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Conserved domains on  [gi|1813372009|ref|NP_000543|]
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von Willebrand factor preproprotein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.15e-46

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: 165.24  E-value: 1.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  388 CLVTGQSHFKSFDNRYFTFSGICQYLLARDC-QDHSFSIVIETVQCADDRDAVCTRSVTVRLPGLHnslVKLKHGAGVAM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  467 DGQDVQLPLLKGDLRIQHTV--TASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 1.11e-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: 139.73  E-value: 1.11e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1813372009 1198 VCEVAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 2.46e-38

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 142.41  E-value: 2.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVT-GNPASDEIKRL-----PGDIQVVPIGVGpNANVQELERIGWPNAP--- 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVG-NADDEELRKIASEPGEghv 159

                          170
                   ....*....|
gi 1813372009 1649 ILIQDFETLP 1658
Cdd:pfam00092  160 FTVSDFEALE 169
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 3.48e-38

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: 140.97  E-value: 3.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1950 CTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2028 LVSVPYVGGNMEVNVYGAIMHEVRFnHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 6.45e-38

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: 140.61  E-value: 6.45e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   856 WNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNKGCShPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   936 LFDGEV-------NVKRPMKDETHFEVVES-GRYIILLLGKAL-SVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 1813372009  1007 LTSSN 1011
Cdd:smart00216  158 FRTPD 162
VWA pfam00092
von Willebrand factor type A domain;
1691-1862 1.64e-35

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 134.32  E-value: 1.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVD-VMQREGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1770 IGDALGFAVRYLTSEMHGARPGASKaVVILVT--DVSVDSVDAAADAARSNRVTVFPIGIGDRYDaAQLRILAGPAGDSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTdgRSQDGDPEEVARELKSAGVTVFAVGVGNADD-EELRKIASEPGEGH 158

                          170
                   ....*....|....*
gi 1813372009 1848 VVKLQRIEDLPTMVT 1862
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 2.52e-34

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 130.18  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   35 CSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRS-FSIIGDFQNGKR-------VSLSVYLGEFFdIHLFVNGTVTQGD 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGgasgvclKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  107 QRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 2.76e-29

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: 116.40  E-value: 2.76e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1357 TSEVLKYTLFQIFSKID--RPEASRItLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 1813372009  1435 NKAFVLSSVDELEQQ 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 2.31e-21

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 90.09  E-value: 2.31e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009  1053 QTMVDSSCRILTSD--VFQDCNKLVDPEPYLDVCIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-KVVTWRTATLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-291 1.33e-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: 1.33e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009   222 WEQCQLLKSTS-VFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSAC 291
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 2.71e-19

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: 84.38  E-value: 2.71e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  2727 ITARLQYVKVGSCKSEVeVDIHYCQGKCASKAMYSIdiNDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 1813372009  2807 SP 2808
Cdd:smart00041   78 EP 79
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2135-2200 3.97e-13

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: 66.60  E-value: 3.97e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009  2135 DSSHCQVLLLPL--FAECHKVLAPATFYAICQQDSC----HQEQVCEVIASYAHLCRTNGVCV-DWRTPDFCA 2200
Cdd:smart00832    4 ACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 4.27e-13

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 65.80  E-value: 4.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009  652 CPKGQVYLQCGTPCNLTCRSLSYPdEECNEACLEGCFCPPGLYMDERGDCVPKAQC 707
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 7.26e-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: 62.33  E-value: 7.26e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  295 CPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDE-GLCVESTEC 348
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-648 4.86e-09

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 55.04  E-value: 4.86e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009   579 FSEEACAVLTSP--TFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRV-AWREPGRC 648
Cdd:smart00832    3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFC 75
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 4.50e-08

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 51.75  E-value: 4.50e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009  2261 DGVQHQFLEAWVPDhqPCQICTCLSGRKVNCTTQPCPTAKAptcglCEVARLRQNADQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPPD-----CPNPERVKPPGECCP 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 5.83e-08

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.16  E-value: 5.83e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1813372009 1146 YNSCAPACQVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDPEDC 1196
Cdd:cd19941      7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 1.14e-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: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2582 CMLNGTVIGPGKTVMIDVCTTCRCMVqvgvisgFKLECRKTTCNP--CPLGYkEENNTGECCGRC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 5.98e-07

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.67  E-value: 5.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  2431 CVHRSTIYPVGQFWEEG-CDVCTCTDMEdavmglrVAQCSQKPCEDS--CRSGFTyVLHEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 9.98e-05

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.30  E-value: 9.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2203 CPPSLVYNHCEHGCPRHCD--GNVSSCGDHPSEGCFCPPDKVM-LEGSCVPEEAC 2254
Cdd:cd19941      1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 350-394 1.92e-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: 39.08  E-value: 1.92e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1813372009   350 CVHSGKRYPPGTSLSRDCNTCICRNSQWICSNEEC-PGECLVTGQS 394
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 2.59e-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: 38.07  E-value: 2.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1813372009  788 CTKTCQNYDL--ECmSMGCVSGCLCPPGMVRHEN-RCVALERC 827
Cdd:cd19941     14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.15e-46

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: 165.24  E-value: 1.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  388 CLVTGQSHFKSFDNRYFTFSGICQYLLARDC-QDHSFSIVIETVQCADDRDAVCTRSVTVRLPGLHnslVKLKHGAGVAM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  467 DGQDVQLPLLKGDLRIQHTV--TASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 1.44e-45

