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Conserved domains on  [gi|823432200|ref|XP_012422640|]
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PREDICTED: von Willebrand factor isoform X2 [Odobenus rosmarus divergens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 2.00e-47

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


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 167.96  E-value: 2.00e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    377 WICSNEECPGECLVTGQSHFKSFDNRHFTFSGVCRYLLAQDCQDH-TFSVVIDTVQCadDPDAVCTRSVTVRLPrlDNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVELN--GDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    456 VKLKHGGGVSMDGQDVQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVMLSPVYAGKTCGLCGNFNGNRG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 823432200    533 DDFVTPAG 540
Cdd:smart00216  156 DDFRTPDG 163
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 1.58e-40

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: 145.12  E-value: 1.58e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 823432200  1198 VCEVAGRRLAPGKKITLNPDDPEHCQICHCEGVNLTCEACREPGGLVVAPTEGPIASTTPYVEDTPEPPLHDFYCSKLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 2.38e-40

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: 147.55  E-value: 2.38e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    856 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCDSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    936 LFDGEV-------NVKKPMKDETHFEVVES-GQYIILLLGKAL-SVVWDHRLSIFVSLKQTYQERVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 823432200   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 3.14e-39

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.73  E-value: 3.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhADVQELQSISWPNAP- 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEg 157

                          170
                   ....*....|..
gi 823432200  1649 --ILIQDFETLP 1658
Cdd:pfam00092  158 hvFTVSDFEALE 169
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 7.45e-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: 131.72  E-value: 7.45e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    35 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQKH---SFSLIGGFQNGK-----RVSLSVYLGEFfSIHLFVNGTALQGT 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDL-EITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200   107 QNISMPYASNGLYLETEAGYYKLSSEAYGFVARIDGSGNFQ--VLLSDRYFNKTCGLCGDYNIFAEDDFRTQEGT 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 9.86e-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: 131.34  E-value: 9.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1950 CMGSSTRHIVTFDGQNFNLTGSCSYVLFQNKEQ--DLEVILHNGACSPGVRQACMKSIEVKHDGFSVELHSDMQVRVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2028 LVPVPYVGGDMEVNVYGTIMYEIRLnHLGHIFTFTPRNNEFQLQLSPKTFASKTYGLCGICDENGANDFVLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA pfam00092
von Willebrand factor type A domain;
1691-1860 9.97e-34

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 128.93  E-value: 9.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVD-LMQREGGLSH 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1770 IGDALDYAVRYVTSEVHGARPGASKaVVILVT--DVSADSVDAAADAATSNRVTVFPIGIGDRyDEAQLRRLAGPNAGSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTdgRSQDGDPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 823432200  1848 VLRLQRIEDLSTM 1860
Cdd:pfam00092  159 VFTVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 2.83e-26

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: 107.93  E-value: 2.83e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1357 TSEVLKYTLFQIFGKID--RPEASRIaLILMASQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHANLKQIRNIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 823432200   1435 NKAFVLSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 1.60e-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: 87.78  E-value: 1.60e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200   1053 QTMVDSFCRILTSD--IFQDCNRLVDPEPYLDICIYDSCSCEspGDCTCFCDTVAAYAHVCARHGKAV-AWRTATLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 5.31e-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: 86.24  E-value: 5.31e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200    579 FAEEACALLTSSK--FEACHQAVSPLPYVQNCRYDVCSCSDGRDCLCSAVANYAAACSRRGVHI-GWREPSFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-292 5.05e-17

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: 77.77  E-value: 5.05e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823432200    222 WEQCRLLKSAS-VFARCHPLVDPEPFVALCERALCTCAWGLGCPCEVLLEYSRACAQQGMVLYHWTDHSTCR 292
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 7.74e-16

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: 74.75  E-value: 7.74e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   2727 ITARLRYVKVGDCKSEEeVDIHYCEGKCASKALYSIdtEDVQDQCFCCSPTHTEPMRVPLRCTNGSLVYHEILNAMQCRC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 823432200   2807 SP 2808
Cdd:smart00041   78 EP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 4.76e-13

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 65.80  E-value: 4.76e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200  652 CPQGQVYLQCGTPCNMTCRSLSYPDEgCDEVCLEGCFCPPGLYLDERGDCVPKTQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP-CTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 1.28e-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: 64.65  E-value: 1.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  295 CPAGMEYKECVSPCTRTCQSLHVQEVCQEQCVDGCSCPEGQLLDE-GRCVGSAEC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 2.24e-11

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


:

Pssm-ID: 462584  Cd Length: 68  Bit Score: 61.63  E-value: 2.24e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200  2138 HCQVLL-SELFAECHKVLTPTTFYAMCQQDSCH----QEQVCEVIALYAHLCRTKGVCV-DWRRTNFC 2199
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 3.40e-08

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.93  E-value: 3.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 823432200 1146 YNSCAPACPTTCQHPE-PLACPVPCVEGChaHCPPGKILDElLQTCISPEDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 2.60e-07

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 49.82  E-value: 2.60e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   2431 CVHRGTIYPVGQFWEEG-CDVCTCTDLEdsvmglrVAQCSQKPCEDN--CRSGFTyVIQEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 7.22e-06

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.58  E-value: 7.22e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823432200   2261 DGVRHQFLETWVPAhqPCQICMCLSGRKVNCTSQPCPTARaptcgPCEVARLRQNAEQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 2.21e-05

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 44.04  E-value: 2.21e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200   2582 CMLNGTIIGPGKSLMIDVCTTCRCTIQVgVISGFKLECRKTTckACPLGYKeEKNQGECCGKC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 2.28e-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: 41.15  E-value: 2.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200 2203 CPPSLVYNHCERGCPRLCE--GNTSSCGDHPSEGCFCPPNQVMLESS-CVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 350-394 2.62e-03

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


The actual alignment was detected with superfamily member smart00215:

Pssm-ID: 450195  Cd Length: 67  Bit Score: 38.70  E-value: 2.62e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 823432200    350 CVHAGERYPPGSSLLQDCNTCICRNSLWICSNEEC-PGECLVTGQS 394
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 4.12e-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: 4.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 823432200  788 CAKTCQNYDLQ--CmSTGCVSGCLCPPGMVRHEN-KCVALERC 827
Cdd:cd19941    14 CPPTCANPNAPppC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 2.00e-47

