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 190609994   1013 WHCSQSSCAGVCVATGDPHYVTFDGRYYSFLGDCQYVLVRERS--GLFSVTAENVPCGStGVTCTKSVTLSLGNTVIHLL 1090
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSsePTFSVLLKNVPCGG-GATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190609994   1091 R-GKAVTVNGMPVNLPKSYSGSGLTLERAGMFVTLSSRLGV-SLLWDGGMRVYVRLAAFLHGQVGGLCGNFDGDTENDFT 1168
Cdd:smart00216   80 DdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159

                    ....
gi 190609994   1169 TRQG 1172
Cdd:smart00216  160 TPDG 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 190609994 2086 STQSPYVQIDLLRFHNITGVLTQGGGVFGT--FVSSFYLQFSQDGRRWYTYKElvaqaQPRAKIFLGNHDDRGVAEIHLD 2163
Cdd:cd00057    42 NDPPQWLQVDLGKTRRVTGIQTQGRKGGGSseWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNSDGSTPVTNDFP 116

                          90       100
                  ....*....|....*....|....*..
gi 190609994 2164 RMVSARFVRLLPHDFQNGIYLRLEIMG 2190
Cdd:cd00057   117 PPIVARYIRILPTTWNGNISLRLELYG 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 190609994    750 YAEAVCSVIHTA--VFQACHDAVEREHYFRLCLLEVCGCAPERLCHCTVITAYAQHCAQEGVAVH-WRNQTFCP 820
Cdd:smart00832    3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 190609994   4188 WTPWSVWSDCSVTCGHGTQIRTHACINPPPRNNGSDCLGPERETRDCPTLPC 4239
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 190609994   3941 WSRWSPWSRCDKRCGGGRSIRTRSCSSPPPKNGGKKCQGEKNHVKPCNTKPCD 3993
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 190609994   3182 WGQWSNWTACTKSCGGGIQTRKRDCDNPIPEQEGRFCEGLGTEVLSCNTNHCP 3234
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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 190609994  461 CPKGQVYSDCVSSCPPNCASPQPPGPaaalgqCREECVGGCECPPGLYL-YQGNCLKRDDC 520
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP------CTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55

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 190609994   391 CHRLLEN-PFIHCHLRLDPAAYVDACLYLFCSLPakERESAVCDTFANYARECAQQHVVI-SWRTASLC 457
Cdd:pfam08742    2 CGLLSDSgPFAPCHSVVDPEPYFEACVYDMCSCG--GDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 190609994   2929 WSSWTQWSACSRTCDVGVRRRYRSGTNPPAAFGGQPCKGDRVGIDTCSIEPC 2980
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

sporozoite surface protein 2 (SSP2); Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190609994 4690 PWRPWNPCSVSCGNGTRSRTRlcqateggPS----CThTEQTESCEMPPCPVGQMFSECSSSCPHICEDLWPHT 4759
Cdd:PTZ00441  242 PWDEWTPCSVTCGKGTHSRSR--------PIlhegCT-THMVEECEEEECPVEPEPLPVPAPVPPTPEDDNPRP 306

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 190609994  823 CSGGQVYQECGRACGDSCSDGLSCGDATDgtglrTCVPGCQCPPGLMQDHRGQCVPISMC 882
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 190609994 2197 CKEKEFRCENGRCVPAGSlgvVCDGVDDCGDGSDEKYC 2234
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW---VCDGEDDCGDGSDEENC 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 190609994 1559 CRSYEFSCDSGaQCVPQAWHCDGETDCLDGSDERQC 1594
Cdd:cd00112     1 CPPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 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 190609994 1428 CDKGEFLCSGGRCILYLHRCDGHDDCGDLSDERGC 1462
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 190609994  3997 CPPGQEFVSCAKQCPQKCADLQQGIECQEsgECQPGCRCPEGQ-LQQDGLCVQMWQC 4052
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGFvRNSGGKCVPPSDC 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 190609994 2344 CVEGQFACWSFGCVDSKQVCDGKQDCLDGSDEERC 2378
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        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190609994   2707 WSKWTSWSECSKTCfhhvnDVGFRRRFRSCNhtLAAFNNETSTCVGDSEEQEPCNTVHCP 2766
Cdd:smart00209    1 WSEWSEWSPCSVTC-----GGGVQTRTRSCC--SPPPQNGGGPCTGEDVETRACNEQPCP 53

Thrombospondin type 1 domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 190609994  4245 PWSPWSSCSQSCGAGSVSRRRMCLCEAAGDETCPAeieaerNRQENQLCYKQPC 4298
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTG------DDIETQACKMDKC 49

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
                   ....*....|....*....|....*....|....*....|....*..
gi 190609994  4600 CANQCPRSCADLWEHVQCLqGSCHAGCRCPEGQLLQ-DGHCVPVKDC 4645
Cdd:pfam01826   10 CGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 190609994   2986 PWTPWSECSVTCGGGYRSRTRGPIRVH---------GTAQQFSACNLQPC 3026
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpctGEDVETRACNEQPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 190609994   3883 WMEWGSWSSCSRSCGVGQQQRIRTFVSP--GTNGSWCDnilEGNLENRFCNIKPC 3935
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppQNGGGPCT---GEDVETRACNEQPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 190609994   1884 WSAWSDWGECLGPCGVqSIQWSFRSPNNPTKRGEGKTCRGIYRKARRCQTEPCE 1937
Cdd:smart00209    1 WSEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 190609994   3587 WLPWSQWSMCSVSCGGGQQHRSRICSSPPCSSL-------SRQSKTCNTHVC 3631
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggpctgeDVETRACNEQPC 52

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. 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. Mutations in the LDL receptor gene cause familial hypercholesterolemia.

