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Conserved domains on  [gi|568941439|ref|XP_006505981|]
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von Willebrand factor isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 324-477 7.99e-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: 160.23  E-value: 7.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   324 CLVTGQSHFKSFDNRYFTFSGICQYLLARDC-EDHTFSIVIETMQCADDPDAVCTRSVSVRLSALHnslVKLKHGGAVGI 402
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   403 DGQDVQLPFLQGDLRIQHTVMASVRLSYAED--LQMDWDGRGRLLVKLSPVYSGKTCGLCGNYNGNKGDDFLTPAGL 477
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVVVDLSPGvgLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA pfam00092
von Willebrand factor type A domain;
1434-1594 7.12e-43

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 155.13  E-value: 7.12e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTN 1513
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVT-GNPASDEIKRL-----PGDIQVVPIGVGPhANMQELERIS---RPIAP 1584
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGN-ADDEELRKIAsepGEGHV 159

                          170
                   ....*....|
gi 568941439  1585 IFIRDFETLP 1594
Cdd:pfam00092  160 FTVSDFEALE 169
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1134-1212 4.47e-38

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: 137.80  E-value: 4.47e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439  1134 VCEVAGRRLAPGKKITLSPDDPAHCQNCHCDGVNLTCEACQEPGGLVAPPTDAPVSSTTPYVEDTPEPPLHNFYCSKLL 1212
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1627-1799 4.73e-38

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 141.64  E-value: 4.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVD-LMQQEGGPSQ 1705
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1706 IGDALAFAVRYVTSQIHGARPGASKAVVIIIMDTSLDP-VDTAADAARSNRVAVFPVGVGDRyDEAQLRILAGPGASSNV 1784
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 568941439  1785 VKlqqVEDLSTMATL 1799
Cdd:pfam00092  160 FT---VSDFEALEDL 171
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 792-947 4.58e-37

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


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 138.30  E-value: 4.58e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    792 WNCTNHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFQILVGNEGCSyPSVKCRKRVTILVDGGELE 871
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    872 LFDGEV-------NVKRPLRDESHFEVVES-GRYVILLLGQAL-SVVWDHHLSISVVLKHTYQEQVCGLCGNFDGIQNND 942
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 568941439    943 FTTSS 947
Cdd:smart00216  158 FRTPD 162
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1886-2038 7.96e-33

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.95  E-value: 7.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1886 CTGSSTRHIVTFDGQNFKLTGSCSYVIFQNKEQ--DLEVLLHNGACSPGAKQACMKSIEIKHAGVSAELHSNMEMAVDGR 1963
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  1964 LVLAPYVGENMEVSIYGAIMYEVRFtHLGHILTYTPQNNEFQLQLSPKTFASKMHGLCGICDENGANDFTLRDGT 2038
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1213-1385 9.70e-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: 106.38  E-value: 9.70e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1213 DLVFLLDGS-SMlSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVA 1291
Cdd:smart00327    1 DVVFLLDGSgSM-GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1292 STSEVLKYTLFQIFGKID--RPEASHITLLLTaSQEPPRMARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAP 1369
Cdd:smart00327   80 NLGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 568941439   1370 ENKAFLLSGVDELEQR 1385
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 989-1063 4.29e-21

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 89.32  E-value: 4.29e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439    989 QTMVDSACRILTSD--VFQGCNRLVDPEPYLDICIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-QVVAWRTPTLCP 1063
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 19-115 4.19e-20

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: 89.35  E-value: 4.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    19 SLSVYLGEFFdIHLFANGTVTQGDQSISMPYASQGLYLEREAGYYKLSSETFGFAARIDGNGNFQ--VLMSDRHFNKTCG 96
Cdd:pfam00094   57 SVTVIVGDLE-ITLQKGGTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCG 135

                           90
                   ....*....|....*....
gi 568941439    97 LCGDFNIFAEDDFRTQEGT 115
Cdd:pfam00094  136 LCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 515-585 1.16e-19

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 85.08  E-value: 1.16e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439    515 FAEEACALLTSSK--FEACHHAVSPLPYLQNCRYDVCSCSDSRDCLCNAVANYAAECARKGVHI-GWREPGFCA 585
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 154-228 5.51e-18

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 80.46  E-value: 5.51e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439    154 HQAMWEQCQLLKTAS-VFARCHPLVDPESFVALCEKILCTCATGPECACPVLLEYARTCAQEGMVLYGWTDHSACR 228
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2663-2744 9.62e-18

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


:

Pssm-ID: 214482  Cd Length: 82  Bit Score: 80.14  E-value: 9.62e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   2663 ITAKVQYIKVGDCKSqEEVDIHYCQGKCASKAVYSIdiEDVQEQCSCCLPSRTEPMRVPLHCTNGSVVYHEVINAMQCRC 2742
Cdd:smart00041    1 KSPVRQTITYNGCTS-VTVKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 568941439   2743 SP 2744
Cdd:smart00041   78 EP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 231-284 1.67e-13

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 66.96  E-value: 1.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  231 CPAGMEYKECVSPCPRTCQSLSINEVCQQQCVDGCSCPEGELLDED-RCVQSSDC 284
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 588-643 2.54e-12

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 2.54e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439  588 CPQGQVYLQCGNSCNLTCRSLSLPdEECSEVCLEGCYCPPGLYQDERGDCVPKAQC 643
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2074-2135 2.88e-12

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


:

Pssm-ID: 462584  Cd Length: 68  Bit Score: 63.94  E-value: 2.88e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439  2074 HCQVLLSAS-FAECHKVIAPATFHTICQQDSCH----QERVCEVIASYAHLCRTSGVCV-DWRTTDFC 2135
Cdd:pfam08742    1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
VWC smart00214
von Willebrand factor (vWF) type C domain;
2367-2430 2.78e-08

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 52.52  E-value: 2.78e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   2367 CVHRGTVYPVGQFWEEG-CDTCTCTDMEdtvvglrVVQCSQRPCEDS--CQPGFSyVLHEGECCGRC 2430
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1082-1132 9.38e-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: 50.78  E-value: 9.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568941439 1082 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGRILDElLQTCVDPQDC 1132
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2518-2580 4.77e-06

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


The actual alignment was detected with superfamily member pfam00093:

Pssm-ID: 450195  Cd Length: 57  Bit Score: 45.88  E-value: 4.77e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2518 CLLNGTIIGPGKSVMVDLCTTCRCIvqtdaisRFKLECRKTTCEA--CPMGyREEKSQGECCGRC 2580
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNP-RLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2193-2257 9.76e-06

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.20  E-value: 9.76e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439   2193 CVGeDGVRHQFLETWVPDhqPCQICMCLSGRKINCTAQPCPTARaptcgPCEVARLKQSTNLCCP 2257
Cdd:smart00214    1 CVH-NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2139-2190 1.81e-04