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 167.96  E-value: 2.00e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    377 WICSNEECPGECLVTGQSHFKSFDNRHFTFSGVCRYLLAQDCQDH-TFSVVIDTVQCadDPDAVCTRSVTVRLPrlDNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVELN--GDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    456 VKLKHGGGVSMDGQDVQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVMLSPVYAGKTCGLCGNFNGNRG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 823432200    533 DDFVTPAG 540
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.55e-45

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: 162.15  E-value: 1.55e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   388 CLVTGQSHFKSFDNRHFTFSGVCRYLLAQDCQDHT-FSVVIDTVQCADDPDAVCTRSVTVRLPrldNSLVKLKHGGGVSM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSVTVIVG---DLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   467 DGQDVQIPLLQGDLRIQHTV--MASVRLSYGEDLQMDWDGRGRLLVMLSPVYAGKTCGLCGNFNGNRGDDFVTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 1.58e-40

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: 145.12  E-value: 1.58e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 823432200  1198 VCEVAGRRLAPGKKITLNPDDPEHCQICHCEGVNLTCEACREPGGLVVAPTEGPIASTTPYVEDTPEPPLHDFYCSKLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 2.38e-40

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: 147.55  E-value: 2.38e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    856 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCDSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    936 LFDGEV-------NVKKPMKDETHFEVVES-GQYIILLLGKAL-SVVWDHRLSIFVSLKQTYQERVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 823432200   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 3.14e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.73  E-value: 3.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhADVQELQSISWPNAP- 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEg 157

                          170
                   ....*....|..
gi 823432200  1649 --ILIQDFETLP 1658
Cdd:pfam00092  158 hvFTVSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1645 4.28e-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: 141.27  E-value: 4.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRT 1576
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200 1577 NTGLALQYLSEHSFSVSQgDREQVPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhADVQELQSISWP 1645
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 1.55e-36

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: 136.35  E-value: 1.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   867 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCDSNPG-TFRILVGNEGCSYPSVkCKKRVTILVEGGEIELFDG---EVN 942
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200   943 VKK---PMK-DETHFEVVESGQYIILL-LGKALSVVWDHRLSIFVSLKQTYQERVCGLCGNFDGIQNNDFTSSS 1011
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFVVVDLsPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 7.45e-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: 131.72  E-value: 7.45e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    35 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQKH---SFSLIGGFQNGK-----RVSLSVYLGEFfSIHLFVNGTALQGT 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDL-EITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200   107 QNISMPYASNGLYLETEAGYYKLSSEAYGFVARIDGSGNFQ--VLLSDRYFNKTCGLCGDYNIFAEDDFRTQEGT 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 9.86e-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: 131.34  E-value: 9.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1950 CMGSSTRHIVTFDGQNFNLTGSCSYVLFQNKEQ--DLEVILHNGACSPGVRQACMKSIEVKHDGFSVELHSDMQVRVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2028 LVPVPYVGGDMEVNVYGTIMYEIRLnHLGHIFTFTPRNNEFQLQLSPKTFASKTYGLCGICDENGANDFVLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1643 4.03e-34

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: 130.27  E-value: 4.03e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200   1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHADVQELQSIS 1643
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLA 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 5.23e-34

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: 129.44  E-value: 5.23e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1938 ETCGCrWTCPCVCMGSSTRHIVTFDGQNFNLTGSCSYVLFQN--KEQDLEVILHNGACSPGVrqACMKSIEVKHDGFSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   2016 LHSD-MQVRVNGRLVPVPYVGGDMEVNVYGTIMYEIRLNHLGHI-FTFTPRNNeFQLQLSPKtFASKTYGLCGICDENGA 2093
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 823432200   2094 NDFVLRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWA pfam00092
von Willebrand factor type A domain;
1691-1860 9.97e-34

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 128.93  E-value: 9.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVD-LMQREGGLSH 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1770 IGDALDYAVRYVTSEVHGARPGASKaVVILVT--DVSADSVDAAADAATSNRVTVFPIGIGDRyDEAQLRRLAGPNAGSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTdgRSQDGDPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 823432200  1848 VLRLQRIEDLSTM 1860
Cdd:pfam00092  159 VFTVSDFEALEDL 171
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 22-178 4.19e-29

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: 115.58  E-value: 4.19e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200     22 CTKGTVGrssmARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQ-KHSFSLIG-----GFQNGKRVSLSVYLGEFfSIH 95
Cdd:smart00216    3 CTQEECS----PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSsEPTFSVLLknvpcGGGATCLKSVKVELNGD-EIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200     96 LF-VNGTALQGTQNISMPYASNGLYLETE-AGYYKLSSEAYG-FVARIDGSGNFQVLLSDRYFNKTCGLCGDYNIFAEDD 172
Cdd:smart00216   78 LKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 823432200    173 FRTQEG 178
Cdd:smart00216  158 FRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1859 1.09e-28

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: 114.86  E-value: 1.09e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVD-LMQREGGLSH 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALAsLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1770 IGDALDYAVRYVTSEVHGARPGASKaVVILVT----DVSADSVDAAADAATSNRVTVFPIGIGDRYDEAQLRRLAGPNAG 1845
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITdgesNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....
gi 823432200   1846 SNVLRLQRIEDLST 1859
Cdd:smart00327  160 VYVFLPELLDLLID 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 2.83e-26

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: 107.93  E-value: 2.83e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1357 TSEVLKYTLFQIFGKID--RPEASRIaLILMASQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHANLKQIRNIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 823432200   1435 NKAFVLSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 1.48e-25