                            10        20        30
                    ....*....|....*....|....*....|...
gi 190609994   1503 TCAP-QFACSDSTCISTNMLCDGATDCPGGEDE 1534
Cdd:smart00192    1 TCPPgEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 190609994   1939 CEFQGRSHPVGDRWTSDRCQLCYCLSNLTVQCAPFCPHAVSGCPQGQTLVPGekDRCC 1996
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTTVLCDPVECPPPPDCPNPERVKPP--GECC 56

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 190609994 2826 CPQGMMYMtaaECeaqGGACPRVCLDMTVSEVqCATSCYDGCYCAPGFYL-LNRSCVPLSQC 2886
Cdd:cd19941     1 CPPNEVYS---EC---GSACPPTCANPNAPPP-CTKQCVEGCFCPEGYVRnSGGKCVPPSQC 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 190609994   1013 WHCSQSSCAGVCVATGDPHYVTFDGRYYSFLGDCQYVLVRERS--GLFSVTAENVPCGStGVTCTKSVTLSLGNTVIHLL 1090
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSsePTFSVLLKNVPCGG-GATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190609994   1091 R-GKAVTVNGMPVNLPKSYSGSGLTLERAGMFVTLSSRLGV-SLLWDGGMRVYVRLAAFLHGQVGGLCGNFDGDTENDFT 1168
Cdd:smart00216   80 DdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159

                    ....
gi 190609994   1169 TRQG 1172
Cdd:smart00216  160 TPDG 163

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 190609994    194 SATCMSWGGSHYRSFDRKHFHFQGGCTYLLA--SSIDGTWAVYIRTV-CDGGGGCSKALKMMFGLDLVSVHHRN--LTLN 268
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAqdCSSEPTFSVLLKNVpCGGGATCLKSVKVELNGDEIELKDDNgkVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190609994    269 NLLVPNGEAIFQNGVTVYWLGDFVFVESGLGV-RVKFDLTSTVYVTVTAEHKSATRGLCGVYDGNADDDFTT 339
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRT 160

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 190609994 2086 STQSPYVQIDLLRFHNITGVLTQGGGVFGT--FVSSFYLQFSQDGRRWYTYKElvaqaQPRAKIFLGNHDDRGVAEIHLD 2163
Cdd:cd00057    42 NDPPQWLQVDLGKTRRVTGIQTQGRKGGGSseWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNSDGSTPVTNDFP 116

                          90       100
                  ....*....|....*....|....*..
gi 190609994 2164 RMVSARFVRLLPHDFQNGIYLRLEIMG 2190
Cdd:cd00057   117 PPIVARYIRILPTTWNGNISLRLELYG 143

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 190609994   2085 SSTQSPYVQIDLLRFHNITGVLTQGGGVFGTFVSSFYLqFSQDGRRWYTYKElvaqaqPRAKIFLGNHDDRGVAEIHLDR 2164
Cdd:smart00231   40 KNDLPPWIQVDLGRLRTVTGVITGRRHGNGDWVTYKLE-YSDDGVNWTTYKD------GNSKVFPGNSDAGTVVLNDFPP 112

                            90       100
                    ....*....|....*....|....*..
gi 190609994   2165 MVSARFVRLLPHDFQNGIYLRLEIMGC 2191
Cdd:smart00231  113 PIVARYVRILPTGWNGNIILRVELLGC 139

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 190609994    750 YAEAVCSVIHTA--VFQACHDAVEREHYFRLCLLEVCGCAPERLCHCTVITAYAQHCAQEGVAVH-WRNQTFCP 820
Cdd:smart00832    3 YACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76

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 190609994  2084 TSSTQSPYVQIDLLRFHNITGVLTQGGGVFGT-FVSSFYLQFSQDGRRWYTYKELVAQaqprakiflGNHDDRGVAEIHL 2162
Cdd:pfam00754   29 WSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNgYVTSYKIEYSLDGENWTTVKDEKIP---------GNNDNNTPVTNTF 99

                           90       100
                   ....*....|....*....|....*...
gi 190609994  2163 DRMVSARFVRLLPHDFQNG--IYLRLEI 2188
Cdd:pfam00754  100 DPPIKARYVRIVPTSWNGGngIALRAEL 127

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 190609994   4188 WTPWSVWSDCSVTCGHGTQIRTHACINPPPRNNGSDCLGPERETRDCPTLPC 4239
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

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 190609994   755 CSVIHTA-VFQACHDAVEREHYFRLCLLEVCGCAPERLCHCTVITAYAQHCAQEGVAV-HWRNQTFC 819
Cdd:pfam08742    2 CGLLSDSgPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 190609994   2771 WSAWSQWSKCSAKCDSGVQIRERFCNSPSPLHGGSKCPGPHIQTGDCNSHPCS 2823
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 190609994   3125 WSVWTPWGDCSVTCGVGLQSRYRFCPSLQPSESGLSCLGPHREDQVCLSAPCD 3177
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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.

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gi 190609994  461 CPKGQVYSDCVSSCPPNCASPQPPGPaaalgqCREECVGGCECPPGLYL-YQGNCLKRDDC 520
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP------CTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55