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 41.53  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439 2139 CPPSLVYNHCERGCPRHCD--GNTSFCGDHPSEGCFCPQHQVF-LEGSCVPEEAC 2190
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 286-330 2.91e-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: 38.31  E-value: 2.91e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568941439    286 CVHAGKRYPPGTSLSQDCNTCICRNSLWICSNEEC-PGECLVTGQS 330
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 724-763 4.02e-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: 4.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568941439  724 CAKTCQNYDL--ECmSLGCVSGCLCPPGMVRHEN-KCVALERC 763
Cdd:cd19941    14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 324-477 7.99e-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: 160.23  E-value: 7.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   324 CLVTGQSHFKSFDNRYFTFSGICQYLLARDC-EDHTFSIVIETMQCADDPDAVCTRSVSVRLSALHnslVKLKHGGAVGI 402
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   403 DGQDVQLPFLQGDLRIQHTVMASVRLSYAED--LQMDWDGRGRLLVKLSPVYSGKTCGLCGNYNGNKGDDFLTPAGL 477
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVVVDLSPGvgLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 313-476 6.58e-43

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 154.87  E-value: 6.58e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    313 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCEDH-TFSIVIETMQCadDPDAVCTRSVSVRLsalHNSL 391
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVEL---NGDE 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    392 VKLK-HGGAVGIDGQDVQLPFLQGDLRIQHTV---MASVRLSYAeDLQMDWDGRGRLLVKLSPVYSGKTCGLCGNYNGNK 467
Cdd:smart00216   76 IELKdDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 568941439    468 GDDFLTPAG 476
Cdd:smart00216  155 EDDFRTPDG 163
VWA pfam00092
von Willebrand factor type A domain;
1434-1594 7.12e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 155.13  E-value: 7.12e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTN 1513
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVT-GNPASDEIKRL-----PGDIQVVPIGVGPhANMQELERIS---RPIAP 1584
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGN-ADDEELRKIAsepGEGHV 159

                          170
                   ....*....|
gi 568941439  1585 IFIRDFETLP 1594
Cdd:pfam00092  160 FTVSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1433-1579 1.78e-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: 142.05  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRT 1512
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439 1513 NTGQALQYLSEHSFSPSQgDRVEAPNLVYMVT-GNP--------ASDEIKRLpgDIQVVPIGVGPhANMQELERIS 1579
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIA 152
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1134-1212 4.47e-38

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: 137.80  E-value: 4.47e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439  1134 VCEVAGRRLAPGKKITLSPDDPAHCQNCHCDGVNLTCEACQEPGGLVAPPTDAPVSSTTPYVEDTPEPPLHNFYCSKLL 1212
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1627-1799 4.73e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 141.64  E-value: 4.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVD-LMQQEGGPSQ 1705
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1706 IGDALAFAVRYVTSQIHGARPGASKAVVIIIMDTSLDP-VDTAADAARSNRVAVFPVGVGDRyDEAQLRILAGPGASSNV 1784
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 568941439  1785 VKlqqVEDLSTMATL 1799
Cdd:pfam00092  160 FT---VSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1434-1593 8.56e-38

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: 140.67  E-value: 8.56e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTN 1513
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVT-GNP---------ASDEIKRLPgdIQVVPIGVGPHANMQELERISRPIA 1583
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|
gi 568941439   1584 PIFIRDFETL 1593
Cdd:smart00327  159 GVYVFLPELL 168
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 792-947 4.58e-37

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 138.30  E-value: 4.58e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    792 WNCTNHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFQILVGNEGCSyPSVKCRKRVTILVDGGELE 871
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    872 LFDGEV-------NVKRPLRDESHFEVVES-GRYVILLLGQAL-SVVWDHHLSISVVLKHTYQEQVCGLCGNFDGIQNND 942
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 568941439    943 FTTSS 947
Cdd:smart00216  158 FRTPD 162
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 803-947 1.32e-33

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 127.87  E-value: 1.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   803 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFQILVGNEGCSYPSVkCRKRVTILVDGGELELFDG---EVN 878
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439   879 VKR---PL-RDESHFEVVESGR-YVILLLGQALSVVWDHHLSISVVLKHTYQEQVCGLCGNFDGIQNNDFTTSS 947
Cdd:pfam00094   79 GQKvslPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1886-2038 7.96e-33

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.95  E-value: 7.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1886 CTGSSTRHIVTFDGQNFKLTGSCSYVIFQNKEQ--DLEVLLHNGACSPGAKQACMKSIEIKHAGVSAELHSNMEMAVDGR 1963
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  1964 LVLAPYVGENMEVSIYGAIMYEVRFtHLGHILTYTPQNNEFQLQLSPKTFASKMHGLCGICDENGANDFTLRDGT 2038
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1627-1795 1.03e-32

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 126.42  E-value: 1.03e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQE-GGPSQ 1705
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1706 IGDALAFAVRYVTSQIHGARPGASKAVVII---IMDTSLDPVDTAADAARSNRVAVFPVGVGDRYDEAQLRILAGPGASS 1782
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILItdgESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|...
gi 568941439   1783 NVVKLQQVEDLST 1795
Cdd:smart00327  161 YVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1626-1785 1.41e-32

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 125.48  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1626 LDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGP-S 1704
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1705 QIGDALAFAVRYVTSQiHGARPGASKaVVIIIMD---TSLDPVDTAADAARSNRVAVFPVGVGDrYDEAQLRILAGPGAS 1781
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDgrsDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 568941439 1782 SNVV 1785
Cdd:cd01450   158 RHVF 161
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1874-2037 5.68e-30

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 117.89  E-value: 5.68e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1874 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVIFQN--KEQDLEVLLHNGACSPGAkqACMKSIEIKHAGVSAE 1951
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1952 LHS-NMEMAVDGRLVLAPYVGENMEVSIYGAIMYEVRFTHLGHI-LTYTPQNNeFQLQLSPKtFASKMHGLCGICDENGA 2029
Cdd:smart00216   78 LKDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 568941439   2030 NDFTLRDG 2037
Cdd:smart00216  156 DDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1213-1385 9.70e-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: 106.38  E-value: 9.70e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1213 DLVFLLDGS-SMlSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVA 1291
Cdd:smart00327    1 DVVFLLDGSgSM-GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1292 STSEVLKYTLFQIFGKID--RPEASHITLLLTaSQEPPRMARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAP 1369
Cdd:smart00327   80 NLGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 568941439   1370 ENKAFLLSGVDELEQR 1385
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1212-1374 4.06e-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: 103.91  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1212 LDLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVA 1291
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1292 STSEVLKYTLFQIFGKI-DRPEASHITLLLTASQepPRMARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIRLIEKQAPE 1370
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 568941439 1371 NKAF 1374
Cdd:cd01450   158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 989-1063 4.29e-21

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 89.32  E-value: 4.29e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439    989 QTMVDSACRILTSD--VFQGCNRLVDPEPYLDICIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-QVVAWRTPTLCP 1063
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 19-115 4.19e-20

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: 89.35  E-value: 4.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    19 SLSVYLGEFFdIHLFANGTVTQGDQSISMPYASQGLYLEREAGYYKLSSETFGFAARIDGNGNFQ--VLMSDRHFNKTCG 96
Cdd:pfam00094   57 SVTVIVGDLE-ITLQKGGTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCG 135

                           90
                   ....*....|....*....
gi 568941439    97 LCGDFNIFAEDDFRTQEGT 115
Cdd:pfam00094  136 LCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 515-585 1.16e-19