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: 105.07  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1690 LDVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQ-REGGLS 1768
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKyLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1769 HIGDALDYAVRYVTSEvHGARPGASKaVVILVT---DVSADSVDAAADAATSNRVTVFPIGIGDrYDEAQLRRLAGPNAG 1845
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTdgrSDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 823432200 1846 SNVL 1849
Cdd:cd01450   158 RHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 2.13e-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: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVA 1355
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1356 STSEVLKYTLFQIFGKI-DRPEASRIALILMASQepPRLARNLVRYVQGLKKKKVIVIPVGIGPhANLKQIRNIEKQAPE 1434
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 823432200 1435 NKAF 1438
Cdd:cd01450   158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 1.60e-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: 87.78  E-value: 1.60e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200   1053 QTMVDSFCRILTSD--IFQDCNRLVDPEPYLDICIYDSCSCEspGDCTCFCDTVAAYAHVCARHGKAV-AWRTATLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 5.31e-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: 86.24  E-value: 5.31e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200    579 FAEEACALLTSSK--FEACHQAVSPLPYVQNCRYDVCSCSDGRDCLCSAVANYAAACSRRGVHI-GWREPSFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 1.37e-18

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: 82.04  E-value: 1.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   584 CALLTSSK-FEACHQAVSPLPYVQNCRYDVCSCSDGRDCLCSAVANYAAACSRRGVHIG-WREPSFC 648
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-292 5.05e-17

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: 77.77  E-value: 5.05e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823432200    222 WEQCRLLKSAS-VFARCHPLVDPEPFVALCERALCTCAWGLGCPCEVLLEYSRACAQQGMVLYHWTDHSTCR 292
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1059-1126 6.12e-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: 77.42  E-value: 6.12e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1059 FCRILT-SDIFQDCNRLVDPEPYLDICIYDSCSCEspGDCTCFCDTVAAYAHVCARHGKAVA-WRTATLC 1126
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1277-1448 1.19e-16

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 80.01  E-value: 1.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYhdGSHAYIE--LKDRKRPSELRRIASQVKYVGSEV 1354
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1355 ASTSEVLKYTLFQIFGKI--DRPEASRIALIL----MASQEPPRLARNlvryvqgLKKKKVIVIPVGIGPHANlKQIRNI 1428
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKI 150

                          170       180
                   ....*....|....*....|
gi 823432200  1429 EKQAPENKAFVLSGVDELEQ 1448
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 7.74e-16

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: 74.75  E-value: 7.74e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   2727 ITARLRYVKVGDCKSEEeVDIHYCEGKCASKALYSIdtEDVQDQCFCCSPTHTEPMRVPLRCTNGSLVYHEILNAMQCRC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 823432200   2807 SP 2808
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 2.88e-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: 72.41  E-value: 2.88e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200   224 QCRLLKSASVFARCHPLVDPEPFVALCERALCTCAWGLGCPCEVLLEYSRACAQQGMVLYHWTDHSTC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 4.76e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 65.80  E-value: 4.76e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200  652 CPQGQVYLQCGTPCNMTCRSLSYPDEgCDEVCLEGCFCPPGLYLDERGDCVPKTQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP-CTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 1.28e-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: 64.65  E-value: 1.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  295 CPAGMEYKECVSPCTRTCQSLHVQEVCQEQCVDGCSCPEGQLLDE-GRCVGSAEC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 2.41e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.95  E-value: 2.41e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200   295 CPAGMEYKECVSPCTRTCQSLHVQEVCQEQCVDGCSCPEGQLLD-EGRCVGSAEC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 4.00e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.18  E-value: 4.00e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200   652 CPQGQVYLQCGTPCNMTCRSLSYPDEgCDEVCLEGCFCPPGLYLDERGDCVPKTQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 2.24e-11

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 61.63  E-value: 2.24e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200  2138 HCQVLL-SELFAECHKVLTPTTFYAMCQQDSCH----QEQVCEVIALYAHLCRTKGVCV-DWRRTNFC 2199
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2134-2199 3.40e-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: 3.40e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200   2134 SSNSHCQVLLSEL--FAECHKVLTPTTFYAMCQQDSC----HQEQVCEVIALYAHLCRTKGVCV-DWRRTNFC 2199
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFC 75
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 3.40e-08

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.93  E-value: 3.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 823432200 1146 YNSCAPACPTTCQHPE-PLACPVPCVEGChaHCPPGKILDElLQTCISPEDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 2.60e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 49.82  E-value: 2.60e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   2431 CVHRGTIYPVGQFWEEG-CDVCTCTDLEdsvmglrVAQCSQKPCEDN--CRSGFTyVIQEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 6.69e-07

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: 48.54  E-value: 6.69e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 823432200  1146 YNSCAPACPTTCQHPE-PLACPVPCVEGChaHCPPGKILDElLQTCISPEDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 9.31e-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: 9.31e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200  2431 CVHRGTIYPVGQFWEEG-CDVCTCTDledsvmglRVAQCSQKPCEDN-CRSGFtYVIQEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLdCPNPR-LEIPPGECCPVC 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1645-1862 1.98e-06

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: 51.86  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1645 PNAPILIQDFETLPREAPDLVLQRCCSGEGPQSPTLAPTPDcSQPLDVALLLDGSSS-FPNSYFEEMKSFAKAFISRanL 1723
Cdd:COG1240    49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARP-QRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDD--Y 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1724 GPRlTQVSVLQYGSSTITAVPwnVAYEKAHLLSHVDLMQREGGlSHIGDALDYAVRYVTSEVHGARPgaskaVVILVT-- 1801
Cdd:COG1240   126 RPR-DRVGLVAFGGEAEVLLP--LTRDREALKRALDELPPGGG-TPLGDALALALELLKRADPARRK-----VIVLLTdg 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200 1802 --DVSADSVDAAADAATSNRVTVFPIGIG-DRYDEAQLRRLAGpNAGSNVLRLQRIEDLSTMAT 1862
Cdd:COG1240   197 rdNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE-ATGGRYFRADDLSELAAIYR 259
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 7.22e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.58  E-value: 7.22e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823432200   2261 DGVRHQFLETWVPAhqPCQICMCLSGRKVNCTSQPCPTARaptcgPCEVARLRQNAEQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2260-2322 1.47e-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: 44.72  E-value: 1.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200  2260 EDGVRHQFLETWVPAhqPCQICMCLSGrKVNCTSQPCPTAraptcgPCEVARLRQNAEQCCPE 2322
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 2.21e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 44.04  E-value: 2.21e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200   2582 CMLNGTIIGPGKSLMIDVCTTCRCTIQVgVISGFKLECRKTTckACPLGYKeEKNQGECCGKC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 4.67e-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: 43.18  E-value: 4.67e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2582 CMLNGTIIGPGKSLMIDVCTTCRCTiqvgvisGFKLECRKTTCKA--CPLGYkEEKNQGECCGKC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 2.28e-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: 41.15  E-value: 2.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200 2203 CPPSLVYNHCERGCPRLCE--GNTSSCGDHPSEGCFCPPNQVMLESS-CVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 7.21e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 39.68  E-value: 7.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2203 CPPSLVYNHCERGCPRLCE--GNTSSCGDHPSEGCFCPPNQVML-ESSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
350-394 2.62e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 38.70  E-value: 2.62e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 823432200    350 CVHAGERYPPGSSLLQDCNTCICRNSLWICSNEEC-PGECLVTGQS 394
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 4.12e-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: 4.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 823432200  788 CAKTCQNYDLQ--CmSTGCVSGCLCPPGMVRHEN-KCVALERC 827
Cdd:cd19941    14 CPPTCANPNAPppC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 2.00e-47