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: 162.57  E-value: 1.44e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   377 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCQDH-SFSIVIETVQCadDRDAVCTRSVTVRLPGLhnSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVELNGD--EI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   456 VKLKHGAGVAMDGQDVQLPLLKGDLRIQHTVTAS---VRLSYGeDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGylvVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1813372009   533 DDFLTPSG 540
Cdd:smart00216  156 DDFRTPDG 163
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 1.11e-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: 139.73  E-value: 1.11e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1813372009 1198 VCEVAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 2.46e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 142.41  E-value: 2.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVT-GNPASDEIKRL-----PGDIQVVPIGVGpNANVQELERIGWPNAP--- 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVG-NADDEELRKIASEPGEghv 159

                          170
                   ....*....|
gi 1813372009 1649 ILIQDFETLP 1658
Cdd:pfam00092  160 FTVSDFEALE 169
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 3.48e-38

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: 140.97  E-value: 3.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1950 CTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2028 LVSVPYVGGNMEVNVYGAIMHEVRFnHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 6.45e-38

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: 140.61  E-value: 6.45e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   856 WNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNKGCShPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   936 LFDGEV-------NVKRPMKDETHFEVVES-GRYIILLLGKAL-SVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 1813372009  1007 LTSSN 1011
Cdd:smart00216  158 FRTPD 162
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1645 1.55e-36

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: 136.65  E-value: 1.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRT 1576
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 1577 NTGLALRYLSDHSFLVSQgDREQAPNLVYMVT-GNP--------ASDEIKRLpgDIQVVPIGVGPnANVQELERIGWP 1645
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154
VWA pfam00092
von Willebrand factor type A domain;
1691-1862 1.64e-35

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 134.32  E-value: 1.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVD-VMQREGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1770 IGDALGFAVRYLTSEMHGARPGASKaVVILVT--DVSVDSVDAAADAARSNRVTVFPIGIGDRYDaAQLRILAGPAGDSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTdgRSQDGDPEEVARELKSAGVTVFAVGVGNADD-EELRKIASEPGEGH 158

                          170
                   ....*....|....*
gi 1813372009 1848 VVKLQRIEDLPTMVT 1862
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 9.86e-35

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 131.34  E-value: 9.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  867 CSTIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFRILVGNKGCSHPSVkCKKRVTILVEGGEIELFDG---EVN 942
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1813372009  943 VKR---PMK-DETHFEVVESGRYIILL-LGKALSVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNNDLTSSN 1011
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFVVVDLsPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 2.52e-34

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 130.18  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   35 CSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRS-FSIIGDFQNGKR-------VSLSVYLGEFFdIHLFVNGTVTQGD 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGgasgvclKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  107 QRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 6.23e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 129.44  E-value: 6.23e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1938 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHNGACSPGArqGCMKSIEVKHSALSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  2016 LHSD-MEVTVNGRLVSVPYVGGNMEVNVYGAIMHEVRFNHLGHI-FTFTPQNNeFQLQLSPKtFASKTYGLCGICDENGA 2093
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1813372009  2094 NDFMLRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1642 1.04e-31

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 123.33  E-value: 1.04e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVT-GNP---------ASDEIKRLPgdIQVVPIGVGPNANVQELERI 1642
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 33-178 5.65e-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: 5.65e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009    33 ARCSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKR-SFSIIG-----DFQNGKRVSLSVYLGEFfDIHLF-VNGTVTQG 105
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLknvpcGGGATCLKSVKVELNGD-EIELKdDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009   106 DQRVSMPYASKGLYLETE-AGYYKLSGEAYG-FVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEG 178
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 2.76e-29

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: 116.40  E-value: 2.76e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1357 TSEVLKYTLFQIFSKID--RPEASRItLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 1813372009  1435 NKAFVLSSVDELEQQ 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1857 4.14e-29

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: 116.01  E-value: 4.14e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQRE-GGPSQ 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1770 IGDALGFAVRYLTSEMHGARPGASKaVVILVT----DVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGd 1845
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITdgesNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG- 158

                           170
                    ....*....|..
gi 1813372009  1846 SNVVKLQRIEDL 1857
Cdd:smart00327  159 GVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 1.94e-28

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: 113.54  E-value: 1.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1690 LDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGP-S 1768
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1769 QIGDALGFAVRYLTSEmHGARPGASKaVVILVT---DVSVDSVDAAADAARSNRVTVFPIGIGDrYDAAQLRILAGPAGD 1845
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTdgrSDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                   ....
gi 1813372009 1846 SNVV 1849
Cdd:cd01450    158 RHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 3.86e-27

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: 109.69  E-value: 3.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVA 1355
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1356 STSEVLKYTLFQIFSKI-DRPEASRITLLLMASQepQRMSRNFVRYVQGLKKKKVIVIPVGIGPhANLKQIRLIEKQAPE 1434
Cdd:cd01450     81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                   ....
gi 1813372009 1435 NKAF 1438
Cdd:cd01450    158 RHVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 2.31e-21

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 90.09  E-value: 2.31e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009  1053 QTMVDSSCRILTSD--VFQDCNKLVDPEPYLDVCIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-KVVTWRTATLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-291 1.33e-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: 1.33e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009   222 WEQCQLLKSTS-VFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSAC 291
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 2.71e-19

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: 84.38  E-value: 2.71e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  2727 ITARLQYVKVGSCKSEVeVDIHYCQGKCASKAMYSIdiNDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 1813372009  2807 SP 2808
Cdd:smart00041   78 EP 79
VWA pfam00092
von Willebrand factor type A domain;
1277-1452 1.95e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.40  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAS 1356
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1357 TSEVLKYTLFQIFSKI--DRPEASRITLLL----MASQEPQRMSRNfvryvqgLKKKKVIVIPVGIGPHANlKQIRLIEK 1430
Cdd:pfam00092   81 TGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 1813372009 1431 QAPENKAFVLSSVDELEQQRDE 1452
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1060-1126 1.98e-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: 1.98e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1813372009 1060 CRILT-SDVFQDCNKLVDPEPYLDVCIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-KVVTWRTATLC 1126
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 3.45e-17