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 85.08  E-value: 1.16e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439    515 FAEEACALLTSSK--FEACHHAVSPLPYLQNCRYDVCSCSDSRDCLCNAVANYAAECARKGVHI-GWREPGFCA 585
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 520-584 2.26e-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: 81.27  E-value: 2.26e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   520 CALLTSSK-FEACHHAVSPLPYLQNCRYDVCSCSDSRDCLCNAVANYAAECARKGVHIG-WREPGFC 584
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 154-228 5.51e-18

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 80.46  E-value: 5.51e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439    154 HQAMWEQCQLLKTAS-VFARCHPLVDPESFVALCEKILCTCATGPECACPVLLEYARTCAQEGMVLYGWTDHSACR 228
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2663-2744 9.62e-18

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


Pssm-ID: 214482  Cd Length: 82  Bit Score: 80.14  E-value: 9.62e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   2663 ITAKVQYIKVGDCKSqEEVDIHYCQGKCASKAVYSIdiEDVQEQCSCCLPSRTEPMRVPLHCTNGSVVYHEVINAMQCRC 2742
Cdd:smart00041    1 KSPVRQTITYNGCTS-VTVKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 568941439   2743 SP 2744
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 996-1062 1.93e-17

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 78.58  E-value: 1.93e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439   996 CRILT-SDVFQGCNRLVDPEPYLDICIYDTCSCEsiGDCACFCDTIAAYAHVCAQHGQVVA-WRTPTLC 1062
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1213-1384 1.24e-15

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 76.93  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1213 DLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYhdGSRAYLE--LKARKRPSELRRITSQIKYTGSQV 1290
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1291 ASTSEVLKYTLFQIFGKI--DRPEASHITLLLTA----SQEPPRMARNlvryvqgLKKKKVIVIPVGIGPhASLKQIRLI 1364
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKI 150

                          170       180
                   ....*....|....*....|
gi 568941439  1365 EKQAPENKAFLLSGVDELEQ 1384
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 160-227 8.81e-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: 71.26  E-value: 8.81e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439   160 QCQLLKTASVFARCHPLVDPESFVALCEKILCTCATGPECACPVLLEYARTCAQEGMVLYGWTDHSAC 227
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 6-114 2.06e-14

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: 73.20  E-value: 2.06e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439      6 VLTKRNFQDG---KRMSLSVYLGEFfDIHLF-ANGTVTQGDQSISMPYASQGLYLERE-AGYYKLSSETFGFA-ARIDGN 79
Cdd:smart00216   50 VLLKNVPCGGgatCLKSVKVELNGD-EIELKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGLIqVTFDGL 128

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 568941439     80 GNFQVLMSDRHFNKTCGLCGDFNIFAEDDFRTQEG 114
Cdd:smart00216  129 TLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 231-284 1.67e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 66.96  E-value: 1.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  231 CPAGMEYKECVSPCPRTCQSLSINEVCQQQCVDGCSCPEGELLDED-RCVQSSDC 284
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 588-643 2.54e-12

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 2.54e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439  588 CPQGQVYLQCGNSCNLTCRSLSLPdEECSEVCLEGCYCPPGLYQDERGDCVPKAQC 643
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2074-2135 2.88e-12

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 63.94  E-value: 2.88e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439  2074 HCQVLLSAS-FAECHKVIAPATFHTICQQDSCH----QERVCEVIASYAHLCRTSGVCV-DWRTTDFC 2135
Cdd:pfam08742    1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 231-284 6.50e-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: 62.40  E-value: 6.50e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439   231 CPAGMEYKECVSPCPRTCQSLSINEVCQQQCVDGCSCPEGELLDED-RCVQSSDC 284
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 588-643 1.78e-11

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 61.25  E-value: 1.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439   588 CPQGQVYLQCGNSCNLTCRSLSLPDEeCSEVCLEGCYCPPGLYQDERGDCVPKAQC 643
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2070-2136 9.00e-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: 60.05  E-value: 9.00e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439   2070 SDSSHCQVLLSAS--FAECHKVIAPATFHTICQQDSC----HQERVCEVIASYAHLCRTSGVCV-DWRTTDFCA 2136
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1624-1776 1.79e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1624 QPLDVVLLLDGSSS-LPESSFDKMKSFAKAFISKANIGphlTQVSVIQYGSinTIDVPWNVVQEKAHLQSLVDLMQQEGG 1702
Cdd:COG1240    91 RGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDYRPR---DRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439 1703 pSQIGDALAFAVRYVTSqihgARPGASKAVVII---IMDTSLDPVDTAADAARSNRVAVFPVGVG-DRYDEAQLRILA 1776
Cdd:COG1240   166 -TPLGDALALALELLKR----ADPARRKVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIA 238
VWC smart00214
von Willebrand factor (vWF) type C domain;
2367-2430 2.78e-08

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 52.52  E-value: 2.78e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   2367 CVHRGTVYPVGQFWEEG-CDTCTCTDMEdtvvglrVVQCSQRPCEDS--CQPGFSyVLHEGECCGRC 2430
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1082-1132 9.38e-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: 50.78  E-value: 9.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568941439 1082 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGRILDElLQTCVDPQDC 1132
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2367-2430 1.34e-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: 50.50  E-value: 1.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2367 CVHRGTVYPVGQFWEEG-CDTCTCTDmedtvvglRVVQCSQRPCEDSCQPGFSYVLHEGECCGRC 2430
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1082-1132 2.12e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 2.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941439  1082 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGRILDElLQTCVDPQDC 1132
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2518-2580 4.77e-06

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 45.88  E-value: 4.77e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2518 CLLNGTIIGPGKSVMVDLCTTCRCIvqtdaisRFKLECRKTTCEA--CPMGyREEKSQGECCGRC 2580
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNP-RLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2193-2257 9.76e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.20  E-value: 9.76e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439   2193 CVGeDGVRHQFLETWVPDhqPCQICMCLSGRKINCTAQPCPTARaptcgPCEVARLKQSTNLCCP 2257
Cdd:smart00214    1 CVH-NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1433-1579 2.24e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 47.61  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGS--------DEVGEAnfnkskefVEEVIQRMDVSPDAT---RISVLQYSYTVTMEYAFngaQSKEEVlrHV 1501
Cdd:COG4245     6 LPVYLLLDTSgsmsgepiEALNEG--------LQALIDELRQDPYALetvEVSVITFDGEAKVLLPL---TDLEDF--QP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1502 REIRYQGGnrTNTGQALQYL-----SEHSFSPSQGDRVEAPnLVYMVT-GNP-------ASDEIKRLPGD--IQVVPIGV 1566
Cdd:COG4245    73 PDLSASGG--TPLGAALELLldlieRRVQKYTAEGKGDWRP-VVFLITdGEPtdsdweaALQRLKDGEAAkkANIFAIGV 149

                         170
                  ....*....|...
gi 568941439 1567 GPHANMQELERIS 1579
Cdd:COG4245   150 GPDADTEVLKQLT 162
VWC smart00214
von Willebrand factor (vWF) type C domain;
2518-2580 4.26e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 43.27  E-value: 4.26e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941439   2518 CLLNGTIIGPGKSVMVDLCTTCRCIVQTdAISRFKLECRKTTceACPMGYReEKSQGECCGRC 2580
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2139-2190 1.81e-04