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 167.96  E-value: 2.00e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    377 WICSNEECPGECLVTGQSHFKSFDNRHFTFSGVCRYLLAQDCQDH-TFSVVIDTVQCadDPDAVCTRSVTVRLPrlDNSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVELN--GDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    456 VKLKHGGGVSMDGQDVQIPLLQGDLRIQHTV---MASVRLSYGeDLQMDWDGRGRLLVMLSPVYAGKTCGLCGNFNGNRG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 823432200    533 DDFVTPAG 540
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.55e-45

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: 162.15  E-value: 1.55e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   388 CLVTGQSHFKSFDNRHFTFSGVCRYLLAQDCQDHT-FSVVIDTVQCADDPDAVCTRSVTVRLPrldNSLVKLKHGGGVSM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSVTVIVG---DLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   467 DGQDVQIPLLQGDLRIQHTV--MASVRLSYGEDLQMDWDGRGRLLVMLSPVYAGKTCGLCGNFNGNRGDDFVTPAGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 1.58e-40

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: 145.12  E-value: 1.58e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 823432200  1198 VCEVAGRRLAPGKKITLNPDDPEHCQICHCEGVNLTCEACREPGGLVVAPTEGPIASTTPYVEDTPEPPLHDFYCSKLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 2.38e-40

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: 147.55  E-value: 2.38e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    856 WNCTDHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCDSNPgTFRILVGNEGCSyPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    936 LFDGEV-------NVKKPMKDETHFEVVES-GQYIILLLGKAL-SVVWDHRLSIFVSLKQTYQERVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 823432200   1007 FTSSS 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 3.14e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 144.73  E-value: 3.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhADVQELQSISWPNAP- 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEg 157

                          170
                   ....*....|..
gi 823432200  1649 --ILIQDFETLP 1658
Cdd:pfam00092  158 hvFTVSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1645 4.28e-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: 141.27  E-value: 4.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRT 1576
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200 1577 NTGLALQYLSEHSFSVSQgDREQVPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhADVQELQSISWP 1645
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1498-1643 1.17e-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: 136.97  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNrTN 1577
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823432200 1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIKRMPG-----DIQVVPIGVGPhADVQELQSIS 1643
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVelkqaGIEVFAVGVKN-ADEEELKQIA 150
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 1.55e-36

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: 136.35  E-value: 1.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   867 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCDSNPG-TFRILVGNEGCSYPSVkCKKRVTILVEGGEIELFDG---EVN 942
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200   943 VKK---PMK-DETHFEVVESGQYIILL-LGKALSVVWDHRLSIFVSLKQTYQERVCGLCGNFDGIQNNDFTSSS 1011
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFVVVDLsPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1498-1654 1.68e-36

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: 136.68  E-value: 1.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRTN 1577
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1578 TGLALQYLSEHSFSVSQGDR--EQVPNLVYMVTGNPASDEIKRMPGDIQ---VVPIGVGP-HADVQELQSISW-PNAPIL 1650
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQIAFdPSFVFQ 161


                  ....
gi 823432200 1651 IQDF 1654
Cdd:cd01481   162 VSDF 165
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 7.45e-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: 131.72  E-value: 7.45e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200    35 CSLFGGDFINTFDESMYSFAGDCSYLLAGDCQKH---SFSLIGGFQNGK-----RVSLSVYLGEFfSIHLFVNGTALQGT 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGasgvcLKSVTVIVGDL-EITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200   107 QNISMPYASNGLYLETEAGYYKLSSEAYGFVARIDGSGNFQ--VLLSDRYFNKTCGLCGDYNIFAEDDFRTQEGT 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 9.86e-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: 131.34  E-value: 9.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1950 CMGSSTRHIVTFDGQNFNLTGSCSYVLFQNKEQ--DLEVILHNGACSPGVRQACMKSIEVKHDGFSVELHSDMQVRVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2028 LVPVPYVGGDMEVNVYGTIMYEIRLnHLGHIFTFTPRNNEFQLQLSPKTFASKTYGLCGICDENGANDFVLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1643 4.03e-34

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: 130.27  E-value: 4.03e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200   1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHADVQELQSIS 1643
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLA 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 5.23e-34

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: 129.44  E-value: 5.23e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1938 ETCGCrWTCPCVCMGSSTRHIVTFDGQNFNLTGSCSYVLFQN--KEQDLEVILHNGACSPGVrqACMKSIEVKHDGFSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   2016 LHSD-MQVRVNGRLVPVPYVGGDMEVNVYGTIMYEIRLNHLGHI-FTFTPRNNeFQLQLSPKtFASKTYGLCGICDENGA 2093
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 823432200   2094 NDFVLRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWA pfam00092
von Willebrand factor type A domain;
1691-1860 9.97e-34

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 128.93  E-value: 9.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVD-LMQREGGLSH 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1770 IGDALDYAVRYVTSEVHGARPGASKaVVILVT--DVSADSVDAAADAATSNRVTVFPIGIGDRyDEAQLRRLAGPNAGSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTdgRSQDGDPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 823432200  1848 VLRLQRIEDLSTM 1860
Cdd:pfam00092  159 VFTVSDFEALEDL 171
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1498-1642 5.05e-30