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 77.81  E-value: 3.45e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009  224 QCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSAC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2135-2200 3.97e-13

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: 66.60  E-value: 3.97e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009  2135 DSSHCQVLLLPL--FAECHKVLAPATFYAICQQDSC----HQEQVCEVIASYAHLCRTNGVCV-DWRTPDFCA 2200
Cdd:smart00832    4 ACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 4.27e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 65.80  E-value: 4.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009  652 CPKGQVYLQCGTPCNLTCRSLSYPdEECNEACLEGCFCPPGLYMDERGDCVPKAQC 707
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 1.36e-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: 65.09  E-value: 1.36e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 2138 HCQVLLL-PLFAECHKVLAPATFYAICQQDSCH----QEQVCEVIASYAHLCRTNGVCV-DWRTPDFC 2199
Cdd:pfam08742    1 KCGLLSDsGPFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 3.85e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.18  E-value: 3.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009  652 CPKGQVYLQCGTPCNLTCRSLSYPDEeCNEACLEGCFCPPGLYMDERGDCVPKAQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 7.26e-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: 62.33  E-value: 7.26e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  295 CPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDE-GLCVESTEC 348
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 1.16e-11

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 62.02  E-value: 1.16e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  295 CPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLD-EGLCVESTEC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-648 4.86e-09

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 55.04  E-value: 4.86e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009   579 FSEEACAVLTSP--TFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRV-AWREPGRC 648
Cdd:smart00832    3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFC 75
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 4.50e-08

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 51.75  E-value: 4.50e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009  2261 DGVQHQFLEAWVPDhqPCQICTCLSGRKVNCTTQPCPTAKAptcglCEVARLRQNADQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPPD-----CPNPERVKPPGECCP 57
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 5.83e-08

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.16  E-value: 5.83e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1813372009 1146 YNSCAPACQVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDPEDC 1196
Cdd:cd19941      7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 1.14e-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: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2582 CMLNGTVIGPGKTVMIDVCTTCRCMVqvgvisgFKLECRKTTCNP--CPLGYkEENNTGECCGRC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 1.81e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 50.21  E-value: 1.81e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009  2582 CMLNGTVIGPGKTVMIDVCTTCRCMVQVgVISGFKLECRKTTcnPCPLGYKEENNtGECCGRC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPERVKPP-GECCPRC 59
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 2.36e-07

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: 50.07  E-value: 2.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  584 CAVLT-SPTFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRVA-WREPGRC 648
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2260-2322 3.13e-07

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 3.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009 2260 EDGVQHQFLEAWVPDhqPCQICTCLSGrKVNCTTQPCPTAKaptcglCEVARLRQNADQCCPE 2322
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPLD------CPNPRLEIPPGECCPV 56
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 5.98e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.67  E-value: 5.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  2431 CVHRSTIYPVGQFWEEG-CDVCTCTDMEdavmglrVAQCSQKPCEDS--CRSGFTyVLHEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 1.09e-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: 47.77  E-value: 1.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1813372009 1146 YNSCAPACQVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDPEDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 1.60e-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: 47.42  E-value: 1.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009 2431 CVHRSTIYPVGQFWEEG-CDVCTCTDmedavmglRVAQCSQKPCED-SCRSGFtYVLHEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPlDCPNPR-LEIPPGECCPVC 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1611-1862 2.83e-05

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: 48.40  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1611 PASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRCCSGEGLQIPTLSPAPDCSQPL 1690
Cdd:COG1240     14 ALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPA-SYFDEMKSFAKAFISKanIGPRlTQVSVLQYGsiTTIDVPWNVVPEKAHLLSLVDVMQREGGpSQ 1769
Cdd:COG1240     94 DVVLVVDASGSMAAeNRLEAAKGALLDFLDD--YRPR-DRVGLVAFG--GEAEVLLPLTRDREALKRALDELPPGGG-TP 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1770 IGDALGFAVRYLTSEmhgaRPGASKaVVILVT----DVSVDSVDAAADAARSNRVTVFPIGIG-DRYDAAQLRILAGpAG 1844
Cdd:COG1240    168 LGDALALALELLKRA----DPARRK-VIVLLTdgrdNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE-AT 241

                          250
                   ....*....|....*...
gi 1813372009 1845 DSNVVKLQRIEDLPTMVT 1862
Cdd:COG1240    242 GGRYFRADDLSELAAIYR 259
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 9.98e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.30  E-value: 9.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2203 CPPSLVYNHCEHGCPRHCD--GNVSSCGDHPSEGCFCPPDKVM-LEGSCVPEEAC 2254
Cdd:cd19941      1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 6.73e-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: 40.06  E-value: 6.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2203 CPPSLVYNHCEHGCPRHCD--GNVSSCGDHPSEGCFCPPDKVML-EGSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
350-394 1.92e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 39.08  E-value: 1.92e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1813372009   350 CVHSGKRYPPGTSLSRDCNTCICRNSQWICSNEEC-PGECLVTGQS 394
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 2.59e-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: 38.07  E-value: 2.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1813372009  788 CTKTCQNYDL--ECmSMGCVSGCLCPPGMVRHEN-RCVALERC 827
Cdd:cd19941     14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 388-541 1.15e-46

