID 173
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 2.34e-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: 119.04  E-value: 2.34e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1938 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGNCSYVIFQN--KEQDLEVVLHNGACSPGAvqTCMKTIEVKHAGLSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   2016 L-RSDMEMAVNGRPVLAPYVGGNMQVSIYGAIMYEVRFTHLGH-TLTFTPQNNeFQLQLSPKtFASKMYGLCGICDENGA 2093
Cdd:smart00216   78 LkDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 449083357   2094 NDFTLRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 28-178 3.32e-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: 118.66  E-value: 3.32e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357     28 DRPSTARCSLFGDGFINTFDEAMYSFAGGCSYLLAGDCQKR-SFSILG-NFQDGKRVG--LSVYLGEFF-DIHLF-ANGT 101
Cdd:smart00216    5 QEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLkNVPCGGGATclKSVKVELNGdEIELKdDNGK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357    102 VMQGDQSISMPYASKGLYVEHE-AGYYKISSEAFGFA-ARIDGDGNFQVLMSDRHFNKTCGLCGDFNIFAEDDFRTQEG 178
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 8.06e-30

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: 117.39  E-value: 8.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1690 LDVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGP-S 1768
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1769 QIGNALAFAVRYVTSQiHGARPGASKaVVMIIMD---TSLDSVDTAVDAARSNRVAVFPIGVGDrYDEAQLRILAGPGAS 1845
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDgrsDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 449083357 1846 SNVV 1849
Cdd:cd01450   158 RHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 3.38e-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: 104.84  E-value: 3.38e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1357 TSEVLKYTLFQIFGKID--RPEASRVILLLTaSQEPQRMARYFTRYLQGFKKKKVILIPVGIGPHANLKQIRLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 449083357   1435 NKAFLLSGVDELEQR 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 2.17e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 101.98  E-value: 2.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLA 1355
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1356 STSEVLKYTLFQIFGKI-DRPEASRVILLLTASQepQRMARYFTRYLQGFKKKKVILIPVGIGPhANLKQIRLIEKQAPE 1434
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 449083357 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 2.00e-20

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: 87.40  E-value: 2.00e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357   1053 QTMVDSSCRILTSD--IFQGCNRLVDPEPYLDICIYDTCSCEsiGDCSCFCDTIAAYAHVCAQHG-QVVAWRKPTLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 218-292 6.39e-18

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 80.46  E-value: 6.39e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357    218 QQAMWEQCQLLKTAS-VFARCHPLVDPEPFVALCEKTLCTCVTGPECACPALLEYARTCAQEGMVLYGWADHSACR 292
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWA pfam00092
von Willebrand factor type A domain;
1277-1448 2.33e-17

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 81.94  E-value: 2.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYhdGSHAYLE--LRARKRPSELRRIASQIKYVGSQL 1354
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1355 ASTSEVLKYTLFQIFGKI--DRPEASRVILLLTA----SQEPQRMARYftrylqgFKKKKVILIPVGIGPHANlKQIRLI 1428
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKI 150

                          170       180
                   ....*....|....*....|
gi 449083357  1429 EKQAPENKAFLLSGVDELEQ 1448
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1060-1126 3.76e-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: 77.81  E-value: 3.76e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357  1060 CRILT-SDIFQGCNRLVDPEPYLDICIYDTCSCEsiGDCSCFCDTIAAYAHVCAQHGQVVA-WRKPTLC 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 2.56e-15

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: 72.80  E-value: 2.56e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357   224 QCQLLKTASVFARCHPLVDPEPFVALCEKTLCTCVTGPECACPALLEYARTCAQEGMVLYGWADHSAC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2726-2807 5.88e-15

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: 72.05  E-value: 5.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   2726 ITAKVQYIKVGDCKSEEeVDIHYCQGKCASKAVYSIdiEDLQEQCSCCWPSSTERMRVPLLCTNGSVVHHEVINAMQCRC 2805
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 449083357   2806 SP 2807
Cdd:smart00041   78 EP 79
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 1.53e-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: 65.05  E-value: 1.53e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357    579 FAEEACALLTSSK--FETCHHAVSPLPYLQNCRYDVCSCADSQDCLCSAVANYAAACARKGVHI-GWREPDFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 2.08e-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: 63.88  E-value: 2.08e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  295 CPAGMEYKECVSPCTRTCQSLPINEVCQQQCVDGCGCPEGELLDED-RCVQSSDC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 2.18e-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: 63.88  E-value: 2.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357  652 CPQGQVYLQCGNSCNMTCRSLSLPdEECSEVCLEGCFCPPGLYQDERGDCVPKAQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 2.72e-12

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: 63.94  E-value: 2.72e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357  2138 HCQVLLSAS-FAECHKVIAPATFHTICQQDSCH----QERVCEVIASYAHLCRTNGVCV-DWRTTDFC 2199
Cdd:pfam08742    1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 1.06e-11

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: 62.02  E-value: 1.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357   652 CPQGQVYLQCGNSCNMTCRSLSLPDEeCSEVCLEGCFCPPGLYQDERGDCVPKAQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2134-2200 3.97e-11