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 41.53  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439 2139 CPPSLVYNHCERGCPRHCD--GNTSFCGDHPSEGCFCPQHQVF-LEGSCVPEEAC 2190
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2196-2258 3.85e-04

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 40.49  E-value: 3.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941439  2196 EDGVRHQFLETWVPDhqPCQICMCLSGrKINCTAQPCPTAraptcgPCEVARLKQSTNLCCPE 2258
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2139-2190 7.04e-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: 7.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2139 CPPSLVYNHCERGCPRHCD--GNTSFCGDHPSEGCFCPQHQVFL-EGSCVPEEAC 2190
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 2667-2742 1.72e-03

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


Pssm-ID: 460786  Cd Length: 108  Bit Score: 40.35  E-value: 1.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439  2667 VQYIKVGDCKSQEeVDIHYCQGKCASKAV-YSIDIEDVQEQ-CSCCLPSRTEPMRVPLHCT-NGSVVYHEVINAMQCRC 2742
Cdd:pfam03045   30 TQTITEEGCLSRT-VQNRFCYGQCNSFYIpNSIGRGKWSFAsCSRCKPSKFTTVTVTLNCPgGPPTRTKRVMRVKECKC 107
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
286-330 2.91e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 38.31  E-value: 2.91e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568941439    286 CVHAGKRYPPGTSLSQDCNTCICRNSLWICSNEEC-PGECLVTGQS 330
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 724-763 4.02e-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: 4.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568941439  724 CAKTCQNYDL--ECmSLGCVSGCLCPPGMVRHEN-KCVALERC 763
Cdd:cd19941    14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 324-477 7.99e-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: 160.23  E-value: 7.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   324 CLVTGQSHFKSFDNRYFTFSGICQYLLARDC-EDHTFSIVIETMQCADDPDAVCTRSVSVRLSALHnslVKLKHGGAVGI 402
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   403 DGQDVQLPFLQGDLRIQHTVMASVRLSYAED--LQMDWDGRGRLLVKLSPVYSGKTCGLCGNYNGNKGDDFLTPAGL 477
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVVVDLSPGvgLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 313-476 6.58e-43

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 154.87  E-value: 6.58e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    313 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCEDH-TFSIVIETMQCadDPDAVCTRSVSVRLsalHNSL 391
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVEL---NGDE 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    392 VKLK-HGGAVGIDGQDVQLPFLQGDLRIQHTV---MASVRLSYAeDLQMDWDGRGRLLVKLSPVYSGKTCGLCGNYNGNK 467
Cdd:smart00216   76 IELKdDNGKVTVNGQQVSLPYKTSDGSIQIRSsggYLVVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 568941439    468 GDDFLTPAG 476
Cdd:smart00216  155 EDDFRTPDG 163
VWA pfam00092
von Willebrand factor type A domain;
1434-1594 7.12e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 155.13  E-value: 7.12e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTN 1513
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVT-GNPASDEIKRL-----PGDIQVVPIGVGPhANMQELERIS---RPIAP 1584
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGN-ADDEELRKIAsepGEGHV 159

                          170
                   ....*....|
gi 568941439  1585 IFIRDFETLP 1594
Cdd:pfam00092  160 FTVSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1433-1579 1.78e-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: 142.05  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRT 1512
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439 1513 NTGQALQYLSEHSFSPSQgDRVEAPNLVYMVT-GNP--------ASDEIKRLpgDIQVVPIGVGPhANMQELERIS 1579
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIA 152
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1134-1212 4.47e-38

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: 137.80  E-value: 4.47e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439  1134 VCEVAGRRLAPGKKITLSPDDPAHCQNCHCDGVNLTCEACQEPGGLVAPPTDAPVSSTTPYVEDTPEPPLHNFYCSKLL 1212
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1627-1799 4.73e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 141.64  E-value: 4.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVD-LMQQEGGPSQ 1705
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1706 IGDALAFAVRYVTSQIHGARPGASKAVVIIIMDTSLDP-VDTAADAARSNRVAVFPVGVGDRyDEAQLRILAGPGASSNV 1784
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNA-DDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 568941439  1785 VKlqqVEDLSTMATL 1799
Cdd:pfam00092  160 FT---VSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1434-1593 8.56e-38

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: 140.67  E-value: 8.56e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTN 1513
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVT-GNP---------ASDEIKRLPgdIQVVPIGVGPHANMQELERISRPIA 1583
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|
gi 568941439   1584 PIFIRDFETL 1593
Cdd:smart00327  159 GVYVFLPELL 168
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1434-1579 1.25e-37

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: 140.06  E-value: 1.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNrTN 1513
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568941439 1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVTGNPASDEIkRLPG------DIQVVPIGVGPhANMQELERIS 1579
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDV-EEPAvelkqaGIEVFAVGVKN-ADEEELKQIA 150
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 792-947 4.58e-37

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 138.30  E-value: 4.58e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    792 WNCTNHVCDATCSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFQILVGNEGCSyPSVKCRKRVTILVDGGELE 871
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    872 LFDGEV-------NVKRPLRDESHFEVVES-GRYVILLLGQAL-SVVWDHHLSISVVLKHTYQEQVCGLCGNFDGIQNND 942
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 568941439    943 FTTSS 947
Cdd:smart00216  158 FRTPD 162
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1434-1579 8.69e-35

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: 131.68  E-value: 8.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTN 1513
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568941439 1514 TGQALQYLSEHSFSPSQGDRVE--APNLVYMVTGNPASDEIKRLPGDIQ---VVPIGVGP-HANMQELERIS 1579
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQIA 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 803-947 1.32e-33

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 127.87  E-value: 1.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   803 CSAIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFQILVGNEGCSYPSVkCRKRVTILVDGGELELFDG---EVN 878
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439   879 VKR---PL-RDESHFEVVESGR-YVILLLGQALSVVWDHHLSISVVLKHTYQEQVCGLCGNFDGIQNNDFTTSS 947
Cdd:pfam00094   79 GQKvslPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1886-2038 7.96e-33

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.95  E-value: 7.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1886 CTGSSTRHIVTFDGQNFKLTGSCSYVIFQNKEQ--DLEVLLHNGACSPGAKQACMKSIEIKHAGVSAELHSNMEMAVDGR 1963
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  1964 LVLAPYVGENMEVSIYGAIMYEVRFtHLGHILTYTPQNNEFQLQLSPKTFASKMHGLCGICDENGANDFTLRDGT 2038
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1627-1795 1.03e-32

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 126.42  E-value: 1.03e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQE-GGPSQ 1705
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1706 IGDALAFAVRYVTSQIHGARPGASKAVVII---IMDTSLDPVDTAADAARSNRVAVFPVGVGDRYDEAQLRILAGPGASS 1782
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILItdgESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|...
gi 568941439   1783 NVVKLQQVEDLST 1795
Cdd:smart00327  161 YVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1626-1785 1.41e-32

