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 345842432    556 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 633
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842432    634 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 711
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158

                    ....*
gi 345842432    712 LTPAG 716
Cdd:smart00216  159 RTPDG 163

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842432 2105 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2181
Cdd:cd00057    31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 345842432 2182 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2225
Cdd:cd00057   106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143

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 345842432   1202 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1275
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 345842432   3236 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3288
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345842432   396 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 468
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 345842432   2968 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3019
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

Thrombospondin type 1 domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 345842432  2815 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2863
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 345842432 1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1453
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 345842432   3629 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3673
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 345842432 1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1414
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35

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 345842432  472 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 527
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 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 345842432  4052 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4107
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 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 345842432  4814 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4868
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 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 345842432  3071 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3123
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 345842432  3386 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3432
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42

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 345842432 2613 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2656
Cdd:cd19941    11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 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 345842432 4416 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4471
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 345842432 2388 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2422
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 345842432 2233 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2267
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 345842432 1455 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1489
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

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 345842432  3510 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3566
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 345842432   4611 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4659
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53

von Willebrand factor (vWF) type C domain;

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 345842432   2928 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 2975
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 345842432 2867 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2926
Cdd:cd19941     1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 345842432   4361 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4412
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 345842432  4980 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5035
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDDGKVLCDKiICPPLDCPNPRLE-IPPGECCPVC 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 345842432  4920 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 4978
Cdd:pfam01826    1 CPANEVYSECG-SACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 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 345842432   1006 WHCTGQRCSGWCQASGAPHYVTFDGLVFTFPGACEYLLVREA--GGRFSVSVQNLPCGaSGLTCTKALVVRLDSTVVHML 1083
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842432   1084 RGQ-AVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGLTL-LWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLR 1161
Cdd:smart00216   80 DDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQvTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159

                    ....
gi 345842432   1162 SRQG 1165
Cdd:smart00216  160 TPDG 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 345842432   567 CAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACD---TGSCLHALSVFLGNTHIQLRYSGAVLVD 642
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGT--CTYVLAKDcSEEPDFSFSVTNKNCNggaSGVCLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345842432   643 GEDVDLP-WIGVEGFNISWASSTFLLLHwPGAWVLW-GVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDFLTPAG 716
Cdd:pfam00094   79 GQKVSLPyKSDGGEVEILGSGFVVVDLS-PGVGLQVdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153

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 345842432   195 CATWSGFHYQTFDGHHYHFLGQCTYLLA----GAMDSTWAVHLRPsVHCPQHRHCW-LVQVVMGPEEVLIQDG-EVSVKG 268
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAkdcsEEPDFSFSVTNKN-CNGGASGVCLkSVTVIVGDLEITLQKGgTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345842432   269 QPVPVgePQLLHGMSLQ--WQGDWLV-LSGGLGVVVRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 341
Cdd:pfam00094   80 QKVSL--PYKSDGGEVEilGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153

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 345842432    754 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 826
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 345842432   2539 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2591
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842432  2114 WH----TQPLYLQLDLRRPRNLTGIIVQ-RAGSSAAYVSTLSLQFSSDNLQWHNYVNSLSSTlsppkpspeSSNHMAPEV 2188
Cdd:pfam00754   26 WSawsgDDPQWIQVDLGKPKKITGVVTQgRQDGSNGYVTSYKIEYSLDGENWTTVKDEKIPG---------NNDNNTPVT 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 345842432  2189 WTFDQMVQARYIRVWPhsghLRDNNQHDIFLWVEL 2223
Cdd:pfam00754   97 NTFDPPIKARYVRIVP----TSWNGGNGIALRAEL 127

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 345842432   3236 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3288
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 345842432   4246 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4297
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52