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 149033467  719 YAEWHTQPLYLQLDLLWPRNLTGIMVQRA--GSSAAYISNLSLQFSSDGLQWHSVLNslsstlpppkpspeSSNHMV--- 793
Cdd:cd00057    38 TPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD--------------KGEEKVftg 103

                          90       100
                  ....*....|....*....|....*....
gi 149033467  794 ------PEVWTFDQMVQARYIRVWPHGSH 816
Cdd:cd00057   104 nsdgstPVTNDFPPPIVARYIRILPTTWN 132

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 149033467   1575 WSPWTPWSPCSQSCNVGIRRRFRAGTAPPAAFGGAECRGPNLDAEFCTLRPC 1626
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52

Thrombospondin type 1 domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 149033467  1422 GLWASWSACSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNVHPC 1470
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 149033467   45 CGEGQMSCQSGRCLPLSLICDGQDDCGDGTDEQGC 79
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 149033467    5 CAEGEALCReSGHCVPLEWLCDNQDDCGDGSDEEGC 40
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
                  ....*....|....*....|....*....|....*....|....
gi 149033467 1221 PPCPPSCLDPEANRSCSGHCVEGCRCPPGLFL-QDSHCLPLSEC 1263
Cdd:cd19941    12 SACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 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 149033467 1052 CSPSQLSCGSGECLPLEHRCDLQVNCQDGSDEDDC 1086
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 149033467  995 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 1029
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        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 149033467   383 SSWSLWSPCSEPCG-GTMTRHRQ-CRPPQNGGQDCALLpgsthstHQTSPCPQEGC 436
Cdd:pfam19028    4 SEWSEWSECSVTCGgGVQTRTRTvIVEPQNGGRPCPEL-------LERRPCNLPPC 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 149033467    121 CTSGEVSCVDGPCIRTIQLCDGVWDCPDGADE 152
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

von Willebrand factor (vWF) type C domain;

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 149033467   1535 CQLHGQLYAPGAVARLDCNNCTCSSGEMVCTSERCPVA----------CGWSPWTPWS 1582
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 149033467    525 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEPCE 578
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 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 149033467  719 YAEWHTQPLYLQLDLLWPRNLTGIMVQRA--GSSAAYISNLSLQFSSDGLQWHSVLNslsstlpppkpspeSSNHMV--- 793
Cdd:cd00057    38 TPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD--------------KGEEKVftg 103

                          90       100
                  ....*....|....*....|....*....
gi 149033467  794 ------PEVWTFDQMVQARYIRVWPHGSH 816
Cdd:cd00057   104 nsdgstPVTNDFPPPIVARYIRILPTTWN 132

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 149033467   1306 WSAWSPWTACDHSCGSGVRARFRSPTNPPAAFGGSPCEGDRQELQACYTD 1355
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 149033467    326 WGSWGPWEPCSQTCGPGIQSRNRNC-SISSLHVLQNCPGLQHQSQSCFTEACP 377
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53

Thrombospondin type 1 domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 149033467  1422 GLWASWSACSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNVHPC 1470
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 149033467  194 CSLSEFQCNSGECTPRGWRCDREEDCTDGSDELDC 228
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 149033467   45 CGEGQMSCQSGRCLPLSLICDGQDDCGDGTDEQGC 79
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

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 149033467    678 CYSPLGLAGLPTWAPSqplehSTRAAPVEAPTAGpgpreDAYAEWH----TQPLYLQLDLLWPRNLTGIMVQRAGSSAAY 753
Cdd:smart00231    2 CNEPLGLESDSQITAS-----SSYWAAKIARLNG-----GSDGGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNGDW 71

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149033467    754 IsNLSLQFSSDGLQWHSVLNSLSSTLPPPKpspessNHMVPEVWTFDQMVQARYIRVWPHGSH 816
Cdd:smart00231   72 V-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN 127