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: 61.20  E-value: 3.97e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357   2134 SDSSHCQVLLSAS--FAECHKVIAPATFHTICQQDSC----HQERVCEVIASYAHLCRTNGVCV-DWRTTDFCA 2200
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 9.04e-11

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: 59.32  E-value: 9.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   295 CPAGMEYKECVSPCTRTCQSLPINEVCQQQCVDGCGCPEGELLDED-RCVQSSDC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 4.83e-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: 57.78  E-value: 4.83e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   584 CALLTSSK-FETCHHAVSPLPYLQNCRYDVCSCADSQDCLCSAVANYAAACARKGVHIG-WREPDFC 648
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1688-1840 1.37e-08

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: 58.41  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1688 QPLDVVLLLDGSSSLPASS-FDEMKSFAKAFISKANIGphlTQVSVIQYGSinTIDVPWNVAQEKAYLQSLVDLMQQEGG 1766
Cdd:COG1240    91 RGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357 1767 pSQIGNALAFAVRYVTSqihgARPGASKAVVMI---IMDTSLDSVDTAVDAARSNRVAVFPIGVG-DRYDEAQLRILA 1840
Cdd:COG1240   166 -TPLGDALALALELLKR----ADPARRKVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIA 238
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 1.98e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 49.82  E-value: 1.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   2431 CVHRGTVYPVGQFWEEG-CDTCTCTDMEdtvvglrVAQCSQKPCEDS--CQPGFSyVLHEGECCGKC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 2.43e-07

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: 49.62  E-value: 2.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 449083357 1146 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDAQDC 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 9.12e-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: 48.19  E-value: 9.12e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2431 CVHRGTVYPVGQFWEEG-CDTCTCTDmedtvvglRVAQCSQKPCEDSCQPGFSYVLHEGECCGKC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 1.87e-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: 1.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 449083357  1146 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDAQDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2257-2321 2.99e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 46.74  E-value: 2.99e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   2257 CVGDdGVRHQFLETWVPDhqPCQICMCLSGRKINCTAQPCPTARaptcgPCEVARLKQSADLCCP 2321
Cdd:smart00214    1 CVHN-GRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2581-2643 1.78e-05

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 44.34  E-value: 1.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2581 CLLNGTIIGPGKSVMVDLCTTCRCIvqrgaifRFKLECRKTTCEA--CPVGyREEKSQSECCGRC 2643
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNP-RLEIPPGECCPVC 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 1.57e-04

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: 41.53  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357 2203 CPPSLIYNHCERGCPRYCD--GNTSFCGDHPSEGCFCPQHQVL-LEGSCVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2261-2322 1.58e-04

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 41.64  E-value: 1.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449083357  2261 DGVRHQFLETWVPDhqPCQICMCLSGrKINCTAQPCPTAraptcgPCEVARLKQSADLCCPE 2322
Cdd:pfam00093    4 NGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2581-2643 7.68e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 39.81  E-value: 7.68e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357   2581 CLLNGTIIGPGKSVMVDLCTTCRCIVQRgaifrfKLECRKTTCE---ACPVGYReEKSQSECCGRC 2643
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT------TVLCDPVECPpppDCPNPER-VKPPGECCPRC 59
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1459-1644 9.37e-04

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: 43.77  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1459 DLAPEAPAPTKPPQVAHITVSPGISGVSSPGPKRKSLVLDVVFVLEASDEVGEAN-FNKSKEFLEEVIQRMdvsPAGTHI 1537
Cdd:COG1240    55 GLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1538 AVLQYSYTVNVEYTFkeAQSKEDVLRHVREIRYQGGnrTNTGQALQYLSEHsfspSQGDREQAPNLVYMVT-GNP----- 1611
Cdd:COG1240   132 GLVAFGGEAEVLLPL--TRDREALKRALDELPPGGG--TPLGDALALALEL----LKRADPARRKVIVLLTdGRDnagri 203

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 449083357 1612 ----ASDEIRRLpgDIQVVPIGVGSRA-NLQELERISR 1644
Cdd:COG1240   204 dpleAAELAAAA--GIRIYTIGVGTEAvDEGLLREIAE 239
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 2.89e-03

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: 38.14  E-value: 2.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2203 CPPSLIYNHCERGCPRYCD--GNTSFCGDHPSEGCFCPQHQVLL-EGSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 4.11e-03

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: 37.68  E-value: 4.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 449083357  788 CAKTCQNYDL--ECmSLGCVSGCLCPPGMVRHEN-RCVALERC 827
Cdd:cd19941    14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.08e-43

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: 156.76  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   388 CLVTGQSHFKSFDNRHFTFSGICQYLLARDC-QDHSFSIVIETMQCADDPDAVCTRSVSVRLSALHNSLmklKHGGGVAI 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITL---QKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   467 DGQDVQIPFLQGDLRIQHTV--MASVRLSYGEDLQMEWDGRGRLLVKLSPIYSGKTCGLCGNYNGNKGDDFLTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 2.37e-43