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: 165.24  E-value: 1.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  388 CLVTGQSHFKSFDNRYFTFSGICQYLLARDC-QDHSFSIVIETVQCADDRDAVCTRSVTVRLPGLHnslVKLKHGAGVAM 466
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLE---ITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  467 DGQDVQLPLLKGDLRIQHTV--TASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSGL 541
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGsgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 377-540 1.44e-45

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: 162.57  E-value: 1.44e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   377 WICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCQDH-SFSIVIETVQCadDRDAVCTRSVTVRLPGLhnSL 455
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVELNGD--EI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   456 VKLKHGAGVAMDGQDVQLPLLKGDLRIQHTVTAS---VRLSYGeDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQG 532
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGylvVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1813372009   533 DDFLTPSG 540
Cdd:smart00216  156 DDFRTPDG 163
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1198-1276 1.11e-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: 139.73  E-value: 1.11e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1813372009 1198 VCEVAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLL 1276
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
1498-1658 2.46e-38

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 142.41  E-value: 2.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTN 1577
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVT-GNPASDEIKRL-----PGDIQVVPIGVGpNANVQELERIGWPNAP--- 1648
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVG-NADDEELRKIASEPGEghv 159

                          170
                   ....*....|
gi 1813372009 1649 ILIQDFETLP 1658
Cdd:pfam00092  160 FTVSDFEALE 169
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1950-2102 3.48e-38

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: 140.97  E-value: 3.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1950 CTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGR 2027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2028 LVSVPYVGGNMEVNVYGAIMHEVRFnHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRDGT 2102
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDL-SPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 856-1011 6.45e-38

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: 140.61  E-value: 6.45e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   856 WNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPgTFRILVGNKGCShPSVKCKKRVTILVEGGEIE 935
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-CSSEP-TFSVLLKNVPCG-GGATCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   936 LFDGEV-------NVKRPMKDETHFEVVES-GRYIILLLGKAL-SVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNND 1006
Cdd:smart00216   78 LKDDNGkvtvngqQVSLPYKTSDGSIQIRSsGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*
gi 1813372009  1007 LTSSN 1011
Cdd:smart00216  158 FRTPD 162
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1645 1.55e-36

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: 136.65  E-value: 1.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRT 1576
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 1577 NTGLALRYLSDHSFLVSQgDREQAPNLVYMVT-GNP--------ASDEIKRLpgDIQVVPIGVGPnANVQELERIGWP 1645
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154
VWA pfam00092
von Willebrand factor type A domain;
1691-1862 1.64e-35

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 134.32  E-value: 1.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVD-VMQREGGPSQ 1769
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDnLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1770 IGDALGFAVRYLTSEMHGARPGASKaVVILVT--DVSVDSVDAAADAARSNRVTVFPIGIGDRYDaAQLRILAGPAGDSN 1847
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPK-VVVLLTdgRSQDGDPEEVARELKSAGVTVFAVGVGNADD-EELRKIASEPGEGH 158

                          170
                   ....*....|....*
gi 1813372009 1848 VVKLQRIEDLPTMVT 1862
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 867-1011 9.86e-35

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 131.34  E-value: 9.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  867 CSTIGMAHYLTFDGLKYLFPGECQYVLVQDyCGSNPG-TFRILVGNKGCSHPSVkCKKRVTILVEGGEIELFDG---EVN 942
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD-CSEEPDfSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGgtvLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1813372009  943 VKR---PMK-DETHFEVVESGRYIILL-LGKALSVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNNDLTSSN 1011
Cdd:pfam00094   79 GQKvslPYKsDGGEVEILGSGFVVVDLsPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 35-179 2.52e-34

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 130.18  E-value: 2.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009   35 CSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRS-FSIIGDFQNGKR-------VSLSVYLGEFFdIHLFVNGTVTQGD 106
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGgasgvclKSVTVIVGDLE-ITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  107 QRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQ--VLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGT 179
Cdd:pfam00094   80 QKVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1938-2101 6.23e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 129.44  E-value: 6.23e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1938 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHNGACSPGArqGCMKSIEVKHSALSVE 2015
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  2016 LHSD-MEVTVNGRLVSVPYVGGNMEVNVYGAIMHEVRFNHLGHI-FTFTPQNNeFQLQLSPKtFASKTYGLCGICDENGA 2093
Cdd:smart00216   78 LKDDnGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1813372009  2094 NDFMLRDG 2101
Cdd:smart00216  156 DDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1498-1642 1.04e-31

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 123.33  E-value: 1.04e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTN 1577
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVT-GNP---------ASDEIKRLPgdIQVVPIGVGPNANVQELERI 1642
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1498-1642 6.83e-31

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: 120.80  E-value: 6.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNrTN 1577
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009 1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVTGNPASDEIkRLPG------DIQVVPIGVGpNANVQELERI 1642
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDV-EEPAvelkqaGIEVFAVGVK-NADEEELKQI 149
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1498-1654 4.34e-30

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: 118.20  E-value: 4.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTN 1577
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1578 TGLALRYLSDHSFLVSQGDR--EQAPNLVYMVTGNPASDEIKRLPGDIQ---VVPIGVGP-NANVQELERIGW-PNAPIL 1650
Cdd:cd01481     82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQIAFdPSFVFQ 161


                   ....
gi 1813372009 1651 IQDF 1654
Cdd:cd01481    162 VSDF 165
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 33-178 5.65e-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: 5.65e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009    33 ARCSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKR-SFSIIG-----DFQNGKRVSLSVYLGEFfDIHLF-VNGTVTQG 105
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLknvpcGGGATCLKSVKVELNGD-EIELKdDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009   106 DQRVSMPYASKGLYLETE-AGYYKLSGEAYG-FVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEG 178
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRsSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1277-1449 2.76e-29

