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 568941757    177 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 250
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 568941757   2200 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 2252
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 568941757   1663 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 1712
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941757    675 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 726
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53

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 568941757    60 GQAVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSR 138
Cdd:pfam00094   72 GGTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151

                   ...
gi 568941757   139 QGV 141
Cdd:pfam00094  152 DGT 154

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 568941757  394 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 428
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 568941757   2770 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 2822
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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 568941757   253 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 309
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-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 568941757  3018 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 3073
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 568941757  3780 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 3834
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 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 568941757 1409 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 1443
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

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 568941757  2350 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 2396
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 568941757 1577 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 1620
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 568941757 3382 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 3437
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 568941757 1352 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 1386
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 568941757   3118 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 3168
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53

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        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941757  1446 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 1497
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52

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 568941757  2474 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 2530
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55

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 568941757    470 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 501
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941757   2839 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 2887
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568941757   2420 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 2464
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941757    890 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 943
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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 568941757    177 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 250
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 568941757   1503 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 1555
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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 568941757   1045 CYSPLGLAGLPMWAPSQH--WEHITRADPVEApmagpgpregasAEWH----TQPLYLQLDLRRPRNLTGIIVQRAGSSA 1118
Cdd:smart00231    2 CNEPLGLESDSQITASSSywAAKIARLNGGSD------------GGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941757   1119 AYVsTLSLQFSSDNLQWHNYVNSLSSTLSPPKpspessNHMAPEVWTFDQMVQARYIRVWPHSGHlrdnnqHDIFLWVEL 1198
Cdd:smart00231   70 DWV-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN------GNIILRVEL 136

                    ...
gi 568941757   1199 LGC 1201
Cdd:smart00231  137 LGC 139

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941757   3212 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 3263
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

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        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941757  1505 EWGPWTACSVSCGGGHQSRQRScVDPPPKNGGAPCPgPSHEKAPCNLQLC 1554
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRT-VIVEPQNGGRPCP-ELLERRPCNLPPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941757    675 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 726
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 568941757   1778 WGLWASWSTCSASCNGGIQTRGRSCSGSAPGNP--VCLGPHTQTRDCNMHPC 1827
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVETRACNEQPC 52

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 568941757    60 GQAVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSR 138
Cdd:pfam00094   72 GGTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151

                   ...
gi 568941757   139 QGV 141
Cdd:pfam00094  152 DGT 154

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 568941757  394 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 428
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

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
                    ....*....|....*....|....*....|....*....
gi 568941757    102 WDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQG 140
Cdd:smart00216  125 FDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163

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 568941757  354 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 389
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941757   2593 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 2637
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52

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 568941757 2260 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 2310
Cdd:cd19941     3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 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 568941757  3018 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 3073
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 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 568941757  253 CEGGQVYEPCGSTCPPTCHDHHSELRwhCqVITCVEGCFCPEGTLLH-GGACMKLAAC 309
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP--C-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 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        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568941757  3727 VLGPWSAWSECSAVCGKGTMVRHRSCEEHPDR--EPCQalDLQQWQECNLQAC 3777
Cdd:pfam19028    2 VVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNggRPCP--ELLERRPCNLPPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941757   2905 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 2958
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 53

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 568941757  2035 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 2087
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 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 568941757  2260 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGAiCVKPSYC 2310
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLsppDVCPEPCVEGCVCPPGFVRNSGGK-CVPPSDC 55

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941757   2963 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 3015
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53