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: 156.41  E-value: 2.37e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    377 WICSNEECPGECLVTGQSHFKSFDNRHFTFSGICQYLLARDCQDH-SFSIVIETMQCadDPDAVCTRSVSVRlsaLHNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVE---LNGDE 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    456 MKLKHGGG-VAIDGQDVQIPFLQGDLRIQHTV---MASVRLSYGeDLQMEWDGRGRLLVKLSPIYSGKTCGLCGNYNGNK 531
Cdd:smart00216   76 IELKDDNGkVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 449083357    532 GDDFLTPAG 540
Cdd:smart00216  155 EDDFRTPDG 163
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 2.28e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 150.89  E-value: 2.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVT-GNPASDEIRRL-----PGDIQVVPIGVGSrANLQELERIS---RPIAP 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGN-ADDEELRKIAsepGEGHV 159

                          170
                   ....*....|
gi 449083357  1649 IFIQDFETLP 1658
Cdd:pfam00092  160 FTVSDFEALE 169
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 4.00e-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: 4.00e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357  1198 VCEVAGRRLASGKKITLSPNDPQHCQNCHCDGVNLTCEACQEPGGLVVPPTDAPVSSTTPYVEDTPEPPLHNFYCSKLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1643 7.00e-38

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: 140.50  E-value: 7.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRT 1576
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357 1577 NTGQALQYLSEHSFSPSQgDREQAPNLVYMVT-GNP--------ASDEIRRLpgDIQVVPIGVGSrANLQELERIS 1643
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIA 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 1.56e-37

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: 139.46  E-value: 1.56e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    856 WNCTTHVCDATCSALGMAHYLTFDGLKYLFPGECQYVLVQDyCgGSSGTFRILVGNEGCTyPSVKCKKRVTILVDGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-C-SSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    936 LFNGEV-------NVKRPLKDESHFEMVES-GQYVILLLGQGL-SVVWDHRLSISVVLKYTYQEHVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 449083357   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1498-1643 2.62e-36

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: 136.20  E-value: 2.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNrTN 1577
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449083357 1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVTGNPASDEIrRLPG------DIQVVPIGVGSrANLQELERIS 1643
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDV-EEPAvelkqaGIEVFAVGVKN-ADEEELKQIA 150
VWA pfam00092
von Willebrand factor type A domain;
1691-1862 3.07e-36

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 136.25  E-value: 3.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVD-LMQQEGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1770 IGNALAFAVRYVTSQIHGARPGASKAVVMIIMDTSLD-SVDTAVDAARSNRVAVFPIGVGDRyDEAQLRILAGPGASSNV 1848
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGHV 159

                          170
                   ....*....|....
gi 449083357  1849 VKLQQVEDLLTMVT 1862
Cdd:pfam00092  160 FTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1657 5.29e-36

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: 135.66  E-value: 5.29e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVT-GNP---------ASDEIRRLPgdIQVVPIGVGSRANLQELERISRPIA 1647
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|
gi 449083357   1648 PIFIQDFETL 1657
Cdd:smart00327  159 GVYVFLPELL 168
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 4.46e-35

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: 132.11  E-value: 4.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357    35 CSLFGDGFINTFDEAMYSFAGGCSYLLAGDCQKR---SFSILGNFQDGK-----RVGLSVYLGEFFdIHLFANGTVMQGD 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   107 QSISMPYASKGLYVEHEAGYYKISSEAFGFAARIDGDGNFQ--VLMSDRHFNKTCGLCGDFNIFAEDDFRTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 3.34e-34

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: 129.80  E-value: 3.34e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   867 CSALGMAHYLTFDGLKYLFPGECQYVLVQDYCGGSSGTFRILVGNEGCTYPSVkCKKRVTILVDGGEIEL-------FNG 939
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLqkggtvlVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357   940 EVnVKRPLKDES-HFEMVESGQ-YVILLLGQGLSVVWDHRLSISVVLKYTYQEHVCGLCGNFDGIQNNDFTSSS 1011
Cdd:pfam00094   80 QK-VSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 1.50e-33

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: 127.87  E-value: 1.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1950 CTGSSTRHIVTFDGQNFKLTGNCSYVIFQNKEQ--DLEVVLHNGACSPGAVQTCMKTIEVKHAGLSVELRSDMEMAVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2028 PVLAPYVGGNMQVSIYGAIMYEVRFtHLGHTLTFTPQNNEFQLQLSPKTFASKMYGLCGICDENGANDFTLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1498-1643 2.02e-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: 127.83  E-value: 2.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRTN 1577
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449083357 1578 TGQALQYLSEHSFSPSQGDR--EQAPNLVYMVTGNPASDEIRRLPGDIQ---VVPIGVGSR-ANLQELERIS 1643
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGARnADLAELQQIA 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1859 9.30e-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: 123.72  E-value: 9.30e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQE-GGPSQ 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1770 IGNALAFAVRYVTSQIHGARPGASKAVVMI---IMDTSLDSVDTAVDAARSNRVAVFPIGVGDRYDEAQLRILAGPGASS 1846
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILItdgESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|...
gi 449083357   1847 NVVKLQQVEDLLT 1859
Cdd:smart00327  161 YVFLPELLDLLID 173
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1498-1645 1.22e-31