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 125.48  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1626 LDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGP-S 1704
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1705 QIGDALAFAVRYVTSQiHGARPGASKaVVIIIMD---TSLDPVDTAADAARSNRVAVFPVGVGDrYDEAQLRILAGPGAS 1781
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTDgrsDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 568941439 1782 SNVV 1785
Cdd:cd01450   158 RHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1434-1581 1.89e-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: 119.31  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1434 DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNrTN 1513
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439 1514 TGQALQYLSEHSFSPSQGDRVEAPNLVYMVTGNPASDEIkRLPGD------IQVVPIGVGpHANMQELERI-SRP 1581
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGVK-DADESELKMIaSKP 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1874-2037 5.68e-30

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 117.89  E-value: 5.68e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1874 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVIFQN--KEQDLEVLLHNGACSPGAkqACMKSIEIKHAGVSAE 1951
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1952 LHS-NMEMAVDGRLVLAPYVGENMEVSIYGAIMYEVRFTHLGHI-LTYTPQNNeFQLQLSPKtFASKMHGLCGICDENGA 2029
Cdd:smart00216   78 LKDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 568941439   2030 NDFTLRDG 2037
Cdd:smart00216  156 DDFRTPDG 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1433-1583 7.91e-27

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 110.94  E-value: 7.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRY--QGgn 1510
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1511 rTNTGQALQYLSEHSFSPSQGDR---VEAPNLVYMVTGNPASDEIK------RLPGdIQVVPIGVGpHANMQELERI-SR 1580
Cdd:cd01475    81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIaSE 157


                  ...
gi 568941439 1581 PIA 1583
Cdd:cd01475   158 PLA 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1213-1385 9.70e-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: 106.38  E-value: 9.70e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1213 DLVFLLDGS-SMlSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVA 1291
Cdd:smart00327    1 DVVFLLDGSgSM-GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   1292 STSEVLKYTLFQIFGKID--RPEASHITLLLTaSQEPPRMARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAP 1369
Cdd:smart00327   80 NLGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 568941439   1370 ENKAFLLSGVDELEQR 1385
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1212-1374 4.06e-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: 103.91  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1212 LDLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVA 1291
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1292 STSEVLKYTLFQIFGKI-DRPEASHITLLLTASQepPRMARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIRLIEKQAPE 1370
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 568941439 1371 NKAF 1374
Cdd:cd01450   158 RHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1627-1786 1.86e-24

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: 102.31  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGPSQI 1706
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1707 GDALAFAVRYVTSQIHGARPGASKAVVIIIMDTSLDPVDTAADAARSNRVAVFPVGVGDRyDEAQLRILAGPGASSNVVK 1786
Cdd:cd01472    82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNA-DEEELKQIASDPKELYVFN 160
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1626-1785 6.23e-24

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 100.72  E-value: 6.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1626 LDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQE-GGPS 1704
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1705 QIGDALAFAVRYVTSQIHGARpgasKAVVIIIMD----TSLDPVDTAADAARSNRVAVFPVGVGDRYDEAQLRILAGPGA 1780
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA----RRVIILLTDgepnDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTT 156


                  ....*
gi 568941439 1781 SSNVV 1785
Cdd:cd00198   157 GGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1625-1825 7.79e-24

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 102.46  E-value: 7.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1625 PLDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGPS 1704
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1705 QIGDALAFAVRYVTSQIHGARPGASKA--VVIIIMD-TSLDPVDTAADAARSNRVAVFPVGVGdRYDEAQLRILAGPGAS 1781
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVprVGIVVTDgRPQDDVSEVAAKARALGIEMFAVGVG-RADEEELREIASEPLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568941439 1782 SNVVklqQVEDLSTMATLGNSFFHKLCSGfSGVCVDEDGNEKRP 1825
Cdd:cd01475   161 DHVF---YVEDFSTIEELTKKFQGKICVV-PDLCATLSHVCQQV 200
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 989-1063 4.29e-21

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 89.32  E-value: 4.29e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439    989 QTMVDSACRILTSD--VFQGCNRLVDPEPYLDICIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-QVVAWRTPTLCP 1063
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1433-1581 6.48e-21

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: 91.86  E-value: 6.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRT 1512
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439 1513 NTGQALQYLSEHSFSPsqgDRVEAPNLVYMVT-GNP---------ASDEIKRLpgDIQVVPIGVGPHANMQELERISRP 1581
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEIADK 154
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1626-1767 9.81e-21

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 92.03  E-value: 9.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1626 LDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGPSQ 1705
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439 1706 IGDALAFAVRYVTSQIHGARPGASKaVVIIIMDTSL--DPVDTAA-DAARSNRVAVFPVGVGDRY 1767
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATK-VLVVITDGEShdDPLLKDViPQAEREGIIRYAIGVGGHF 144
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 19-115 4.19e-20

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: 89.35  E-value: 4.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439    19 SLSVYLGEFFdIHLFANGTVTQGDQSISMPYASQGLYLEREAGYYKLSSETFGFAARIDGNGNFQ--VLMSDRHFNKTCG 96
Cdd:pfam00094   57 SVTVIVGDLE-ITLQKGGTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCG 135

                           90
                   ....*....|....*....
gi 568941439    97 LCGDFNIFAEDDFRTQEGT 115
Cdd:pfam00094  136 LCGNYNGNQEDDFMTPDGT 154
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1433-1581 5.40e-20

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 89.72  E-value: 5.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGnRT 1512
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1513 NTGQALQYLSEHSFSPSQGDRVEAPNLVYMVTGNPASDEikrlPGDIQVVP-----------IGVGPHAN----MQELER 1577
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDD----PLLKDVIPqaeregiiryaIGVGGHFQrensREELKT 155


                  ....*
gi 568941439 1578 I-SRP 1581
Cdd:cd01469   156 IaSKP 160
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 515-585 1.16e-19

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 85.08  E-value: 1.16e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439    515 FAEEACALLTSSK--FEACHHAVSPLPYLQNCRYDVCSCSDSRDCLCNAVANYAAECARKGVHI-GWREPGFCA 585
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1627-1778 2.65e-19

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: 87.34  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGPSQI 1706
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568941439 1707 GDALAFAVRYVTSQIHGARPGASKAVVIIIMDTSLDPVDTAADAARSNRVAVFPVGVGDrYDEAQLRILAGP 1778
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKD-ADESELKMIASK 152
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1433-1587 1.33e-18

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: 85.14  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEAnFNKSKEFVEEVIQRMDVSPDATRISVLQYS--YTVTMEYAFNGAQSKEEVLRHVREIRYQGGN 1510
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1511 rTNTGQALQYLSEHsFSPSQGDRVEAPNLVYMVTG-----NP--ASDEIKRLPGdIQVVPIGVG--PHANMQELERISRP 1581
Cdd:cd01476    80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDgrshdDPekQARILRAVPN-IETFAVGTGdpGTVDTEELHSITGN 156


                  ....*.
gi 568941439 1582 IAPIFI 1587
Cdd:cd01476   157 EDHIFT 162
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 520-584 2.26e-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: 81.27  E-value: 2.26e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   520 CALLTSSK-FEACHHAVSPLPYLQNCRYDVCSCSDSRDCLCNAVANYAAECARKGVHIG-WREPGFC 584
Cdd:pfam08742    2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1626-1777 3.77e-18