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: 116.40  E-value: 2.76e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAS 1356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1357 TSEVLKYTLFQIFSKID--RPEASRItLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPE 1434
Cdd:smart00327   81 LGAALQYALENLFSKSAgsRRGAPKV-VILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 1813372009  1435 NKAFVLSSVDELEQQ 1449
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1691-1857 4.14e-29

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: 116.01  E-value: 4.14e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQRE-GGPSQ 1769
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  1770 IGDALGFAVRYLTSEMHGARPGASKaVVILVT----DVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGd 1845
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPK-VVILITdgesNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG- 158

                           170
                    ....*....|..
gi 1813372009  1846 SNVVKLQRIEDL 1857
Cdd:smart00327  159 GVYVFLPELLDL 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 1.94e-28

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: 113.54  E-value: 1.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1690 LDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGP-S 1768
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1769 QIGDALGFAVRYLTSEmHGARPGASKaVVILVT---DVSVDSVDAAADAARSNRVTVFPIGIGDrYDAAQLRILAGPAGD 1845
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPK-VIIVLTdgrSDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                   ....
gi 1813372009 1846 SNVV 1849
Cdd:cd01450    158 RHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 3.86e-27

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: 109.69  E-value: 3.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVA 1355
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1356 STSEVLKYTLFQIFSKI-DRPEASRITLLLMASQepQRMSRNFVRYVQGLKKKKVIVIPVGIGPhANLKQIRLIEKQAPE 1434
Cdd:cd01450     81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                   ....
gi 1813372009 1435 NKAF 1438
Cdd:cd01450    158 RHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1498-1643 1.17e-25

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: 105.45  E-value: 1.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNrTN 1577
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1813372009 1578 TGLALRYLSDHSFLVSQGDREQAPNLVYMVTGNPASDEIkRLPGD------IQVVPIGVGpNANVQELERIG 1643
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGVK-DADESELKMIA 150
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1127 2.31e-21

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 90.09  E-value: 2.31e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009  1053 QTMVDSSCRILTSD--VFQDCNKLVDPEPYLDVCIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-KVVTWRTATLCP 1127
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1497-1643 7.18e-21

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: 93.99  E-value: 7.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRY--QGgn 1574
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 1575 rTNTGLALRYLSDHSFLVSQGDR---EQAPNLVYMVTGNPASDEIK------RLPGdIQVVPIGVGpNANVQELERIG 1643
Cdd:cd01475     81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIA 155
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1690-1849 7.94e-20

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 88.78  E-value: 7.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1690 LDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVD-VMQREGGPS 1768
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDaLKKGLGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1769 QIGDALGFAVRYLTSEMHGARpgasKAVVILVT----DVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAG 1844
Cdd:cd00198     81 NIGAALRLALELLKSAKRPNA----RRVIILLTdgepNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTT 156


                   ....*
gi 1813372009 1845 DSNVV 1849
Cdd:cd00198    157 GGAVF 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 222-291 1.33e-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: 1.33e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009   222 WEQCQLLKSTS-VFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSAC 291
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1497-1642 1.46e-19

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 88.01  E-value: 1.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRT 1576
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009 1577 NTGLALRYLSDhsfLVSQGDREQAPNLVYMVT-GNP---------ASDEIKRLpgDIQVVPIGVGPNANVQELERI 1642
Cdd:cd00198     81 NIGAALRLALE---LLKSAKRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEI 151
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2727-2808 2.71e-19

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: 84.38  E-value: 2.71e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009  2727 ITARLQYVKVGSCKSEVeVDIHYCQGKCASKAMYSIdiNDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKC 2806
Cdd:smart00041    1 KSPVRQTITYNGCTSVT-VKNAFCEGKCGSASSYSI--QDVQHSCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77


                    ..
gi 1813372009  2807 SP 2808
Cdd:smart00041   78 EP 79
VWA pfam00092
von Willebrand factor type A domain;
1277-1452 1.95e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.40  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAS 1356
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1357 TSEVLKYTLFQIFSKI--DRPEASRITLLL----MASQEPQRMSRNfvryvqgLKKKKVIVIPVGIGPHANlKQIRLIEK 1430
Cdd:pfam00092   81 TGKALKYALENLFSSAagARPGAPKVVVLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 1813372009 1431 QAPENKAFVLSSVDELEQQRDE 1452
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1060-1126 1.98e-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: 1.98e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1813372009 1060 CRILT-SDVFQDCNKLVDPEPYLDVCIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-KVVTWRTATLC 1126
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 224-291 3.45e-17

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 77.81  E-value: 3.45e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009  224 QCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSAC 291
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1497-1608 1.79e-16

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 79.71  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGnRT 1576
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1813372009 1577 NTGLALRYLSDHSFLVSQGDREQAPNLVYMVT 1608
Cdd:cd01469     80 NTATAIQYVVTELFSESNGARKDATKVLVVIT 111
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1276-1438 3.28e-16

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 78.38  E-value: 3.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVA 1355
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1356 STSEVLKYTLfQIFSKIDRPEASRItLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPEN 1435
Cdd:cd00198     81 NIGAALRLAL-ELLKSAKRPNARRV-IILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGG 158


                   ...
gi 1813372009 1436 KAF 1438
Cdd:cd00198    159 AVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1690-1831 2.67e-15

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: 76.24  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1690 LDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPSQ 1769
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1813372009 1770 IGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVDSVDAAADAARSNR--VTVFPIGIGDRY 1831
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAERegIIRYAIGVGGHF 144
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1691-1850 4.48e-15