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: 122.78  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1498 DVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNrTN 1577
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357 1578 TGQALQYLSEHSFSPSQGDREQAPNLVYMVTGNPASDEIrRLPGD------IQVVPIGVgSRANLQELERI-SRP 1645
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGV-KDADESELKMIaSKP 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 2.34e-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: 119.04  E-value: 2.34e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1938 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGNCSYVIFQN--KEQDLEVVLHNGACSPGAvqTCMKTIEVKHAGLSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   2016 L-RSDMEMAVNGRPVLAPYVGGNMQVSIYGAIMYEVRFTHLGH-TLTFTPQNNeFQLQLSPKtFASKMYGLCGICDENGA 2093
Cdd:smart00216   78 LkDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 449083357   2094 NDFTLRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 28-178 3.32e-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: 118.66  E-value: 3.32e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357     28 DRPSTARCSLFGDGFINTFDEAMYSFAGGCSYLLAGDCQKR-SFSILG-NFQDGKRVG--LSVYLGEFF-DIHLF-ANGT 101
Cdd:smart00216    5 QEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLkNVPCGGGATclKSVKVELNGdEIELKdDNGK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357    102 VMQGDQSISMPYASKGLYVEHE-AGYYKISSEAFGFA-ARIDGDGNFQVLMSDRHFNKTCGLCGDFNIFAEDDFRTQEG 178
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 8.06e-30

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: 117.39  E-value: 8.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1690 LDVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGP-S 1768
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1769 QIGNALAFAVRYVTSQiHGARPGASKaVVMIIMD---TSLDSVDTAVDAARSNRVAVFPIGVGDrYDEAQLRILAGPGAS 1845
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDgrsDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 449083357 1846 SNVV 1849
Cdd:cd01450   158 RHVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1497-1657 1.68e-27

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: 112.86  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRY--QGgn 1574
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1575 rTNTGQALQYLSEHSFSPSQGDR---EQAPNLVYMVTGNPASDEIR------RLPGdIQVVPIGVGsRANLQELERI-SR 1644
Cdd:cd01475    81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIaSE 157

                         170
                  ....*....|....*
gi 449083357 1645 PIAP--IFIQDFETL 1657
Cdd:cd01475   158 PLADhvFYVEDFSTI 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 3.38e-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: 104.84  E-value: 3.38e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   1357 TSEVLKYTLFQIFGKID--RPEASRVILLLTaSQEPQRMARYFTRYLQGFKKKKVILIPVGIGPHANLKQIRLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 449083357   1435 NKAFLLSGVDELEQR 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 2.17e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 101.98  E-value: 2.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLA 1355
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1356 STSEVLKYTLFQIFGKI-DRPEASRVILLLTASQepQRMARYFTRYLQGFKKKKVILIPVGIGPhANLKQIRLIEKQAPE 1434
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 449083357 1435 NKAF 1438
Cdd:cd01450   158 RHVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 7.72e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 97.64  E-value: 7.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1690 LDVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQE-GGPS 1768
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1769 QIGNALAFAVRYVTSQihgARPGASKAVVMI---IMDTSLDSVDTAVDAARSNRVAVFPIGVGDRYDEAQLRILAGPGAS 1845
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLtdgEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG 157


                  ....
gi 449083357 1846 SNVV 1849
Cdd:cd00198   158 GAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1645 2.44e-22

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: 96.10  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGNRT 1576
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357 1577 NTGQALQYLSEHSFSPsqgDREQAPNLVYMVT-GNP---------ASDEIRRLpgDIQVVPIGVGSRANLQELERISRP 1645
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEIADK 154
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1691-1850 5.17e-22

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: 94.99  E-value: 5.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGPSQI 1770
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1771 GNALAFAVRYVTSQIHGARPGASKAVVMIIMDTSLDSVDTAVDAARSNRVAVFPIGVGDRyDEAQLRILAGPGASSNVVK 1850
Cdd:cd01472    82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNA-DEEELKQIASDPKELYVFN 160
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1690-1831 8.29e-21

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: 92.03  E-value: 8.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1690 LDVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGPSQ 1769
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357 1770 IGNALAFAVRYVTSQIHGARPGASKavVMIIM------DTSLDSvdTAVDAARSNRVAVFPIGVGDRY 1831
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATK--VLVVItdgeshDDPLLK--DVIPQAEREGIIRYAIGVGGHF 144
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 2.00e-20

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: 87.40  E-value: 2.00e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357   1053 QTMVDSSCRILTSD--IFQGCNRLVDPEPYLDICIYDTCSCEsiGDCSCFCDTIAAYAHVCAQHG-QVVAWRKPTLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1497-1657 3.10e-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: 90.49  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKEAQSKEDVLRHVREIRYQGGnRT 1576
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1577 NTGQALQYLSEHSFSPSQGDREQAPNLVYMVTGNPASDEirrlPGDIQVVP-----------IGVGSRAN----LQELER 1641
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDD----PLLKDVIPqaeregiiryaIGVGGHFQrensREELKT 155