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: 83.99  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1626 LDVVLLLDGSSSLpESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNV--VQEKAHLQSLVDLMQQEGGP 1703
Cdd:cd01476     1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLpkHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439 1704 SQIGDALAFAVRYVTSQiHGARPGASKAVVIIIMDTSLDPVDTAADAARSN-RVAVFPVGVGDR--YDEAQLRILAG 1777
Cdd:cd01476    80 TATGAAIEVALQQLDPS-EGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDPgtVDTEELHSITG 155
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 154-228 5.51e-18

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 80.46  E-value: 5.51e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439    154 HQAMWEQCQLLKTAS-VFARCHPLVDPESFVALCEKILCTCATGPECACPVLLEYARTCAQEGMVLYGWTDHSACR 228
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2663-2744 9.62e-18

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


Pssm-ID: 214482  Cd Length: 82  Bit Score: 80.14  E-value: 9.62e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439   2663 ITAKVQYIKVGDCKSqEEVDIHYCQGKCASKAVYSIdiEDVQEQCSCCLPSRTEPMRVPLHCTNGSVVYHEVINAMQCRC 2742
Cdd:smart00041    1 KSPVRQTITYNGCTS-VTVKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 568941439   2743 SP 2744
Cdd:smart00041   78 EP 79
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 996-1062 1.93e-17

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 78.58  E-value: 1.93e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439   996 CRILT-SDVFQGCNRLVDPEPYLDICIYDTCSCEsiGDCACFCDTIAAYAHVCAQHGQVVA-WRTPTLC 1062
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWA pfam00092
von Willebrand factor type A domain;
1213-1384 1.24e-15

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 76.93  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1213 DLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYhdGSRAYLE--LKARKRPSELRRITSQIKYTGSQV 1290
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1291 ASTSEVLKYTLFQIFGKI--DRPEASHITLLLTA----SQEPPRMARNlvryvqgLKKKKVIVIPVGIGPhASLKQIRLI 1364
Cdd:pfam00092   79 TNTGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKI 150

                          170       180
                   ....*....|....*....|
gi 568941439  1365 EKQAPENKAFLLSGVDELEQ 1384
Cdd:pfam00092  151 ASEPGEGHVFTVSDFEALED 170
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1433-1574 1.69e-15

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 77.04  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEAN-FNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNG--AQSKE---EVLRHVREIRY 1506
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDlalNAIRALLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439 1507 QGGNrTNTGQALQYLSEHSFSpSQGDRVEAPNLVYMVT-GNPASD--------EIKRLPGDIQVvpIGVGPHANMQE 1574
Cdd:cd01471    81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEE 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1212-1374 7.35e-15

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 74.52  E-value: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1212 LDLVFLLDGS-SMLSEAeFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQV 1290
Cdd:cd00198     1 ADIVFLLDVSgSMGGEK-LDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1291 ASTSEVLKYTLfQIFGKIDRPEASHITLLLTASqEPPRMARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAPE 1370
Cdd:cd00198    80 TNIGAALRLAL-ELLKSAKRPNARRVIILLTDG-EPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG 157


                  ....
gi 568941439 1371 NKAF 1374
Cdd:cd00198   158 GAVF 161
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 160-227 8.81e-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: 71.26  E-value: 8.81e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439   160 QCQLLKTASVFARCHPLVDPESFVALCEKILCTCATGPECACPVLLEYARTCAQEGMVLYGWTDHSAC 227
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1627-1776 2.05e-14

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 73.51  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGG-PSQ 1705
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941439 1706 IGDALAFAVRYVTSQIHGAR--PGASKAVVIIIMDTSLDPVDTAADAARSNRVAVFPVGVGDrYDEAQLRILA 1776
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARN-ADLAELQQIA 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 6-114 2.06e-14

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: 73.20  E-value: 2.06e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439      6 VLTKRNFQDG---KRMSLSVYLGEFfDIHLF-ANGTVTQGDQSISMPYASQGLYLERE-AGYYKLSSETFGFA-ARIDGN 79
Cdd:smart00216   50 VLLKNVPCGGgatCLKSVKVELNGD-EIELKdDNGKVTVNGQQVSLPYKTSDGSIQIRsSGGYLVVITSLGLIqVTFDGL 128

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 568941439     80 GNFQVLMSDRHFNKTCGLCGDFNIFAEDDFRTQEG 114
Cdd:smart00216  129 TLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 231-284 1.67e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 66.96  E-value: 1.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  231 CPAGMEYKECVSPCPRTCQSLSINEVCQQQCVDGCSCPEGELLDED-RCVQSSDC 284
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 588-643 2.54e-12

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 2.54e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439  588 CPQGQVYLQCGNSCNLTCRSLSLPdEECSEVCLEGCYCPPGLYQDERGDCVPKAQC 643
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2074-2135 2.88e-12

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 63.94  E-value: 2.88e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439  2074 HCQVLLSAS-FAECHKVIAPATFHTICQQDSCH----QERVCEVIASYAHLCRTSGVCV-DWRTTDFC 2135
Cdd:pfam08742    1 KCGLLSDSGpFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 231-284 6.50e-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: 62.40  E-value: 6.50e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439   231 CPAGMEYKECVSPCPRTCQSLSINEVCQQQCVDGCSCPEGELLDED-RCVQSSDC 284
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1433-1528 8.35e-12

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: 66.25  E-value: 8.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRM------DVSPDATRISVLQYSYTVTMEYAFNGA-QSKEEVLRHVREIR 1505
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82

                          90       100
                  ....*....|....*....|....*..
gi 568941439 1506 YQGGNrTNTGQALQY----LSEHSFSP 1528
Cdd:cd01480    83 YIGGG-TFTDCALKYateqLLEGSHQK 108
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 588-643 1.78e-11

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 61.25  E-value: 1.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439   588 CPQGQVYLQCGNSCNLTCRSLSLPDEeCSEVCLEGCYCPPGLYQDERGDCVPKAQC 643
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1213-1361 6.80e-11

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: 63.02  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1213 DLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVAs 1292
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439 1293 TSEVLKYTLFQIFGKIDRPEAS--HITLLLTASQEP---PRMARNlvryvqgLKKKKVIVIPVGIGPHAS--LKQI 1361
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQddvEEPAVE-------LKQAGIEVFAVGVKNADEeeLKQI 149
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2070-2136 9.00e-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: 60.05  E-value: 9.00e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941439   2070 SDSSHCQVLLSAS--FAECHKVIAPATFHTICQQDSC----HQERVCEVIASYAHLCRTSGVCV-DWRTTDFCA 2136
Cdd:smart00832    3 YACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1212-1306 7.81e-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: 61.63  E-value: 7.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1212 LDLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKY--TGSQ 1289
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTGTM 82

                          90
                  ....*....|....*..
gi 568941439 1290 vasTSEVLKYTLFQIFG 1306
Cdd:cd01475    83 ---TGLAIQYAMNNAFS 96
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1624-1776 1.79e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1624 QPLDVVLLLDGSSS-LPESSFDKMKSFAKAFISKANIGphlTQVSVIQYGSinTIDVPWNVVQEKAHLQSLVDLMQQEGG 1702
Cdd:COG1240    91 RGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDYRPR---DRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941439 1703 pSQIGDALAFAVRYVTSqihgARPGASKAVVII---IMDTSLDPVDTAADAARSNRVAVFPVGVG-DRYDEAQLRILA 1776
Cdd:COG1240   166 -TPLGDALALALELLKR----ADPARRKVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIA 238
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1625-1780 1.99e-09

