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).

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 830025609  1222 VCEVAGRRLASGKKVTLNPGDPEHCQICHCDGVNLTCEACREPGGLEVPPTEASVSPTTPYVEDTPEPPLHDFYCSKLL 1300
Cdd:pfam16164    1 VCEVAGRRLPSGKKITLNRSDPEHCQICHCDGVNLTCEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1516 LDVAFVLEGSDKIGEADFNRSREFLEEVIQRMDVGQDGIHVAVLQYSYAVTVEYPFSEVQSKGDVLQRVREIRFRGGNGT 1595
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 830025609 1596 NTGLALQYLSEHSFSASlGDREQAPNLVYMVTG---------SPASDEIRRLpgDIQVVPIGVGPrASVQELERIGWP 1664
Cdd:cd01450    81 NTGKALQYALEQLFSES-NARENVPKVIIVLTDgrsddggdpKEAAAKLKDE--GIKVFVVGVGP-ADEEELREIASC 154

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1969 CTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHKGACSSGEEQSCMKSIEVKHSGLSVELHDNMEVTVNGR 2046
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830025609  2047 LVSVPYEGGNMEVSIYGAVMHELRFSrLGHILTFTPQNNEFQLQLSPKTFASKMYGLCGICDENGANDFMLRDGT 2121
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1300 LDLVFLLDGSSRLSEAEFGVLKAFVVGMMERLHISQKRVRVAVVEYHDGSHSYIGLTDRKRPSELRRITSQVRYAGSQVA 1379
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1380 STSEVLKYTLFQIFSKI-DRPEASHITLLLTASQepPKMARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIRLIEKQAPD 1458
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157

                  ....
gi 830025609 1459 NKAF 1462
Cdd:cd01450   158 RHVF 161

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.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 830025609    246 WEQCQLLKSTS-AFARCHPAVDPEPFVALCEKTLCTCSQGPECLCPAFLEYARACAQEGVVPYGWTHHSMCR 316
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 830025609  319 CPAGMEYKECVSPCTRTCQSLHINEACQEQCVDGCSCPEGQLLDE-GRCVESAEC 372
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 830025609  676 CPQGQVYLQCGTPCNLTCRSLSYPdEECNEVCLEGCFCPPGLYLDERGDCVPKARC 731
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 830025609 1170 YNSCAPACPVTCQHPE-PLACPVQCVEGChaHCPPGKVLDElLQTCINPEDC 1220
Cdd:cd19941     7 YSECGSACPPTCANPNaPPPCTKQCVEGC--FCPEGYVRNS-GGKCVPPSQC 55

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 830025609 2222 CPPSLVYNHCERGCPRHCD--GNASSCGEHPSEGCFCPPGQVLLEGG-CVPEEAC 2273
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnpNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830025609  2601 CMLNGTTIGPGKSVMVDVCTTCRCAVqggptpgFKLECRRSTCEA--CPVGYkEEKNPGECCGRC 2663
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDD-------GKVLCDKIICPPldCPNPR-LEIPPGECCPVC 57

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 830025609  812 CAKTCQNYDL--ECMSVgCVSGCLCPPGMVRHEN-RCVALERC 851
Cdd:cd19941    14 CPPTCANPNAppPCTKQ-CVEGCFCPEGYVRNSGgKCVPPSQC 55

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609    401 WICSNEECPGECLVTGQSHFKSFDNRHFTFSGICQYLLARDCEDH-SFSIVIETVQCadDPDAVCTRSVTVRLPALhnSL 479
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC--GGGATCLKSVKVELNGD--EI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609    480 VKLKHGGGVAMDGQDVQVPLLQGDLRIQHTVMGS---VRLSYGeDLEMDWDGRGRLLVKLSPAYAGKTCGLCGNYNGDQG 556
Cdd:smart00216   77 ELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGylvVITSLG-LIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155

                    ....*...
gi 830025609    557 DDFRTPAG 564
Cdd:smart00216  156 DDFRTPDG 163

von Willebrand factor type A domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1710 DVVLLLDGSSGSPASYFDEMKSFAKAFISKANIGPHLTQVAVLQYGSVATPDVPWAVAQDKAYLLSLVDSM-QRWGGHSQ 1788
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1789 IGNGLDVAVRYITSEVHGARPGVSKAIVVLVVGVSTDP-VQAAADAARSNRVTVFPIGIGDHYDaAQLRVLAGPGASSNV 1867
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADD-EELRKIASEPGEGHV 159

                          170
                   ....*....|....
gi 830025609  1868 VKLQRIEDLPAMVT 1881
Cdd:pfam00092  160 FTVSDFEALEDLQD 173

von Willebrand factor type A domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1517 DVAFVLEGSDKIGEADFNRSREFLEEVIQRMDVGQDGIHVAVLQYSYAVTVEYPFSEVQSKGDVLQRVREIRFRGGNGTN 1596
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1597 TGLALQYLSEHSFSASLGDREQAPNLVYMVTG--------SPASDEIRRlpGDIQVVPIGVGPrASVQELERIGWPNAP- 1667
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDgrsqdgdpEEVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEg 157