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: 75.34  E-value: 4.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPSQI 1770
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1771 GDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVDSVDAAADAARSNRVTVFPIGIGDRyDAAQLRILAGPAGDSNVVK 1850
Cdd:cd01472     82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNA-DEEELKQIASDPKELYVFN 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1497-1638 6.06e-14

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: 72.80  E-value: 6.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEAD-FNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFS-----EAQSKGDILQRVREIRY 1570
Cdd:cd01471      1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSspnstNKDLALNAIRALLSLYY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009 1571 QGGNrTNTGLALRYLSDHSFLvSQGDREQAPNLVYMVT-GNPASD--------EIKRLPGDIQVvpIGVGPNANVQE 1638
Cdd:cd01471     81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEE 153
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1689-1874 7.26e-14

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: 73.57  E-value: 7.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1689 PLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPS 1768
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1769 QIGDALGFAVRYLTSEMHGARPGA---SKAVVILVTDVSVDSVDAAADAARSNRVTVFPIGIGdRYDAAQLRILAGPAGD 1845
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGServPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVG-RADEEELREIASEPLA 160

                          170       180
                   ....*....|....*....|....*....
gi 1813372009 1846 SNVVklqRIEDLPTMVTLGNSFLHKLCSG 1874
Cdd:cd01475    161 DHVF---YVEDFSTIEELTKKFQGKICVV 186
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1691-1848 1.21e-13

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: 71.16  E-value: 1.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPSQI 1770
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 1771 GDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVDSVDAAADAARSNRVTVFPIGIGDrYDAAQLRILAGPAGDSNV 1848
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKD-ADESELKMIASKPSETHV 158
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1497-1643 2.26e-13

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: 70.12  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEAdFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVT--VEYPFSEAQSKGDILQRVREIRYQGGN 1574
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 1575 rTNTGLALRYLSDHsFLVSQGDREQAPNLVYMVTG-----NP--ASDEIKRLPGdIQVVPIGVGPNANV--QELERIG 1643
Cdd:cd01476     80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDgrshdDPekQARILRAVPN-IETFAVGTGDPGTVdtEELHSIT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2135-2200 3.97e-13

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: 66.60  E-value: 3.97e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009  2135 DSSHCQVLLLPL--FAECHKVLAPATFYAICQQDSC----HQEQVCEVIASYAHLCRTNGVCV-DWRTPDFCA 2200
Cdd:smart00832    4 ACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCacggDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 652-707 4.27e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 65.80  E-value: 4.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009  652 CPKGQVYLQCGTPCNLTCRSLSYPdEECNEACLEGCFCPPGLYMDERGDCVPKAQC 707
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1690-1799 1.08e-12

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: 68.19  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1690 LDVILLLDGSSSFPASYFDEMKsFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNV--VPEKAHLLSLVDVMQREGGP 1767
Cdd:cd01476      1 LDLLFVLDSSGSVRGKFEKYKK-YIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLpkHNDGEELLEKVDNLRFIGGT 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1813372009 1768 SQIGDALGFAVRYLTsEMHGARPGASKAVVIL 1799
Cdd:cd01476     80 TATGAAIEVALQQLD-PSEGRREGIPKVVVVL 110
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2138-2199 1.36e-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: 65.09  E-value: 1.36e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1813372009 2138 HCQVLLL-PLFAECHKVLAPATFYAICQQDSCH----QEQVCEVIASYAHLCRTNGVCV-DWRTPDFC 2199
Cdd:pfam08742    1 KCGLLSDsGPFAPCHSVVDPEPYFEACVYDMCScggdDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 652-707 3.85e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 63.18  E-value: 3.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009  652 CPKGQVYLQCGTPCNLTCRSLSYPDEeCNEACLEGCFCPPGLYMDERGDCVPKAQC 707
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 295-348 7.26e-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: 62.33  E-value: 7.26e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  295 CPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDE-GLCVESTEC 348
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 295-348 1.16e-11

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 62.02  E-value: 1.16e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009  295 CPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLD-EGLCVESTEC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1277-1425 9.66e-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: 62.63  E-value: 9.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAs 1356
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009 1357 TSEVLKYTLFQIFSKIDRPEAS--RITLLLMASQEPQRMSRNFVRyvqgLKKKKVIVIPVGIGPH--ANLKQI 1425
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQDDVEEPAVE----LKQAGIEVFAVGVKNAdeEELKQI 149
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1276-1380 2.91e-09

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 59.71  E-value: 2.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAgSQVA 1355
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                           90       100
                   ....*....|....*....|....*..
gi 1813372009 1356 STSEVLKYTLFQIFSKID--RPEASRI 1380
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEgaRPGSERV 108
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 579-648 4.86e-09

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 55.04  E-value: 4.86e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009   579 FSEEACAVLTSP--TFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRV-AWREPGRC 648
Cdd:smart00832    3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFC 75
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1277-1380 1.13e-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: 56.95  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVAS 1356
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                           90       100
                   ....*....|....*....|....
gi 1813372009 1357 TSEVLKYTLFQIFSKidrPEASRI 1380
Cdd:cd01481     82 TGSALDYVVKNLFTK---SAGSRI 102
VWC smart00214
von Willebrand factor (vWF) type C domain;
2261-2321 4.50e-08

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 51.75  E-value: 4.50e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1813372009  2261 DGVQHQFLEAWVPDhqPCQICTCLSGRKVNCTTQPCPTAKAptcglCEVARLRQNADQCCP 2321
Cdd:smart00214    4 NGRVYNDGETWKPD--PCQICTCLDGTTVLCDPVECPPPPD-----CPNPERVKPPGECCP 57
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1691-1867 5.52e-08

