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Conserved domains on  [gi|1720417875|ref|XP_030111229|]
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SCO-spondin isoform X10 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1054-1203 1.59e-32

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.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.56  E-value: 1.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1054 CQASGAPHYVTFDGLVFTFPGACEYLLVREAGGR--FSVSVQNLPCGASGL-TCTKALVVRLDSTVVHMLRGQAVTVNGV 1130
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdFSFSVTNKNCNGGASgVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 1131 SIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQGV 1203
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 593-753 4.55e-26

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.


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 107.49  E-value: 4.55e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   593 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 670
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   671 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 748
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1720417875   749 LTPAG 753
Cdd:smart00216  159 RTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 229-378 2.04e-22

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.


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 97.09  E-value: 2.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   229 SATCATWSGFHYQTFDGHHYHFLGQCTYLLAGAMDS--TWAVHLRPSVHCPQHRHCWLVQVVMGPEEVLIQDGEVSVKGQ 306
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSepTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875   307 PVPVGEPQLLHGMSLQWQ--GDWLVLSGGLGVV-VRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 378
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRssGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
FA58C super family cl25480
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2142-2262 1.54e-17

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.


The actual alignment was detected with superfamily member cd00057:

Pssm-ID: 330301 [Multi-domain]  Cd Length: 143  Bit Score: 82.40  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2142 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2218
Cdd:cd00057     31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720417875 2219 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2262
Cdd:cd00057    106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 791-863 3.52e-17

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 78.92  E-value: 3.52e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875   791 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 863
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1239-1312 2.54e-15

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 73.53  E-value: 2.54e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  1239 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1312
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2565-2617 6.19e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 6.19e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  2565 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2617
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3262-3314 7.71e-12

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.99  E-value: 7.71e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  3262 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3314
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4274-4325 3.01e-10

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 58.37  E-value: 3.01e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  4274 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4325
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 433-505 4.04e-10

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.


:

Pssm-ID: 462584  Cd Length: 68  Bit Score: 58.55  E-value: 4.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875  433 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 505
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2725-2774 5.53e-10

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 57.60  E-value: 5.53e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2725 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 2774
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2994-3045 2.17e-09

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 56.06  E-value: 2.17e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  2994 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3045
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1737-1788 3.25e-09

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.67  E-value: 3.25e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  1737 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 1788
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
2841-2889 1.13e-08

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 2841 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2889
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1603-1639 4.43e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 4.43e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1720417875 1603 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1639
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1456-1490 8.68e-08

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 8.68e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1490
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 866-919 1.61e-07

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 50.78  E-value: 1.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  866 CPGGQVYQECAPVCGHHCGEPE---DCKElgICVAGCNCPPGLLWDLEGQCVPPSMC 919
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNappPCTK--QCVEGCFCPEGYVRNSGGKCVPPSQC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3655-3699 4.94e-07

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 4.94e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  3655 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3699
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3832-3884 5.13e-07

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 5.13e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  3832 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3884
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1315-1371 7.06e-07

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.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.92  E-value: 7.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1315 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 1371
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1416-1451 7.20e-07

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 48.36  E-value: 7.20e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720417875 1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1451
Cdd:cd00112      1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 509-564 7.56e-07

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 48.85  E-value: 7.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  509 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 564
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3322-3372 1.03e-06

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 48.47  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 3322 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 3372
Cdd:cd19941      3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4080-4135 1.55e-06

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.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4080 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4135
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4791-4840 1.65e-06

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 47.97  E-value: 1.65e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4791 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 4840
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4842-4896 2.45e-06

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.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.38  E-value: 2.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875 4842 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4896
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3967-4020 3.37e-06

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 47.20  E-value: 3.37e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  3967 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 4020
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3097-3149 4.97e-06

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.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 4.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875 3097 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3149
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2471-2505 5.26e-06

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 5.26e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2505
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3412-3458 6.98e-06

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.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 46.12  E-value: 6.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720417875 3412 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3458
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4025-4077 1.04e-05

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 1.04e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4025 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 4077
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2639-2682 1.10e-05

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.77  E-value: 1.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720417875 2639 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2682
Cdd:cd19941     11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1852-1908 1.14e-05

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.77  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1852 CFGELVFRTCAP-CPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1908
Cdd:cd19941      1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4444-4499 1.55e-05

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4444 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4499
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4701-4747 2.58e-05

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.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 44.69  E-value: 2.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 4701 DCANQCPRSCADLWDGVQCLqGPCSPGCRCPPGQLVQ-DGHCVPISSC 4747
Cdd:pfam01826    9 ECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2414-2448 4.42e-05

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 43.35  E-value: 4.42e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2414 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2448
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4180-4230 4.83e-05

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 43.73  E-value: 4.83e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  4180 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 4230
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2275-2309 7.09e-05

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.58  E-value: 7.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2309
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3193-3256 8.37e-05

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.96  E-value: 8.37e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  3193 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 3256
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1492-1526 8.71e-05

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.58  E-value: 8.71e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1492 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1526
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2508-2559 1.04e-04

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.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 42.65  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 2508 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 2559
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3536-3592 2.33e-04

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.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.99  E-value: 2.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 3536 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3592
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4639-4687 3.99e-04

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.03  E-value: 3.99e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4639 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4687
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1532-1563 6.85e-04

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.