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: 118.16  E-value: 5.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1498 DVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNrTN 1577
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823432200 1578 TGLALQYLSEHSFSVSQGDREQVPNLVYMVTGNPASDEIkRMPGD------IQVVPIGVGpHADVQELQSI 1642
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGVK-DADESELKMI 149
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 22-178 4.19e-29

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: 115.58  E-value: 4.19e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200     22 CTKGTVGrssmARCSLFGGDFINTFDESMYSFAGDCSYLLAGDCQ-KHSFSLIG-----GFQNGKRVSLSVYLGEFfSIH 95
Cdd:smart00216    3 CTQEECS----PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSsEPTFSVLLknvpcGGGATCLKSVKVELNGD-EIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200     96 LF-VNGTALQGTQNISMPYASNGLYLETE-AGYYKLSSEAYG-FVARIDGSGNFQVLLSDRYFNKTCGLCGDYNIFAEDD 172
Cdd:smart00216   78 LKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 823432200    173 FRTQEG 178
Cdd:smart00216  158 FRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1859 1.09e-28

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: 114.86  E-value: 1.09e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVD-LMQREGGLSH 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALAsLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1770 IGDALDYAVRYVTSEVHGARPGASKaVVILVT----DVSADSVDAAADAATSNRVTVFPIGIGDRYDEAQLRRLAGPNAG 1845
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITdgesNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....
gi 823432200   1846 SNVLRLQRIEDLST 1859
Cdd:smart00327  160 VYVFLPELLDLLID 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 2.83e-26

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: 107.93  E-value: 2.83e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   1357 TSEVLKYTLFQIFGKID--RPEASRIaLILMASQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHANLKQIRNIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 823432200   1435 NKAFVLSGVDELEQR 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1497-1657 8.58e-26

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: 108.24  E-value: 8.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRY--RGgn 1574
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1575 rTNTGLALQYLSEHSFSVSQGDR---EQVPNLVYMVTGNPASDEIK------RMPGdIQVVPIGVGpHADVQELQSI-SW 1644
Cdd:cd01475    81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIaSE 157

                         170
                  ....*....|....*
gi 823432200 1645 PNAP--ILIQDFETL 1657
Cdd:cd01475   158 PLADhvFYVEDFSTI 172
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 1.48e-25

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: 105.07  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1690 LDVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQ-REGGLS 1768
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKyLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1769 HIGDALDYAVRYVTSEvHGARPGASKaVVILVT---DVSADSVDAAADAATSNRVTVFPIGIGDrYDEAQLRRLAGPNAG 1845
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTdgrSDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 823432200 1846 SNVL 1849
Cdd:cd01450   158 RHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 2.13e-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: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVA 1355
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1356 STSEVLKYTLFQIFGKI-DRPEASRIALILMASQepPRLARNLVRYVQGLKKKKVIVIPVGIGPhANLKQIRNIEKQAPE 1434
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 823432200 1435 NKAF 1438
Cdd:cd01450   158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 1.60e-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: 87.78  E-value: 1.60e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200   1053 QTMVDSFCRILTSD--IFQDCNRLVDPEPYLDICIYDSCSCEspGDCTCFCDTVAAYAHVCARHGKAV-AWRTATLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-649 5.31e-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: 86.24  E-value: 5.31e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200    579 FAEEACALLTSSK--FEACHQAVSPLPYVQNCRYDVCSCSDGRDCLCSAVANYAAACSRRGVHI-GWREPSFCA 649
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1648 1.52e-19

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 88.01  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGNRT 1576
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1577 NTGLALQYLSEHsfsVSQGDREQVPNLVYMVT-GNP---------ASDEIKRMpgDIQVVPIGVGPHADVQELQSISWPN 1646
Cdd:cd00198    81 NIGAALRLALEL---LKSAKRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEIADKT 155


                  ..
gi 823432200 1647 AP 1648
Cdd:cd00198   156 TG 157
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1848 2.55e-19

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 87.24  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1690 LDVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQRE-GGLS 1768
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1769 HIGDALDYAVRYVTSEVHGARpgasKAVVILVT----DVSADSVDAAADAATSNRVTVFPIGIGDRYDEAQLRRLAGPNA 1844
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA----RRVIILLTdgepNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTT 156


                  ....
gi 823432200 1845 GSNV 1848
Cdd:cd00198   157 GGAV 160
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1497-1643 1.25e-18

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: 85.87  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFSEAQSKGEVLQHVREIRYRGGnRT 1576
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200 1577 NTGLALQYLSEHSFSVSQGDREQVPNLVYMVT-----GNPASDEIKRMP--GDIQVVPIGVGPHAD----VQELQSIS 1643
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITdgeshDDPLLKDVIPQAerEGIIRYAIGVGGHFQrensREELKTIA 157
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 1.37e-18

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: 82.04  E-value: 1.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   584 CALLTSSK-FEACHQAVSPLPYVQNCRYDVCSCSDGRDCLCSAVANYAAACSRRGVHIG-WREPSFC 648
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-292 5.05e-17

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: 77.77  E-value: 5.05e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823432200    222 WEQCRLLKSAS-VFARCHPLVDPEPFVALCERALCTCAWGLGCPCEVLLEYSRACAQQGMVLYHWTDHSTCR 292
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1059-1126 6.12e-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: 77.42  E-value: 6.12e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1059 FCRILT-SDIFQDCNRLVDPEPYLDICIYDSCSCEspGDCTCFCDTVAAYAHVCARHGKAVA-WRTATLC 1126
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1277-1448 1.19e-16

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 80.01  E-value: 1.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYhdGSHAYIE--LKDRKRPSELRRIASQVKYVGSEV 1354
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1355 ASTSEVLKYTLFQIFGKI--DRPEASRIALIL----MASQEPPRLARNlvryvqgLKKKKVIVIPVGIGPHANlKQIRNI 1428
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKI 150

                          170       180
                   ....*....|....*....|
gi 823432200  1429 EKQAPENKAFVLSGVDELEQ 1448
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1497-1643 3.42e-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: 78.59  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEAnFNKSREFMEEVIQRMDVGQDSIHVMVLQYS--YTVAVEYTFSEAQSKGEVLQHVREIRYRGGN 1574
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200 1575 rTNTGLALQYLSEHsFSVSQGDREQVPNLVYMVTGNPASDEIKRM-------PGdIQVVPIGVGPHADV--QELQSIS 1643
Cdd:cd01476    80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQarilravPN-IETFAVGTGDPGTVdtEELHSIT 154
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1690-1838 4.21e-16