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 54.64  E-value: 5.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGG-PSQ 1769
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1770 IGDALGFAVRYLTSEMHGAR--PGASKAVVILVTDVSVDSVDAAADAARSNRvtVFPIGIGDRydaaqlrilagpagDSN 1847
Cdd:cd01481     82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAG--IVPFAIGAR--------------NAD 145

                          170       180
                   ....*....|....*....|
gi 1813372009 1848 VVKLQRIEDLPTMVTLGNSF 1867
Cdd:cd01481    146 LAELQQIAFDPSFVFQVSDF 165
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1146-1196 5.83e-08

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 51.16  E-value: 5.83e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1813372009 1146 YNSCAPACQVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDPEDC 1196
Cdd:cd19941      7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55
VWA_2 pfam13519
von Willebrand factor type A domain;
1692-1799 9.06e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 52.29  E-value: 9.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1692 VILLLDGSSS-----FPASYFDEMKSFAKAFISKANIgprlTQVSVLQYGSITTIDVPWNvvPEKAHLLSLVDVMQREGG 1766
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1813372009 1767 PSQIGDALgfavRYLTSEMHGARPGASKAVVIL 1799
Cdd:pfam13519   75 GTNLAAAL----QLARAALKHRRKNQPRRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1497-1584 1.09e-07

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 54.31  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRM------DVGQDSIHVTVLQYSYMVTVEYPF-SEAQSKGDILQRVREIR 1569
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLE 82

                           90
                   ....*....|....*
gi 1813372009 1570 YQGGNrTNTGLALRY 1584
Cdd:cd01480     83 YIGGG-TFTDCALKY 96
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2582-2644 1.14e-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: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2582 CMLNGTVIGPGKTVMIDVCTTCRCMVqvgvisgFKLECRKTTCNP--CPLGYkEENNTGECCGRC 2644
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
2582-2644 1.81e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 50.21  E-value: 1.81e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009  2582 CMLNGTVIGPGKTVMIDVCTTCRCMVQVgVISGFKLECRKTTcnPCPLGYKEENNtGECCGRC 2644
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGT-TVLCDPVECPPPP--DCPNPERVKPP-GECCPRC 59
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 584-648 2.36e-07

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: 50.07  E-value: 2.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  584 CAVLT-SPTFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRVA-WREPGRC 648
Cdd:pfam08742    2 CGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2260-2322 3.13e-07

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 3.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009 2260 EDGVQHQFLEAWVPDhqPCQICTCLSGrKVNCTTQPCPTAKaptcglCEVARLRQNADQCCPE 2322
Cdd:pfam00093    3 QNGVVYENGETWKPD--LCTICTCDDG-KVLCDKIICPPLD------CPNPRLEIPPGECCPV 56
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1277-1425 3.43e-07

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 52.29  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1277 DLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQvAS 1356
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 1357 TSEVLKYTLFQIFSKID--RPEASRITLLLM--ASQEpqrmsrNFVRYVQGLKKKKVIVIPVGIGPH--ANLKQI 1425
Cdd:cd01482     81 TGKALTHVREKNFTPDAgaRPGVPKVVILITdgKSQD------DVELPARVLRNLGVNVFAVGVKDAdeSELKMI 149
VWC smart00214
von Willebrand factor (vWF) type C domain;
2431-2494 5.98e-07

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 48.67  E-value: 5.98e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009  2431 CVHRSTIYPVGQFWEEG-CDVCTCTDMEdavmglrVAQCSQKPCEDS--CRSGFTyVLHEGECCGRC 2494
Cdd:smart00214    1 CVHNGRVYNDGETWKPDpCQICTCLDGT-------TVLCDPVECPPPpdCPNPER-VKPPGECCPRC 59
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1276-1446 7.50e-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: 51.59  E-value: 7.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSqVA 1355
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1356 STSEVLKYTLFQIF--SKIDRPEASRITLLLMASQE----------PQRMSRNFVRYVqglkkkkvivipVGIGPHAN-- 1421
Cdd:cd01469     80 NTATAIQYVVTELFseSNGARKDATKVLVVITDGEShddpllkdviPQAEREGIIRYA------------IGVGGHFQre 147

                          170       180
                   ....*....|....*....|....*..
gi 1813372009 1422 --LKQIRLIEKQAPENKAFVLSSVDEL 1446
Cdd:cd01469    148 nsREELKTIASKPPEEHFFNVTDFAAL 174
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1146-1196 1.09e-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: 47.77  E-value: 1.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1813372009 1146 YNSCAPACQVTCQHPE-PLACPVQCVEGChaHCPPGKILDElLQTCVDPEDC 1196
Cdd:pfam01826    7 YSECGSACPPTCANLSpPDVCPEPCVEGC--VCPPGFVRNS-GGKCVPPSDC 55
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1276-1428 1.37e-06

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 51.23  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEA-EFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKD--RKRPSELRRIASQVKYAGS 1352
Cdd:cd01471      1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLSLYY 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1813372009 1353 QVAST--SEVLKYTLFQIFS-KIDRPEASRItLLLMASQEPQRMSRNfVRYVQGLKKKKVIVIPVGIGPHANLKQIRLI 1428
Cdd:cd01471     81 PNGSTntTSALLVVEKHLFDtRGNRENAPQL-VIIMTDGIPDSKFRT-LKEARKLRERGVIIAVLGVGQGVNHEENRSL 157
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2431-2494 1.60e-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: 47.42  E-value: 1.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1813372009 2431 CVHRSTIYPVGQFWEEG-CDVCTCTDmedavmglRVAQCSQKPCED-SCRSGFtYVLHEGECCGRC 2494
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDD--------GKVLCDKIICPPlDCPNPR-LEIPPGECCPVC 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1611-1862 2.83e-05