                          170
                   ....*....|..
gi 830025609  1668 --ILIQDFELLP 1677
Cdd:pfam00092  158 hvFTVSDFEALE 169

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1969 CTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQ--DLEVILHKGACSSGEEQSCMKSIEVKHSGLSVELHDNMEVTVNGR 2046
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830025609  2047 LVSVPYEGGNMEVSIYGAVMHELRFSrLGHILTFTPQNNEFQLQLSPKTFASKMYGLCGICDENGANDFMLRDGT 2121
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609   1957 ETCGCrWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQN--KEQDLEVILHKGACSSGEeqSCMKSIEVKHSGLSVE 2034
Cdd:smart00216    1 WCCTQ-EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcsSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609   2035 LHD-NMEVTVNGRLVSVPYEGGNMEVSIYGAVMHELRFSRLGHI-LTFTPQNNeFQLQLSPKtFASKMYGLCGICDENGA 2112
Cdd:smart00216   78 LKDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL-LSVQLPSK-YRGKTCGLCGNFDGEPE 155

                    ....*...
gi 830025609   2113 NDFMLRDG 2120
Cdd:smart00216  156 DDFRTPDG 163

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609    59 CSLFGDDFVSTFDGSMYSFAGHCSYFLAGDCEGHS-FSLLGDFLNGKRVGLSVYLGE------FFDIHLFVNGTVLQGDQ 131
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdFSFSVTNKNCNGGASGVCLKSvtvivgDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 830025609   132 SISMPYASKGLYLETEAGYYKLSSEAHGFVARIDGSGNFQ--VLLSHRHFNKTCGLCGNFNIFAEDDFRTQEGT 203
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQlfVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1709 LDVVLLLDGSSGSPASYFDEMKSFAKAFISKANIGPHLTQVAVLQYGSVATPDVPWAVAQDKAYLLSLVDSMQRWGG-HS 1787
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1788 QIGNGLDVAVRYITSEvHGARPGVSKAIVVLVVGVSTD--PVQAAADAARSNRVTVFPIGIGDHyDAAQLRVLAGPGASS 1865
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPA-DEEELREIASCPSER 158

                  ...
gi 830025609 1866 NVV 1868
Cdd:cd01450   159 HVF 161

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1300 LDLVFLLDGSSRLSEAEFGVLKAFVVGMMERLHISQKRVRVAVVEYHDGSHSYIGLTDRKRPSELRRITSQVRYAGSQVA 1379
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1380 STSEVLKYTLFQIFSKI-DRPEASHITLLLTASQepPKMARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIRLIEKQAPD 1458
Cdd:cd01450    81 NTGKALQYALEQLFSESnARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157

                  ....
gi 830025609 1459 NKAF 1462
Cdd:cd01450   158 RHVF 161

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.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 830025609   1077 QTMVDSSCRILTSD--VFRDCNRLVDPEPYLDVCIYDTCSCEsiGDCACFCDTIAAYAHVCAQHG-QVVTWRTATLCP 1151
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACG--GDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76

von Willebrand factor type A domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1301 DLVFLLDGSSRLSEAEFGVLKAFVVGMMERLHISQKRVRVAVVEYHDGSHSYIGLTDRKRPSELRRITSQVRYAGSQVAS 1380
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609  1381 TSEVLKYTLFQIFSKI--DRPEASHITLLLTA----SQEPPKMARNlvryvqgLKKKKVIVIPVGIGPhASLKQIRLIEK 1454
Cdd:pfam00092   81 TGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKIAS 152

                          170
                   ....*....|....*...
gi 830025609  1455 QAPDNKAFVLSSVDELEQ 1472
Cdd:pfam00092  153 EPGEGHVFTVSDFEALED 170

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 830025609   248 QCQLLKSTSAFARCHPAVDPEPFVALCEKTLCTCSQGPECLCPAFLEYARACAQEGVVPYGWTHHSMC 315
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 830025609  319 CPAGMEYKECVSPCTRTCQSLHINEACQEQCVDGCSCPEGQLLDE-GRCVESAEC 372
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 830025609  676 CPQGQVYLQCGTPCNLTCRSLSYPdEECNEVCLEGCFCPPGLYLDERGDCVPKARC 731
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAP-PPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 830025609   319 CPAGMEYKECVSPCTRTCQSLHINEACQEQCVDGCSCPEGQLLD-EGRCVESAEC 372
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1630 PASDEIRRLPGDIQVVPIGVGPRASVQELERIGWPNAPILIQDFELLPREAPELVLKGCCSGEGLQLPTLSPVSDCSQPL 1709
Cdd:COG1240    14 ALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830025609 1710 DVVLLLDgSSGSPASY--FDEMKSFAKAFISKANIGphlTQVAVLQYGSVATPDVPwaVAQDKAYLLSLVDSMQrWGGHS 1787
Cdd:COG1240    94 DVVLVVD-ASGSMAAEnrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLP--LTRDREALKRALDELP-PGGGT 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 830025609 1788 QIGNGLDVAVRYITSEvhgaRPGVSKAIVVL---VVGVSTDPVQAAADAARSNRVTVFPIGIG-DHYDAAQLRVLA 1859
Cdd:COG1240   167 PLGDALALALELLKRA----DPARRKVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLREIA 238