                         170
                  ....*....|....*....
gi 449083357 1642 I-SRPIAPIFIQ--DFETL 1657
Cdd:cd01469   156 IaSKPPEEHFFNvtDFAAL 174
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1497-1651 2.35e-19

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: 87.45  E-value: 2.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEAnFNKSKEFLEEVIQRMDVSPAGTHIAVLQYS--YTVNVEYTFKEAQSKEDVLRHVREIRYQGGN 1574
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1575 rTNTGQALQYLSEHsFSPSQGDREQAPNLVYMVTG-----NP--ASDEIRRLPGdIQVVPIGVGSRANL--QELERISRP 1645
Cdd:cd01476    80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDgrshdDPekQARILRAVPN-IETFAVGTGDPGTVdtEELHSITGN 156


                  ....*.
gi 449083357 1646 IAPIFI 1651
Cdd:cd01476   157 EDHIFT 162
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1689-1889 1.01e-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: 87.44  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1689 PLDVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGPS 1768
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1769 QIGNALAFAVRYVTSQIHGARPGASKA--VVMIIMD-TSLDSVDTAVDAARSNRVAVFPIGVGdRYDEAQLRILAGPGAS 1845
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVprVGIVVTDgRPQDDVSEVAAKARALGIEMFAVGVG-RADEEELREIASEPLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 449083357 1846 SNVVklqQVEDLLTMVTPGNSFFHRLCSGfSGVCVDEDGNEKRP 1889
Cdd:cd01475   161 DHVF---YVEDFSTIEELTKKFQGKICVV-PDLCATLSHVCQQV 200
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 218-292 6.39e-18

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 80.46  E-value: 6.39e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357    218 QQAMWEQCQLLKTAS-VFARCHPLVDPEPFVALCEKTLCTCVTGPECACPALLEYARTCAQEGMVLYGWADHSACR 292
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWA pfam00092
von Willebrand factor type A domain;
1277-1448 2.33e-17

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 81.94  E-value: 2.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYhdGSHAYLE--LRARKRPSELRRIASQIKYVGSQL 1354
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1355 ASTSEVLKYTLFQIFGKI--DRPEASRVILLLTA----SQEPQRMARYftrylqgFKKKKVILIPVGIGPHANlKQIRLI 1428
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKI 150

                          170       180
                   ....*....|....*....|
gi 449083357  1429 EKQAPENKAFLLSGVDELEQ 1448
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1060-1126 3.76e-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: 77.81  E-value: 3.76e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449083357  1060 CRILT-SDIFQGCNRLVDPEPYLDICIYDTCSCEsiGDCSCFCDTIAAYAHVCAQHGQVVA-WRKPTLC 1126
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1691-1842 5.42e-17

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: 80.79  E-value: 5.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGPSQI 1770
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449083357 1771 GNALAFAVRYVTSQIHGARPGASKAVVMIIMDTSLDSVDTAVDAARSNRVAVFPIGVGDrYDEAQLRILAGP 1842
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKD-ADESELKMIASK 152
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1690-1841 3.70e-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: 78.21  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1690 LDVVLLLDGSSSLpASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVA--QEKAYLQSLVDLMQQEGGP 1767
Cdd:cd01476     1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPkhNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357 1768 SQIGNALAFAVRYVTSQiHGARPGASKAVVMIIMDTSLDSVDTAVDAARSN-RVAVFPIGVGDR--YDEAQLRILAG 1841
Cdd:cd01476    80 TATGAAIEVALQQLDPS-EGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDPgtVDTEELHSITG 155
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 2.56e-15

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: 72.80  E-value: 2.56e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357   224 QCQLLKTASVFARCHPLVDPEPFVALCEKTLCTCVTGPECACPALLEYARTCAQEGMVLYGWADHSAC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1497-1638 3.63e-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: 76.27  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEAN-FNKSKEFLEEVIQRMDVSPAGTHIAVLQYSYTVNVEYTFKE--AQSKE---DVLRHVREIRY 1570
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDlalNAIRALLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357 1571 QGGNrTNTGQALQYLSEHSFSpSQGDREQAPNLVYMVT-GNPASD--------EIRRLPGDIQVvpIGVGSRANLQE 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 5.22e-15

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: 74.91  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLA 1355
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1356 STSEVLKYTLfQIFGKIDRPEASRVILLLT--ASQEPQRMARYFTRYLqgfKKKKVILIPVGIGPHANLKQIRLIEKQAP 1433
Cdd:cd00198    81 NIGAALRLAL-ELLKSAKRPNARRVIILLTdgEPNDGPELLAEAAREL---RKLGITVYTIGIGDDANEDELKEIADKTT 156


