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 568941755 1277 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 1353
Cdd:cd00057    31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568941755 1354 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 1397
Cdd:cd00057   106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941755   1700 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 1752
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 568941755   3409 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 3460
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 568941755   2129 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 2180
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

Thrombospondin type 1 domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941755  1976 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2024
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 568941755  591 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 625
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 568941755   2790 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 2834
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 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 568941755   450 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 506
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941755   3926 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 3975
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 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 568941755  3977 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4031
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 568941755 1606 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 1640
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 568941755  2232 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 2284
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 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
                  ....*....|....*....|....*....|....*....|....*
gi 568941755 1774 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 1817
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 568941755 3579 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 3634
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 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 568941755     3 PCAVYQECAPVCGHHCGEPE-DCKELGICVAGCNCPPGLLWDLEGQCVPPSMC 54
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941755   3315 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 3365
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53

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 568941755  627 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 661
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 568941755   2328 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 2391
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941755   3774 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 3822
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941755   2089 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 2136
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 568941755 2028 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2087
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 568941755   3524 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 3575
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53

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 568941755    178 WHCTGQRCSGWCQASGAPHYVTFDGLVFTFPGACEYLLVREA--GGRFSVSVQNLPCGaSGLTCTKALVVRLDSTVVHML 255
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941755    256 RGQ-AVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGLTL-LWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLR 333
Cdd:smart00216   80 DDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQvTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159

                    ....
gi 568941755    334 SRQG 337
Cdd:smart00216  160 TPDG 163

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 568941755    374 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 447
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 568941755   1700 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 1752
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 568941755   1242 CYSPLGLAGLPMWAPSQH--WEHITRADPVEApmagpgpregasAEWH----TQPLYLQLDLRRPRNLTGIIVQRAGSSA 1315
Cdd:smart00231    2 CNEPLGLESDSQITASSSywAAKIARLNGGSD------------GGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941755   1316 AYVsTLSLQFSSDNLQWHNYVNSLSSTLSPPKpspessNHMAPEVWTFDQMVQARYIRVWPHSGHlrdnnqHDIFLWVEL 1395
Cdd:smart00231   70 DWV-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN------GNIILRVEL 136

                    ...
gi 568941755   1396 LGC 1398
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 568941755   3409 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 3460
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 568941755  1702 EWGPWTACSVSCGGGHQSRQRScVDPPPKNGGAPCPgPSHEKAPCNLQLC 1751
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 568941755    872 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 923
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 568941755   1975 WGLWASWSTCSASCNGGIQTRGRSCSGSAPGNP--VCLGPHTQTRDCNMHPC 2024
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVETRACNEQPC 52

Low-density lipoprotein receptor domain class A;

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568941755   738 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 774
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37

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 568941755  740 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 774
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 568941755   2967 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3019
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

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 568941755  551 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 586
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 568941755 2457 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 2507
Cdd:cd19941     3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941755   3926 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 3975
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941755  450 CEGGQVYEPCGSTCPPTCHDHHSELRwhCqVITCVEGCFCPEGTLLH-GGACMKLAAC 506
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 568941755  3924 VLGPWSAWSECSAVCGKGTMVRHRSCEEHPDR--EPCQalDLQQWQECNLQAC 3974
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 568941755   3102 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 3155
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 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
                   ....*....|....*....|....*....|....*....|....*..
gi 568941755  2547 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 2593
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42

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 568941755  2457 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGAiCVKPSYC 2507
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLsppDVCPEPCVEGCVCPPGFVRNSGGK-CVPPSDC 55