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: 48.40  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1611 PASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRCCSGEGLQIPTLSPAPDCSQPL 1690
Cdd:COG1240     14 ALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPA-SYFDEMKSFAKAFISKanIGPRlTQVSVLQYGsiTTIDVPWNVVPEKAHLLSLVDVMQREGGpSQ 1769
Cdd:COG1240     94 DVVLVVDASGSMAAeNRLEAAKGALLDFLDD--YRPR-DRVGLVAFG--GEAEVLLPLTRDREALKRALDELPPGGG-TP 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1770 IGDALGFAVRYLTSEmhgaRPGASKaVVILVT----DVSVDSVDAAADAARSNRVTVFPIGIG-DRYDAAQLRILAGpAG 1844
Cdd:COG1240    168 LGDALALALELLKRA----DPARRK-VIVLLTdgrdNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIAE-AT 241

                          250
                   ....*....|....*...
gi 1813372009 1845 DSNVVKLQRIEDLPTMVT 1862
Cdd:COG1240    242 GGRYFRADDLSELAAIYR 259
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1689-1801 3.55e-05

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: 46.99  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1689 PLDVILLLDGSSSFPASYFDEMKSFAKAFIS------KANIGPRLTQVSVLQY-GSITTIDVPWNVVPEKAHLLSLVDVM 1761
Cdd:cd01480      2 PVDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1813372009 1762 QREGGPSQIGDALGFAvrylTSEMHGARPGASKAVVILVT 1801
Cdd:cd01480     82 EYIGGGTFTDCALKYA----TEQLLEGSHQKENKFLLVIT 117
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2203-2254 9.98e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.30  E-value: 9.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2203 CPPSLVYNHCEHGCPRHCD--GNVSSCGDHPSEGCFCPPDKVM-LEGSCVPEEAC 2254
Cdd:cd19941      1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1497-1643 2.37e-04

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 44.59  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1497 LDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYS----YMVTVEYPFSeaQSKGDILQRVREIRYQG 1572
Cdd:cd01470      1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYAsdpkEIVSIRDFNS--NDADDVIKRLEDFNYDD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1573 -GNR--TNTGLALRYLSDHSFLVSQGDRE---QAPNLVYMVT-------GNP--ASDEIKRLPG-------------DIQ 1624
Cdd:cd01470     79 hGDKtgTNTAAALKKVYERMALEKVRNKEafnETRHVIILFTdgksnmgGSPlpTVDKIKNLVYknnksdnpredylDVY 158

                          170
                   ....*....|....*....
gi 1813372009 1625 VvpIGVGPNANVQELERIG 1643
Cdd:cd01470    159 V--FGVGDDVNKEELNDLA 175
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1276-1392 6.03e-04

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: 43.53  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1276 LDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLR------ISQKWVRVAVVEY-HDGSHAYIGLKDRKRPSELRRIASQVK 1348
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1813372009 1349 YAGsQVASTSEVLKYTLFQIF--SKID-----------RPEASRITLLLMASQEPQR 1392
Cdd:cd01480     83 YIG-GGTFTDCALKYATEQLLegSHQKenkfllvitdgHSDGSPDGGIEKAVNEADH 138
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2203-2254 6.73e-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: 40.06  E-value: 6.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1813372009 2203 CPPSLVYNHCEHGCPRHCD--GNVSSCGDHPSEGCFCPPDKVML-EGSCVPEEAC 2254
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAnlSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1498-1620 1.47e-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: 42.30  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1498 DVAFVLEGSDKIGeaDFNRSKEFM---EEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFS--EAQSKGDILQRVREIR--Y 1570
Cdd:cd01473      2 DLTLILDESASIG--YSNWRKDVIpftEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeERYDKNELLKKINDLKnsY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1813372009 1571 QGGNRTNTGLALRYlSDHSFLVSQGDREQAPNLVYMVT-GNPASDEIKRLP 1620
Cdd:cd01473     80 RSGGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTdGNDTSASKKELQ 129
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
350-394 1.92e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 39.08  E-value: 1.92e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1813372009   350 CVHSGKRYPPGTSLSRDCNTCICRNSQWICSNEEC-PGECLVTGQS 394
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCgPKPCLLHNLS 46
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1691-1840 2.30e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 42.36  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1691 DVILLLDGSSSFPASYFDEMKSFAKAFISKANigPRLtQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGpSQI 1770
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR--PNR-RFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TDI 195

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1813372009 1771 GDALGFAVRYLTsemhgaRPGASKAVVILVT---DVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILA 1840
Cdd:COG2425    196 APALRAALELLE------EPDYRNADIVLITdgeAGVSPEELLREVRAKESGVRLFTVAIGDAGNPGLLEALA 262
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 788-827 2.59e-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: 38.07  E-value: 2.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1813372009  788 CTKTCQNYDL--ECmSMGCVSGCLCPPGMVRHEN-RCVALERC 827
Cdd:cd19941     14 CPPTCANPNAppPC-TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1690-1799 5.61e-03

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 40.45  E-value: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1813372009 1690 LDVILLLDGSSSF-PASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPS 1768
Cdd:cd01471      1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYY 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1813372009 1769 QIG-----DALGfAVRYLTSEMHGARPGASKAVVIL 1799
Cdd:cd01471     81 PNGstnttSALL-VVEKHLFDTRGNRENAPQLVIIM 115
 
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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