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: 78.55  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1690 LDVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQREGGLSH 1769
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823432200 1770 IGDALDYAVRYVTSEVHGARPGASKAVVILVTDVSADSVDAAADAATSNR--VTVFPIGIGDRYDEAQLRR 1838
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAERegIIRYAIGVGGHFQRENSRE 151
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1497-1642 5.60e-16

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: 78.58  E-value: 5.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEAN-FNKSREFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFS-----EAQSKGEVLQHVREIRY 1570
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSspnstNKDLALNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1571 RGGNrTNTGLALQYLSEHSFSvSQGDREQVPNLVYMVT-GNPASD--------EIKRMPGDIQVvpIGVGPHADVQELQS 1641
Cdd:cd01471    81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEENRS 156


                  .
gi 823432200 1642 I 1642
Cdd:cd01471   157 L 157
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 5.64e-16

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 77.61  E-value: 5.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVA 1355
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1356 STSEVLKYTLfQIFGKIDRPEASRIaLILMASQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHANLKQIRNIEKQAPEN 1435
Cdd:cd00198    81 NIGAALRLAL-ELLKSAKRPNARRV-IILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGG 158


                  ...
gi 823432200 1436 KAF 1438
Cdd:cd00198   159 AVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1691-1840 6.65e-16

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: 77.65  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQREGGLSHI 1770
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1771 GDALDYAVRYVTSEVHGARPGASKAVVILVTDVSADSVDAAADAATSNRVTVFPIGIGDRyDEAQLRRLA 1840
Cdd:cd01472    82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNA-DEEELKQIA 150
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 7.74e-16

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: 74.75  E-value: 7.74e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200   2727 ITARLRYVKVGDCKSEEeVDIHYCEGKCASKALYSIdtEDVQDQCFCCSPTHTEPMRVPLRCTNGSLVYHEILNAMQCRC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 823432200   2807 SP 2808
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 2.88e-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: 72.41  E-value: 2.88e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200   224 QCRLLKSASVFARCHPLVDPEPFVALCERALCTCAWGLGCPCEVLLEYSRACAQQGMVLYHWTDHSTC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1689-1874 5.78e-15

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: 76.65  E-value: 5.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1689 PLDVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQREGGLS 1768
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1769 HIGDALDYAVRYVTSEVHGARPGASKA--VVILVTDVSADSVDAAADAATSNR-VTVFPIGIGdRYDEAQLRRLAGPNAG 1845
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVprVGIVVTDGRPQDDVSEVAAKARALgIEMFAVGVG-RADEEELREIASEPLA 160

                         170       180
                  ....*....|....*....|....*....
gi 823432200 1846 SNVLrlqRIEDLSTMATLGNSFFHKLCSG 1874
Cdd:cd01475   161 DHVF---YVEDFSTIEELTKKFQGKICVV 186
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1691-1842 7.82e-15

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: 74.63  E-value: 7.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQREGGLSHI 1770
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823432200 1771 GDALDYAVRYVTSEVHGARPGASKAVVILVTDVSADSVDAAADAATSNRVTVFPIGIGDrYDEAQLRRLAGP 1842
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKD-ADESELKMIASK 152
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 4.76e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 65.80  E-value: 4.76e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200  652 CPQGQVYLQCGTPCNMTCRSLSYPDEgCDEVCLEGCFCPPGLYLDERGDCVPKTQC 707
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP-CTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 1.28e-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: 64.65  E-value: 1.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  295 CPAGMEYKECVSPCTRTCQSLHVQEVCQEQCVDGCSCPEGQLLDE-GRCVGSAEC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 2.41e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.95  E-value: 2.41e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200   295 CPAGMEYKECVSPCTRTCQSLHVQEVCQEQCVDGCSCPEGQLLD-EGRCVGSAEC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 4.00e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.18  E-value: 4.00e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200   652 CPQGQVYLQCGTPCNMTCRSLSYPDEgCDEVCLEGCFCPPGLYLDERGDCVPKTQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 2.24e-11

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 61.63  E-value: 2.24e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823432200  2138 HCQVLL-SELFAECHKVLTPTTFYAMCQQDSCH----QEQVCEVIALYAHLCRTKGVCV-DWRRTNFC 2199
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2134-2199 3.40e-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: 3.40e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200   2134 SSNSHCQVLLSEL--FAECHKVLTPTTFYAMCQQDSC----HQEQVCEVIALYAHLCRTKGVCV-DWRRTNFC 2199
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFC 75
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1690-1799 3.57e-11

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 63.96  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1690 LDVALLLDGSSSFpNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVA--YEKAHLLSHVDLMQREGGL 1767
Cdd:cd01476     1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPkhNDGEELLEKVDNLRFIGGT 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 823432200 1768 SHIGDALDYAVRYVTsEVHGARPGASKAVVIL 1799
Cdd:cd01476    80 TATGAAIEVALQQLD-PSEGRREGIPKVVVVL 110
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1276-1385 4.04e-10

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: 62.40  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVA 1355
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 823432200 1356 sTSEVLKYTLFQIFGKID--RPEASRIALILM 1385
Cdd:cd01475    83 -TGLAIQYAMNNAFSEAEgaRPGSERVPRVGI 113
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1277-1425 4.74e-10

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 60.70  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVAs 1356
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200 1357 TSEVLKYTLFQIFGKIDRPEAS--RIALILMASQEPPRLARNLVRyvqgLKKKKVIVIPVGIGPH--ANLKQI 1425
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQDDVEEPAVE----LKQAGIEVFAVGVKNAdeEELKQI 149
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1276-1441 2.84e-08

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 55.82  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGsEVA 1355
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLL-GLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1356 STSEVLKYTLFQIF--GKIDRPEASRIALILM--ASQEPPRLARNLvryvQGLKKKKVIVIPVGIGPHAN----LKQIRN 1427
Cdd:cd01469    80 NTATAIQYVVTELFseSNGARKDATKVLVVITdgESHDDPLLKDVI----PQAEREGIIRYAIGVGGHFQrensREELKT 155