                  ....*
gi 449083357 1434 ENKAF 1438
Cdd:cd00198   157 GGAVF 161
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2726-2807 5.88e-15

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: 72.05  E-value: 5.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357   2726 ITAKVQYIKVGDCKSEEeVDIHYCQGKCASKAVYSIdiEDLQEQCSCCWPSSTERMRVPLLCTNGSVVHHEVINAMQCRC 2805
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 449083357   2806 SP 2807
Cdd:smart00041   78 EP 79
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1691-1840 3.06e-14

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: 72.74  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1691 DVVLLLDGSSSLPASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGG-PSQ 1769
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449083357 1770 IGNALAFAVRYVTSQIHGAR--PGASKAVVMIIMDTSLDSVDTAVDAARSNRVAVFPIGVGDrYDEAQLRILA 1840
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARN-ADLAELQQIA 153
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 1.53e-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: 65.05  E-value: 1.53e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357    579 FAEEACALLTSSK--FETCHHAVSPLPYLQNCRYDVCSCADSQDCLCSAVANYAAACARKGVHI-GWREPDFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 2.08e-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: 63.88  E-value: 2.08e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  295 CPAGMEYKECVSPCTRTCQSLPINEVCQQQCVDGCGCPEGELLDED-RCVQSSDC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 2.18e-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: 63.88  E-value: 2.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357  652 CPQGQVYLQCGNSCNMTCRSLSLPdEECSEVCLEGCFCPPGLYQDERGDCVPKAQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 2.72e-12

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: 63.94  E-value: 2.72e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357  2138 HCQVLLSAS-FAECHKVIAPATFHTICQQDSCH----QERVCEVIASYAHLCRTNGVCV-DWRTTDFC 2199
Cdd:pfam08742    1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1277-1390 6.57e-12

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: 66.10  E-value: 6.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLAs 1356
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 449083357 1357 TSEVLKYTLFQIFGKIDRPEAS--RVILLLTASQEP 1390
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQ 116
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 1.06e-11

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: 62.02  E-value: 1.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357   652 CPQGQVYLQCGNSCNMTCRSLSLPDEeCSEVCLEGCFCPPGLYQDERGDCVPKAQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2134-2200 3.97e-11

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: 61.20  E-value: 3.97e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449083357   2134 SDSSHCQVLLSAS--FAECHKVIAPATFHTICQQDSC----HQERVCEVIASYAHLCRTNGVCV-DWRTTDFCA 2200
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 9.04e-11

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: 59.32  E-value: 9.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   295 CPAGMEYKECVSPCTRTCQSLPINEVCQQQCVDGCGCPEGELLDED-RCVQSSDC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1277-1385 1.18e-10

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: 62.30  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSqLAS 1356
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NTR 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 449083357 1357 TSEVLKYTLFQIF--GKIDRPEASRVILLLT 1385
Cdd:cd01482    81 TGKALTHVREKNFtpDAGARPGVPKVVILIT 111
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1497-1592 3.38e-10

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: 61.63  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRM------DVSPAGTHIAVLQYSYTVNVEYTF-KEAQSKEDVLRHVREIR 1569
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLE 82

                          90       100
                  ....*....|....*....|....*..
gi 449083357 1570 YQGGNrTNTGQALQY----LSEHSFSP 1592
Cdd:cd01480    83 YIGGG-TFTDCALKYateqLLEGSHQK 108
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 4.83e-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: 57.78  E-value: 4.83e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   584 CALLTSSK-FETCHHAVSPLPYLQNCRYDVCSCADSQDCLCSAVANYAAACARKGVHIG-WREPDFC 648
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1276-1385 1.08e-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: 61.25  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVgSQLA 1355
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 449083357 1356 STSEVLKYTLFQIFGKID--RPEA---SRVILLLT 1385
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEgaRPGServPRVGIVVT 116
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1688-1840 1.37e-08

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: 58.41  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1688 QPLDVVLLLDGSSSLPASS-FDEMKSFAKAFISKANIGphlTQVSVIQYGSinTIDVPWNVAQEKAYLQSLVDLMQQEGG 1766
Cdd:COG1240    91 RGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449083357 1767 pSQIGNALAFAVRYVTSqihgARPGASKAVVMI---IMDTSLDSVDTAVDAARSNRVAVFPIGVG-DRYDEAQLRILA 1840
Cdd:COG1240   166 -TPLGDALALALELLKR----ADPARRKVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIA 238
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1277-1388 5.46e-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: 54.64  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1277 DLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSQLAS 1356
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 449083357 1357 TSEVLKYTLFQIFgkiDRPEASRV-------ILLLTASQ 1388
Cdd:cd01481    82 TGSALDYVVKNLF---TKSAGSRIeegvpqfLVLITGGK 117
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 1.98e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 49.82  E-value: 1.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449083357   2431 CVHRGTVYPVGQFWEEG-CDTCTCTDMEdtvvglrVAQCSQKPCEDS--CQPGFSyVLHEGECCGKC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 2.43e-07