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 59.32  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1625 PLDVVLLLDGSSSLPESSFDKMKSFAKAFIS------KANIGPHLTQVSVIQY-GSINTIDVPWNVVQEKAHLQSLVDLM 1697
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1698 QQEGGPSQIGDALAfavrYVTSQIHGARPGASKAVVIIIMDTSLDPVDTAAD-----AARSNRVAVFPVGVGDRYDEAQL 1772
Cdd:cd01480    82 EYIGGGTFTDCALK----YATEQLLEGSHQKENKFLLVITDGHSDGSPDGGIekavnEADHLGIKIFFVAVGSQNEEPLS 157


                  ....*...
gi 568941439 1773 RILAGPGA 1780
Cdd:cd01480   158 RIACDGKS 165
VWA_2 pfam13519
von Willebrand factor type A domain;
1628-1735 5.63e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 55.76  E-value: 5.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1628 VVLLLDGSSS-----LPESSFDKMKSFAKAFISKANIgphlTQVSVIQYGSINTIDVPWNvvQEKAHLQSLVDLMQQEGG 1702
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568941439  1703 PSQIGDALAFAvryvTSQIHGARPGASKAVVII 1735
Cdd:pfam13519   75 GTNLAAALQLA----RAALKHRRKNQPRRIVLI 103
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1213-1333 5.73e-09

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: 57.68  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1213 DLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQvAS 1292
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568941439 1293 TSEVLKYTLFQIF--GKIDRPEASHITLLLT--ASQ----EPPRMARNL 1333
Cdd:cd01482    81 TGKALTHVREKNFtpDAGARPGVPKVVILITdgKSQddveLPARVLRNL 129
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1213-1307 1.53e-08

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 56.18  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1213 DLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSQVAS 1292
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90
                  ....*....|....*
gi 568941439 1293 TSEVLKYTLFQIFGK 1307
Cdd:cd01481    82 TGSALDYVVKNLFTK 96
VWC smart00214
von Willebrand factor (vWF) type C domain;
2367-2430 2.78e-08

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 52.52  E-value: 2.78e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941439   2367 CVHRGTVYPVGQFWEEG-CDTCTCTDMEdtvvglrVVQCSQRPCEDS--CQPGFSyVLHEGECCGRC 2430
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1082-1132 9.38e-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: 50.78  E-value: 9.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568941439 1082 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGRILDElLQTCVDPQDC 1132
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2367-2430 1.34e-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: 50.50  E-value: 1.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2367 CVHRGTVYPVGQFWEEG-CDTCTCTDmedtvvglRVVQCSQRPCEDSCQPGFSYVLHEGECCGRC 2430
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1625-1779 3.74e-07

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 54.34  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1625 PLDVVLLLDGSSSLPESSFDKMKSFAKAFISkaNIGPHlTQVSVIQYGSINTIDVPWNVVQEKAHLQSLVDLMQQEGGpS 1704
Cdd:COG2304    91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVD--QLRPG-DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGG-T 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1705 QIGDALAFAVRYVTSqihGARPGASKaVVIIIMD-------TSLDPVDTAADAARSNRVAVFPVGVGDRYDEAQLRILAG 1777
Cdd:COG2304   167 ALGAGLELAYELARK---HFIPGRVN-RVILLTDgdanvgiTDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242


                  ..
gi 568941439 1778 PG 1779
Cdd:COG2304   243 AG 244
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1212-1377 4.87e-07

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 52.36  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1212 LDLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKARKRPSELRRITSQIKYTGSqVA 1291
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1292 STSEVLKYTLFQIF--GKIDRPEASHITLLLT--ASQEPPRMARNLvryvQGLKKKKVIVIPVGIGPH----ASLKQIRL 1363
Cdd:cd01469    80 NTATAIQYVVTELFseSNGARKDATKVLVVITdgESHDDPLLKDVI----PQAEREGIIRYAIGVGGHfqreNSREELKT 155

                         170
                  ....*....|....
gi 568941439 1364 IEKQAPENKAFLLS 1377
Cdd:cd01469   156 IASKPPEEHFFNVT 169
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1082-1132 2.12e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 2.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941439  1082 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGRILDElLQTCVDPQDC 1132
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2518-2580 4.77e-06

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 45.88  E-value: 4.77e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2518 CLLNGTIIGPGKSVMVDLCTTCRCIvqtdaisRFKLECRKTTCEA--CPMGyREEKSQGECCGRC 2580
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCD-------DGKVLCDKIICPPldCPNP-RLEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2193-2257 9.76e-06

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 45.20  E-value: 9.76e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439   2193 CVGeDGVRHQFLETWVPDhqPCQICMCLSGRKINCTAQPCPTARaptcgPCEVARLKQSTNLCCP 2257
Cdd:smart00214    1 CVH-NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPP-----DCPNPERVKPPGECCP 57
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1433-1579 2.24e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 47.61  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGS--------DEVGEAnfnkskefVEEVIQRMDVSPDAT---RISVLQYSYTVTMEYAFngaQSKEEVlrHV 1501
Cdd:COG4245     6 LPVYLLLDTSgsmsgepiEALNEG--------LQALIDELRQDPYALetvEVSVITFDGEAKVLLPL---TDLEDF--QP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1502 REIRYQGGnrTNTGQALQYL-----SEHSFSPSQGDRVEAPnLVYMVT-GNP-------ASDEIKRLPGD--IQVVPIGV 1566
Cdd:COG4245    73 PDLSASGG--TPLGAALELLldlieRRVQKYTAEGKGDWRP-VVFLITdGEPtdsdweaALQRLKDGEAAkkANIFAIGV 149

                         170
                  ....*....|...
gi 568941439 1567 GPHANMQELERIS 1579
Cdd:COG4245   150 GPDADTEVLKQLT 162
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1626-1777 3.10e-05

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: 46.99  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1626 LDVVLLLDGSSSLPESS-FDKMKSFAKAFISKANIGPHLTQVSVIQYGSINT--IDVPWNVVQEK-------AHLQSlvd 1695
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKelIRLSSPNSTNKdlalnaiRALLS--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1696 lMQQEGGPSQIGDALAfAVRYVTSQIHGARPGASKAVVIIIMDTSLDPVDTAADAA----RSNRVAVFPVGVGDRYDEAq 1771
Cdd:cd01471    78 -LYYPNGSTNTTSALL-VVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEARklreRGVIIAVLGVGQGVNHEEN- 154


                  ....*.
gi 568941439 1772 lRILAG 1777
Cdd:cd01471   155 -RSLVG 159
VWC smart00214
von Willebrand factor (vWF) type C domain;
2518-2580 4.26e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 43.27  E-value: 4.26e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941439   2518 CLLNGTIIGPGKSVMVDLCTTCRCIVQTdAISRFKLECRKTTceACPMGYReEKSQGECCGRC 2580
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPER-VKPPGECCPRC 59
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1433-1578 4.55e-05