                         170
                  ....*....|....
gi 823432200 1428 IEKQAPENKAFVLS 1441
Cdd:cd01469   156 IASKPPEEHFFNVT 169
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 3.40e-08

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.93  E-value: 3.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 823432200 1146 YNSCAPACPTTCQHPE-PLACPVPCVEGChaHCPPGKILDElLQTCISPEDC 1196
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1691-1840 5.62e-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: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1691 DVALLLDGSSSFPNSYFEEMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDLMQREGGLS-H 1769
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQlN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200 1770 IGDALDYAVRYVTSEVHGAR--PGASKAVVILVTDVSADSVDAAADAATSNRvtVFPIGIGDRY-DEAQLRRLA 1840
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAG--IVPFAIGARNaDLAELQQIA 153
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1277-1387 1.07e-07

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 53.87  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEVAS 1356
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 823432200 1357 TSEVLKYTLFQIFgkiDRPEASRIA------LILMAS 1387
Cdd:cd01481    82 TGSALDYVVKNLF---TKSAGSRIEegvpqfLVLITG 115
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1277-1425 1.07e-07

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 53.83  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1277 DLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKDRKRPSELRRIASQVKYVGSEvAS 1356
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200 1357 TSEVLKYTLFQIF--GKIDRPEASRIALILM--ASQEPPRLArnlvryVQGLKKKKVIVIPVGIGPH--ANLKQI 1425
Cdd:cd01482    81 TGKALTHVREKNFtpDAGARPGVPKVVILITdgKSQDDVELP------ARVLRNLGVNVFAVGVKDAdeSELKMI 149
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1497-1587 1.12e-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: 54.31  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRM------DVGQDSIHVMVLQYSYTVAVEYTF-SEAQSKGEVLQHVREIR 1569
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLE 82

                          90
                  ....*....|....*...
gi 823432200 1570 YRGGNrTNTGLALQYLSE 1587
Cdd:cd01480    83 YIGGG-TFTDCALKYATE 99
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1689-1801 2.16e-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: 53.54  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1689 PLDVALLLDGSSSFPNSYFEEMKSFAKAFISR---------ANLGPRltqVSVLQY-GSSTITAVPWNVAYEKAHLLSHV 1758
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyrkdPAGSWR---VGVVQYsDQQEVEAGFLRDIRNYTSLKEAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 823432200 1759 DLMQREGGLSHIGDALdyavRYVTSEVHGARPGASKAVVILVT 1801
Cdd:cd01480    79 DNLEYIGGGTFTDCAL----KYATEQLLEGSHQKENKFLLVIT 117
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 2.60e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 49.82  E-value: 2.60e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823432200   2431 CVHRGTIYPVGQFWEEG-CDVCTCTDLEdsvmglrVAQCSQKPCEDN--CRSGFTyVIQEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
VWA_2 pfam13519
von Willebrand factor type A domain;
1692-1800 5.48e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.98  E-value: 5.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200  1692 VALLLDGSSS-----FPNSYFEEMKSFAKAFISRANLgprlTQVSVLQYGSSTITAVPWNvaYEKAHLLSHVDLMQREGG 1766
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 823432200  1767 LSHIGDALDYAVRYVtsevhGARPGASKAVVILV 1800
Cdd:pfam13519   75 GTNLAAALQLARAAL-----KHRRKNQPRRIVLI 103
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 6.69e-07

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: 48.54  E-value: 6.69e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 823432200  1146 YNSCAPACPTTCQHPE-PLACPVPCVEGChaHCPPGKILDElLQTCISPEDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1276-1421 9.24e-07

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 51.62  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSE-DEFEVLKVFVVGMMERLHISQKRIRVAMVEYHDGSHAYIELKD--RKRPSELRRIASQVK--YV 1350
Cdd:cd01471     1 LDLYLLVDGSGSIGYsNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823432200 1351 GSEVASTSEVLKYTLFQIF-GKIDRPEASRIALIlMASQEPPRLARNLvRYVQGLKKKKVIVIPVGIGPHAN 1421
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFdTRGNRENAPQLVII-MTDGIPDSKFRTL-KEARKLRERGVIIAVLGVGQGVN 150
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 9.31e-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: 9.31e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823432200  2431 CVHRGTIYPVGQFWEEG-CDVCTCTDledsvmglRVAQCSQKPCEDN-CRSGFtYVIQEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLdCPNPR-LEIPPGECCPVC 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1645-1862 1.98e-06

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: 51.86  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1645 PNAPILIQDFETLPREAPDLVLQRCCSGEGPQSPTLAPTPDcSQPLDVALLLDGSSS-FPNSYFEEMKSFAKAFISRanL 1723
Cdd:COG1240    49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARP-QRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDD--Y 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1724 GPRlTQVSVLQYGSSTITAVPwnVAYEKAHLLSHVDLMQREGGlSHIGDALDYAVRYVTSEVHGARPgaskaVVILVT-- 1801
Cdd:COG1240   126 RPR-DRVGLVAFGGEAEVLLP--LTRDREALKRALDELPPGGG-TPLGDALALALELLKRADPARRK-----VIVLLTdg 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823432200 1802 --DVSADSVDAAADAATSNRVTVFPIGIG-DRYDEAQLRRLAGpNAGSNVLRLQRIEDLSTMAT 1862
Cdd:COG1240   197 rdNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE-ATGGRYFRADDLSELAAIYR 259
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 7.22e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.58  E-value: 7.22e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823432200   2261 DGVRHQFLETWVPAhqPCQICMCLSGRKVNCTSQPCPTARaptcgPCEVARLRQNAEQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2260-2322 1.47e-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: 44.72  E-value: 1.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200  2260 EDGVRHQFLETWVPAhqPCQICMCLSGrKVNCTSQPCPTAraptcgPCEVARLRQNAEQCCPE 2322
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 2.21e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 44.04  E-value: 2.21e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823432200   2582 CMLNGTIIGPGKSLMIDVCTTCRCTIQVgVISGFKLECRKTTckACPLGYKeEKNQGECCGKC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 4.67e-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: 43.18  E-value: 4.67e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2582 CMLNGTIIGPGKSLMIDVCTTCRCTiqvgvisGFKLECRKTTCKA--CPLGYkEEKNQGECCGKC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1691-1801 7.30e-05