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: 49.62  E-value: 2.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 449083357 1146 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDAQDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWA_2 pfam13519
von Willebrand factor type A domain;
1692-1799 2.52e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.14  E-value: 2.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1692 VVLLLDGSSS-----LPASSFDEMKSFAKAFISKANIgphlTQVSVIQYGSINTIDVPWNvaQEKAYLQSLVDLMQQEGG 1766
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 449083357  1767 PSQIGNALAFAvryvTSQIHGARPGASKAVVMI 1799
Cdd:pfam13519   75 GTNLAAALQLA----RAALKHRRKNQPRRIVLI 103
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1689-1859 6.70e-07

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 53.57  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1689 PLDVVLLLDGSSSLPASSFDEMKSFAKAFISkaNIGPHlTQVSVIQYGSINTIDVPWNVAQEKAYLQSLVDLMQQEGGpS 1768
Cdd:COG2304    91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVD--QLRPG-DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGG-T 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1769 QIGNALAFAVRYVTSqihGARPGASKAVVMI------IMDTSLDSVDTAVDAARSNRVAVFPIGVGDRYDEAQLRILA-- 1840
Cdd:COG2304   167 ALGAGLELAYELARK---HFIPGRVNRVILLtdgdanVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAda 243

                         170
                  ....*....|....*....
gi 449083357 1841 GPGASSNVVKLQQVEDLLT 1859
Cdd:COG2304   244 GGGNYYYIDDPEEAEKVFV 262
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1689-1844 8.73e-07

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: 51.62  E-value: 8.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1689 PLDVVLLLDGSSSLPASSFDEMKSFAKAFIS------KANIGPHLTQVSVIQY-GSINTIDVPWNVAQEKAYLQSLVDLM 1761
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1762 QQEGGPSQIGNALAfavrYVTSQIHGARPGASKAVVMIIMDTSLDSVD-----TAVDAARSNRVAVFPIGVGDRYDEAQL 1836
Cdd:cd01480    82 EYIGGGTFTDCALK----YATEQLLEGSHQKENKFLLVITDGHSDGSPdggieKAVNEADHLGIKIFFVAVGSQNEEPLS 157


                  ....*...
gi 449083357 1837 RILAGPGA 1844
Cdd:cd01480   158 RIACDGKS 165
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 9.12e-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: 48.19  E-value: 9.12e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2431 CVHRGTVYPVGQFWEEG-CDTCTCTDmedtvvglRVAQCSQKPCEDSCQPGFSYVLHEGECCGKC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 1.87e-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: 1.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 449083357  1146 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDAQDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2257-2321 2.99e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 46.74  E-value: 2.99e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357   2257 CVGDdGVRHQFLETWVPDhqPCQICMCLSGRKINCTAQPCPTARaptcgPCEVARLKQSADLCCP 2321
Cdd:smart00214    1 CVHN-GRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWA_2 pfam13519
von Willebrand factor type A domain;
1499-1607 3.48e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.67  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357  1499 VVFVLEAS-----DEVGEANFNKSKEFLEEVIQRMdvspAGTHIAVLQYSYTVNVEYTFKeaQSKEDVLRHVREIRYQGG 1573
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 449083357  1574 NrTNTGQALQYLSEHsfspSQGDREQAPNLVYMV 1607
Cdd:pfam13519   75 G-TNLAAALQLARAA----LKHRRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1690-1841 5.79e-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: 49.31  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1690 LDVVLLLDGSSSL-PASSFDEMKSFAKAFISKANIGPHLTQVSVIQYGSINT--IDVPWNVAQEKAYLQSLVDLMQQegG 1766
Cdd:cd01471     1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKelIRLSSPNSTNKDLALNAIRALLS--L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1767 PSQIGN-----ALAfAVRYVTSQIHGARPGASKAVvmIIM-DTSLDSVDTAVDAARSNR-----VAVfpIGVGDRYDEAQ 1835
Cdd:cd01471    79 YYPNGStnttsALL-VVEKHLFDTRGNRENAPQLV--IIMtDGIPDSKFRTLKEARKLRergviIAV--LGVGQGVNHEE 153


                  ....*.
gi 449083357 1836 LRILAG 1841
Cdd:cd01471   154 NRSLVG 159
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1276-1385 6.06e-06

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: 49.28  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRARKRPSELRRIASQIKYVGSqLA 1355
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 449083357 1356 STSEVLKYTLFQIF--GKIDRPEASRVILLLT 1385
Cdd:cd01469    80 NTATAIQYVVTELFseSNGARKDATKVLVVIT 111
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2581-2643 1.78e-05

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 44.34  E-value: 1.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2581 CLLNGTIIGPGKSVMVDLCTTCRCIvqrgaifRFKLECRKTTCEA--CPVGyREEKSQSECCGRC 2643
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNP-RLEIPPGECCPVC 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 1.57e-04

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: 41.53  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357 2203 CPPSLIYNHCERGCPRYCD--GNTSFCGDHPSEGCFCPQHQVL-LEGSCVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2261-2322 1.58e-04