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 149033467    194 CSLSEFQCNSGECTPRGWRCDREEDCTDGSDE 225
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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 149033467     45 CGEGQMSCQSGRCLPLSLICDGQDDCGDGTDE 76
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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 149033467  1678 CPKDQQWLDCAQG-PASCAHLSTPREANQTCHPGCYCLSGMLLLNN-VCVPAQDC 1730
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 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 149033467 1052 CSPSQLSCGSGECLPLEHRCDLQVNCQDGSDEDDC 1086
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 149033467   81 CPQGFLACADGRCLPPALLCDGHPDCLDAADEESC 115
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
                   ....*....|....*....|....*....|....*....|....
gi 149033467  1221 PPCPPSCLDPEANRSCSGHCVEGCRCPPGLFLQ-DSHCLPLSEC 1263
Cdd:pfam01826   12 SACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 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 149033467   327 GSWGPWEPCSQTCGPGIQSRNRNCSISSLHVLQNCPGLQhQSQSCFTEAC 376
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELL-ERRPCNLPPC 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 149033467   383 SSWSLWSPCSEPCG-GTMTRHRQ-CRPPQNGGQDCALLpgsthstHQTSPCPQEGC 436
Cdd:pfam19028    4 SEWSEWSECSVTCGgGVQTRTRTvIVEPQNGGRPCPEL-------LERRPCNLPPC 52

Thrombospondin type 1 domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 149033467  1844 GPWSPWSGCSRSCGGGLRSRTRACDKPPPQGP 1875
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGE 32

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 149033467  441 CFGELVFRPCAP-CPLTCDDISGEAVCSpdRPCSsPGCWCPEGKVLGTEGRCVRPRQC 497
Cdd:cd19941     1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 149033467   1093 PWSGWSDCSRSCGLGLIFQHRELLRPP--LPGGSCLLDQLRSQPCFVQACP 1141
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPpqNGGGPCTGEDVETRACNEQPCP 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 149033467 1474 CPGNMVFRSaekCleeGGPCPQLCLAQDPGVECTGSCAPGCSCPPGLFLH-NASCLPRSQC 1533
Cdd:cd19941     1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55

von Willebrand factor (vWF) type C domain;

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 149033467   1535 CQLHGQLYAPGAVARLDCNNCTCSSGEMVCTSERCPVA----------CGWSPWTPWS 1582
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58

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 149033467   1052 CSPSQLSCGSGECLPLEHRCDLQVNCQDGSDE 1083
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33

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 149033467   446 VFRPCA-PCPLTCDDISGEAVCSpdRPCSsPGCWCPEGKVLGTEGRCVRPRQC 497
Cdd:pfam01826    6 VYSECGsACPPTCANLSPPDVCP--EPCV-EGCVCPPGFVRNSGGKCVPPSDC 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 149033467 1678 CPKDQQWLDCAQG-PASCAHLSTPREANQTCHPGCYCLSGMLL-LNNVCVPAQDC 1730
Cdd:cd19941     1 CPPNEVYSECGSAcPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 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 149033467  1632 AWSSWTPCSVPCGGGYRNRT-------QGSGRHSP--VEFSTCSLQPC 1670
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPelLERRPCNLPPC 52

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 149033467    525 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEPCE 578
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53

sporozoite surface protein 2 (SSP2); Provisional

                          10        20
                  ....*....|....*....|..
gi 149033467 1844 GPWSPWSGCSRSCGGGLRSRTR 1865
Cdd:PTZ00441  241 GPWDEWTPCSVTCGKGTHSRSR 262

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 149033467  719 YAEWHTQPLYLQLDLLWPRNLTGIMVQRA--GSSAAYISNLSLQFSSDGLQWHSVLNslsstlpppkpspeSSNHMV--- 793
Cdd:cd00057    38 TPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD--------------KGEEKVftg 103

                          90       100
                  ....*....|....*....|....*....
gi 149033467  794 ------PEVWTFDQMVQARYIRVWPHGSH 816
Cdd:cd00057   104 nsdgstPVTNDFPPPIVARYIRILPTTWN 132

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 149033467   1306 WSAWSPWTACDHSCGSGVRARFRSPTNPPAAFGGSPCEGDRQELQACYTD 1355
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 149033467    326 WGSWGPWEPCSQTCGPGIQSRNRNC-SISSLHVLQNCPGLQHQSQSCFTEACP 377
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53

Thrombospondin type 1 domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 149033467  1422 GLWASWSACSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNVHPC 1470
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 149033467  194 CSLSEFQCNSGECTPRGWRCDREEDCTDGSDELDC 228
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 149033467   45 CGEGQMSCQSGRCLPLSLICDGQDDCGDGTDEQGC 79
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

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

                            10        20        30
                    ....*....|....*....|....*....|....*
gi 149033467   1843 WGPWSPWSGCSRSCGGGLRSRTRACDKPPPQGPGG 1877
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG 35