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 46.16  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1691 DVALLLDGSSSFPNSYFE-EMKSFAKAFISRANLGPRLTQVSVLQYGSSTITAVPW--NVAYEKAHLLSHV-DLMQ--RE 1764
Cdd:cd01473     2 DLTLILDESASIGYSNWRkDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFsdEERYDKNELLKKInDLKNsyRS 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 823432200 1765 GGLSHIGDALDYAVRYVTSevHGARPGASKAVVILVT 1801
Cdd:cd01473    82 GGETYIVEALKYGLKNYTK--HGNRRKDAPKVTMLFT 116
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1689-1846 1.98e-04

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 45.86  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1689 PLDVALLLDGSSSfpnsyfeeM--------KSFAKAFISRanLGPRlTQVSVLQYGSSTITAVPWNVAYEKAHLLSHVDL 1760
Cdd:COG2304    91 PLNLVFVIDVSGS--------MsgdklelaKEAAKLLVDQ--LRPG-DRVSIVTFAGDARVLLPPTPATDRAKILAAIDR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1761 MQREGGLShIGDALDYAVRYVTSevhGARPGASKAVVIL------VTDVSADSVDAAADAATSNRVTVFPIGIGDRYDEA 1834
Cdd:COG2304   160 LQAGGGTA-LGAGLELAYELARK---HFIPGRVNRVILLtdgdanVGITDPEELLKLAEEAREEGITLTTLGVGSDYNED 235

                         170
                  ....*....|..
gi 823432200 1835 QLRRLAGPNAGS 1846
Cdd:COG2304   236 LLERLADAGGGN 247
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 2.28e-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: 41.15  E-value: 2.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200 2203 CPPSLVYNHCERGCPRLCE--GNTSSCGDHPSEGCFCPPNQVMLESS-CVPEEAC 2254
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 7.21e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 39.68  E-value: 7.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 823432200  2203 CPPSLVYNHCERGCPRLCE--GNTSSCGDHPSEGCFCPPNQVML-ESSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1498-1620 9.34e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.07  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1498 DVVFVLEGSDKIGEANFNKS-REFMEEVIQRMDVGQDSIHVMVLQYSYTVAVEYTFS--EAQSKGEVLQHVREIR--YRG 1572
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeERYDKNELLKKINDLKnsYRS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 823432200 1573 GNRTNTGLALQYlSEHSFSVSQGDREQVPNLVYMVT-GNPASDEIKRMP 1620
Cdd:cd01473    82 GGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTdGNDTSASKKELQ 129
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1276-1432 1.68e-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: 41.99  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1276 LDLVFLLDGSSKLSEDEFEVLKVFVVGMMERLHISQKR------IRVAMVEY-HDGSHAYIELKDRKRPSELRRIASQVK 1348
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1349 YVGsEVASTSEVLKYTLFQIFgKIDRPEASRIALILMASQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHAN--LKQIR 1426
Cdd:cd01480    83 YIG-GGTFTDCALKYATEQLL-EGSHQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNEepLSRIA 160


                  ....*.
gi 823432200 1427 NIEKQA 1432
Cdd:cd01480   161 CDGKSA 166
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1497-1642 2.16e-03

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: 41.89  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1497 LDVVFVLEGSDKIGEANFNKSREFMEEVIQRMDVGQDSIHVMVLQYSyTVAVE----YTFSEAQsKGEVLQHVREIRYRG 1572
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYA-SDPKEivsiRDFNSND-ADDVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1573 -GNR--TNTGLALQYLSEHSFSVSQGDRE---QVPNLVYMVT-------GNP--ASDEIKRMPG-------------DIQ 1624
Cdd:cd01470    79 hGDKtgTNTAAALKKVYERMALEKVRNKEafnETRHVIILFTdgksnmgGSPlpTVDKIKNLVYknnksdnpredylDVY 158

                         170
                  ....*....|....*...
gi 823432200 1625 VvpIGVGPHADVQELQSI 1642
Cdd:cd01470   159 V--FGVGDDVNKEELNDL 174
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
350-394 2.62e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 38.70  E-value: 2.62e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 823432200    350 CVHAGERYPPGSSLLQDCNTCICRNSLWICSNEEC-PGECLVTGQS 394
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1690-1799 3.18e-03

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: 41.22  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1690 LDVALLLDGSSSFPNS-YFEEMKSFAKAFISRANLGPRLTQVSVLQYgsSTITAVPWNVAYEKA-------HLLSHVDLM 1761
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTF--STNAKELIRLSSPNStnkdlalNAIRALLSL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 823432200 1762 QREGGLSHIGDALDyAVRYVTSEVHGARPGASKAVVIL 1799
Cdd:cd01471    79 YYPNGSTNTTSALL-VVEKHLFDTRGNRENAPQLVIIM 115
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 4.12e-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: 4.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 823432200  788 CAKTCQNYDLQ--CmSTGCVSGCLCPPGMVRHEN-KCVALERC 827
Cdd:cd19941    14 CPPTCANPNAPppC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1687-1867 7.15e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 40.29  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1687 SQPLDVALLLDGSSSFPNSYFEEMKSFAKAFIS--RANLGPRLT-QVSVLQYGSSTITAVPwnvayekahlLSHVDLMQ- 1762
Cdd:COG4245     3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDelRQDPYALETvEVSVITFDGEAKVLLP----------LTDLEDFQp 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823432200 1763 ---REGGLSHIGDALDYA-------VRYVTSEVHGARpgasKAVVILVT------DVSADSVDAAADAATSNRVTVFPIG 1826
Cdd:COG4245    73 pdlSASGGTPLGAALELLldlierrVQKYTAEGKGDW----RPVVFLITdgeptdSDWEAALQRLKDGEAAKKANIFAIG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 823432200 1827 IGDRYDEAQLRRLAGPN---AGSNVLRLQR-IEDLS-TMATLGNSF 1867
Cdd:COG4245   149 VGPDADTEVLKQLTDPVralDALDGLDFREfFKWLSaSVSSVSRSV 194
 
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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