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 41.64  E-value: 1.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449083357  2261 DGVRHQFLETWVPDhqPCQICMCLSGrKINCTAQPCPTAraptcgPCEVARLKQSADLCCPE 2322
Cdd:pfam00093    4 NGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1497-1588 2.46e-04

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 44.59  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1497 LDVVFVLEASDEVGEANFNKSKEFLEEVIQRM---DVSPagtHIAVLQYS----YTVNVeYTFKEAQsKEDVLRHVREIR 1569
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKIssyEVSP---RYEIISYAsdpkEIVSI-RDFNSND-ADDVIKRLEDFN 75

                          90       100
                  ....*....|....*....|..
gi 449083357 1570 YQG-GNR--TNTGQALQYLSEH 1588
Cdd:cd01470    76 YDDhGDKtgTNTAAALKKVYER 97
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1276-1428 7.19e-04

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: 43.14  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEA-EFEVLKAFVVGTMERLHISQKRIRVAVVEYHDGSHAYLELRA--RKRPSELRRIASQIKYVGS 1352
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1353 QLAST------SEVLKYtLFQifGKIDRPEASRVILLLT--ASQEPQRMaryfTRYLQGFKKKKVILIPVGIGPHANLKQ 1424
Cdd:cd01471    81 PNGSTnttsalLVVEKH-LFD--TRGNRENAPQLVIIMTdgIPDSKFRT----LKEARKLRERGVIIAVLGVGQGVNHEE 153


                  ....
gi 449083357 1425 IRLI 1428
Cdd:cd01471   154 NRSL 157
VWC smart00214
von Willebrand factor (vWF) type C domain;
2581-2643 7.68e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 39.81  E-value: 7.68e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449083357   2581 CLLNGTIIGPGKSVMVDLCTTCRCIVQRgaifrfKLECRKTTCE---ACPVGYReEKSQSECCGRC 2643
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT------TVLCDPVECPpppDCPNPER-VKPPGECCPRC 59
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1459-1644 9.37e-04

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: 43.77  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1459 DLAPEAPAPTKPPQVAHITVSPGISGVSSPGPKRKSLVLDVVFVLEASDEVGEAN-FNKSKEFLEEVIQRMdvsPAGTHI 1537
Cdd:COG1240    55 GLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1538 AVLQYSYTVNVEYTFkeAQSKEDVLRHVREIRYQGGnrTNTGQALQYLSEHsfspSQGDREQAPNLVYMVT-GNP----- 1611
Cdd:COG1240   132 GLVAFGGEAEVLLPL--TRDREALKRALDELPPGGG--TPLGDALALALEL----LKRADPARRKVIVLLTdGRDnagri 203

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 449083357 1612 ----ASDEIRRLpgDIQVVPIGVGSRA-NLQELERISR 1644
Cdd:COG1240   204 dpleAAELAAAA--GIRIYTIGVGTEAvDEGLLREIAE 239
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 2.89e-03

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: 38.14  E-value: 2.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 449083357  2203 CPPSLIYNHCERGCPRYCD--GNTSFCGDHPSEGCFCPQHQVLL-EGSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1276-1384 3.73e-03

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 40.83  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1276 LDLVFLLDGSYRLSEAEFEVLKAFVVGTMERLHISQKR------IRVAVVEY-HDGSHAYLELRARKRPSELRRIASQIK 1348
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 449083357 1349 YVGSQlASTSEVLKYTLFQIfgKIDRPEASRVILLL 1384
Cdd:cd01480    83 YIGGG-TFTDCALKYATEQL--LEGSHQKENKFLLV 115
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 4.11e-03

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: 37.68  E-value: 4.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 449083357  788 CAKTCQNYDL--ECmSLGCVSGCLCPPGMVRHEN-RCVALERC 827
Cdd:cd19941    14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1579-1840 5.56e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 41.20  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1579 GQALQYLSEHSFSPSQGDREQAPNLVYMVTGNPASDEIRRLPGDIQVVPIGVGSRANLQELERISRPIAPIFIQDFETLP 1658
Cdd:COG2425    14 LLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDALLLAVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1659 REAPDLVLRTCCSKEGLQLPTLpplpdcSQPLDVVLLLDGSSSLPASSFDEMKSFAKAFISKANigPHLtQVSVIQYGSI 1738
Cdd:COG2425    94 LLALLLLAALLLLAAPASAAVP------LLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449083357 1739 NTIDVPWNVAQEkayLQSLVDLMQQ---EGGpSQIGNALAFAVRYVTsqihgaRPGASKAVVMIIMD-----TSLDSVDT 1810
Cdd:COG2425   165 VVEDLPLTADDG---LEDAIEFLSGlfaGGG-TDIAPALRAALELLE------EPDYRNADIVLITDgeagvSPEELLRE 234

                         250       260       270
                  ....*....|....*....|....*....|
gi 449083357 1811 AvdAARSNRVAVFPIGVGDRYDEAQLRILA 1840
Cdd:COG2425   235 V--RAKESGVRLFTVAIGDAGNPGLLEALA 262
 
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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