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: 46.90  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1433 LDVVFVLEGSDEVGEANFNKSKEFVEEVIQRM---DVSPdatRISVLQYS---YTVTMEYAFNGAQsKEEVLRHVREIRY 1506
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKIssyEVSP---RYEIISYAsdpKEIVSIRDFNSND-ADDVIKRLEDFNY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1507 QG-GNR--TNTGQALQYLSEHSFSPSQGDR---VEAPNLVYMVT-------GNP--ASDEIKRLPG-------------D 1558
Cdd:cd01470    77 DDhGDKtgTNTAAALKKVYERMALEKVRNKeafNETRHVIILFTdgksnmgGSPlpTVDKIKNLVYknnksdnpredylD 156

                         170       180
                  ....*....|....*....|
gi 568941439 1559 IQVvpIGVGPHANMQELERI 1578
Cdd:cd01470   157 VYV--FGVGDDVNKEELNDL 174
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1212-1353 5.80e-05

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: 46.22  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1212 LDLVFLLDGSSMLSEA-EFEVLKAFVVGMMERLHISQKRIRVAVVEYHDGSRAYLELKA--RKRPSELRRITSQIKYTGS 1288
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941439 1289 QVAST------SEVLKYtLFQifGKIDRPEASHITLLLT--ASQEPPRmARNLVRyvqGLKKKKVIVIPVGIG 1353
Cdd:cd01471    81 PNGSTnttsalLVVEKH-LFD--TRGNRENAPQLVIIMTdgIPDSKFR-TLKEAR---KLRERGVIIAVLGVG 146
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1627-1776 1.55e-04

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 46.21  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1627 DVVLLLDGSSSLPESSFDKMKSFAKAFISKANigPHLtQVSVIQYGSINTIDVPWNvvqEKAHLQSLVDLMQQ---EGGp 1703
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTEVVEDLPLT---ADDGLEDAIEFLSGlfaGGG- 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941439 1704 SQIGDALAFAVRYVTsqihgaRPGASKAVVIIIMD--TSLDPVDTAADA-ARSNRVAVFPVGVGDRYDEAQLRILA 1776
Cdd:COG2425   193 TDIAPALRAALELLE------EPDYRNADIVLITDgeAGVSPEELLREVrAKESGVRLFTVAIGDAGNPGLLEALA 262
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2139-2190 1.81e-04

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 41.53  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439 2139 CPPSLVYNHCERGCPRHCD--GNTSFCGDHPSEGCFCPQHQVF-LEGSCVPEEAC 2190
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWA_2 pfam13519
von Willebrand factor type A domain;
1435-1523 3.24e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.28  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439  1435 VVFVLEGS-----DEVGEANFNKSKEFVEEVIQRMDvspdATRISVLQYSYTVTMEYAFNgaQSKEEVLRHVREIRYQGG 1509
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90
                   ....*....|....
gi 568941439  1510 NrTNTGQALQYLSE 1523
Cdd:pfam13519   75 G-TNLAAALQLARA 87
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2196-2258 3.85e-04

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 40.49  E-value: 3.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941439  2196 EDGVRHQFLETWVPDhqPCQICMCLSGrKINCTAQPCPTAraptcgPCEVARLKQSTNLCCPE 2258
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPL------DCPNPRLEIPPGECCPV 56
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2139-2190 7.04e-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: 7.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941439  2139 CPPSLVYNHCERGCPRHCD--GNTSFCGDHPSEGCFCPQHQVFL-EGSCVPEEAC 2190
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1627-1765 8.52e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 42.70  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1627 DVVLLLDGSSSL------PESSFDKMKSFAKAFISKA---NIGphltqvsVIQYGSINTIDVPWNVVQE--KAHLQSLVD 1695
Cdd:cd01467     4 DIMIALDVSGSMlaqdfvKPSRLEAAKEVLSDFIDRRendRIG-------LVVFAGAAFTQAPLTLDREslKELLEDIKI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941439 1696 LMQQEGgpSQIGDALAFAVRYVTSQihgarpGASKAVVIIIMDTS-----LDPvDTAADAARSNRVAVFPVGVGD 1765
Cdd:cd01467    77 GLAGQG--TAIGDAIGLAIKRLKNS------EAKERVIVLLTDGEnnageIDP-ATAAELAKNKGVRIYTIGVGK 142
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1213-1381 1.05e-03

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 42.69  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1213 DLVFLLD--GSSMLSEAEFEVLKaFVVGMMERLHISQKRIRVAVVEYHDGSRAYLEL--KARKRPSEL-RRITSQIKYTG 1287
Cdd:cd01473     2 DLTLILDesASIGYSNWRKDVIP-FTEKIINNLNISKDKVHVGILLFAEKNRDVVPFsdEERYDKNELlKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1288 SQVAS-TSEVLKYTLFQIFGKIDRPEAS-HITLLLTASQEPPRMARNLVRYVQGLKKKKVIVIPVGIGphaslkqirlie 1365
Cdd:cd01473    81 SGGETyIVEALKYGLKNYTKHGNRRKDApKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVG------------ 148

                         170
                  ....*....|....*.
gi 568941439 1366 kQAPENKAFLLSGVDE 1381
Cdd:cd01473   149 -AASENKLKLLAGCDI 163
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 2667-2742 1.72e-03

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


Pssm-ID: 460786  Cd Length: 108  Bit Score: 40.35  E-value: 1.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941439  2667 VQYIKVGDCKSQEeVDIHYCQGKCASKAV-YSIDIEDVQEQ-CSCCLPSRTEPMRVPLHCT-NGSVVYHEVINAMQCRC 2742
Cdd:pfam03045   30 TQTITEEGCLSRT-VQNRFCYGQCNSFYIpNSIGRGKWSFAsCSRCKPSKFTTVTVTLNCPgGPPTRTKRVMRVKECKC 107
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
286-330 2.91e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 38.31  E-value: 2.91e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568941439    286 CVHAGKRYPPGTSLSQDCNTCICRNSLWICSNEEC-PGECLVTGQS 330
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 724-763 4.02e-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: 4.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568941439  724 CAKTCQNYDL--ECmSLGCVSGCLCPPGMVRHEN-KCVALERC 763
Cdd:cd19941    14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1623-1779 6.20e-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: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1623 SQPLDVVLLLDGSSSLPESSFDKMKSFAKAFIS--KANIGPHLT-QVSVIQYGSintiDVPWnvvqekahLQSLVDLMQ- 1698
Cdd:COG4245     3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDelRQDPYALETvEVSVITFDG----EAKV--------LLPLTDLEDf 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941439 1699 -----QEGGPSQIGDALAFA-------VRYVTSQIHGARpgasKAVVIIIMD---TSLD---PVDTAADAARSNRVAVFP 1760
Cdd:COG4245    71 qppdlSASGGTPLGAALELLldlierrVQKYTAEGKGDW----RPVVFLITDgepTDSDweaALQRLKDGEAAKKANIFA 146

                         170
                  ....*....|....*....
gi 568941439 1761 VGVGDRYDEAQLRILAGPG 1779
Cdd:COG4245   147 IGVGPDADTEVLKQLTDPV 165
 
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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