:

Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.92  E-value: 6.85e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1532 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1563
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2954-3001 7.28e-04

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214565  Cd Length: 67  Bit Score: 41.01  E-value: 7.28e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875  2954 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 3001
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3901-3949 1.11e-03

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.88  E-value: 1.11e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  3901 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 3949
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2893-2952 1.54e-03

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.


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 39.61  E-value: 1.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 2893 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2952
Cdd:cd19941      1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3482-3526 2.30e-03

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.11  E-value: 2.30e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1720417875  3482 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 3526
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4389-4440 4.63e-03

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 4.63e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  4389 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4440
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1952-2005 5.64e-03

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.95  E-value: 5.64e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  1952 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 2005
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 5008-5063 6.28e-03

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


The actual alignment was detected with superfamily member pfam00093:

Pssm-ID: 450195  Cd Length: 57  Bit Score: 37.79  E-value: 6.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 5008 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5063
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDDGKVLCDKiICPPLDCPNPRLE-IPPGECCPVC 57
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3051-3089 8.37e-03

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.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 37.26  E-value: 8.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 3051 AWSSWTPCSVPCGGGYRNRT-------QGSGPHSPI--EFSTCSLQPC 3089
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPEllERRPCNLPPC 52
TIL super family cl20226
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4948-5006 8.72e-03

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.


The actual alignment was detected with superfamily member pfam01826:

Pssm-ID: 473303  Cd Length: 55  Bit Score: 37.37  E-value: 8.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417875 4948 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 5006
Cdd:pfam01826    1 CPANEVYSECG-SACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1054-1203 1.59e-32

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.56  E-value: 1.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1054 CQASGAPHYVTFDGLVFTFPGACEYLLVREAGGR--FSVSVQNLPCGASGL-TCTKALVVRLDSTVVHMLRGQAVTVNGV 1130
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdFSFSVTNKNCNGGASgVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 1131 SIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQGV 1203
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1043-1202 2.63e-32

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 125.59  E-value: 2.63e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  1043 WHCTGQRCSGWCQASGAPHYVTFDGLVFTFPGACEYLLVREA--GGRFSVSVQNLPCGaSGLTCTKALVVRLDSTVVHML 1120
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  1121 RGQ-AVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGLTL-LWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLR 1198
Cdd:smart00216   80 DDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQvTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159


                    ....
gi 1720417875  1199 SRQG 1202
Cdd:smart00216  160 TPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 593-753 4.55e-26

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 107.49  E-value: 4.55e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   593 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 670
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   671 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 748
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1720417875   749 LTPAG 753
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 604-753 2.22e-24

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 102.45  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  604 CAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACD---TGSCLHALSVFLGNTHIQLRYSGAVLVD 679
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGT--CTYVLAKDcSEEPDFSFSVTNKNCNggaSGVCLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  680 GEDVDLP-WIGVEGFNISWASSTFLLLHwPGAWVLW-GVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDFLTPAG 753
Cdd:pfam00094   79 GQKVSLPyKSDGGEVEILGSGFVVVDLS-PGVGLQVdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 229-378 2.04e-22

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 97.09  E-value: 2.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   229 SATCATWSGFHYQTFDGHHYHFLGQCTYLLAGAMDS--TWAVHLRPSVHCPQHRHCWLVQVVMGPEEVLIQDGEVSVKGQ 306
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSepTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875   307 PVPVGEPQLLHGMSLQWQ--GDWLVLSGGLGVV-VRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 378
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRssGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 232-378 1.06e-21

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 94.74  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  232 CATWSGFHYQTFDGHHYHFLGQCTYLLA----GAMDSTWAVHLRPsVHCPQHRHCW-LVQVVMGPEEVLIQDG-EVSVKG 305
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAkdcsEEPDFSFSVTNKN-CNGGASGVCLkSVTVIVGDLEITLQKGgTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  306 QPVPVgePQLLHGMSLQ--WQGDWLV-LSGGLGVVVRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 378
Cdd:pfam00094   80 QKVSL--PYKSDGGEVEilGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2142-2262 1.54e-17

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.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 82.40  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2142 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2218
Cdd:cd00057     31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720417875 2219 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2262
Cdd:cd00057    106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 791-863 3.52e-17

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 78.92  E-value: 3.52e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875   791 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 863
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1239-1312 2.54e-15

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 73.53  E-value: 2.54e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  1239 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1312
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2565-2617 6.19e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 6.19e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  2565 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2617
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1244-1311 7.56e-15

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 72.03  E-value: 7.56e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1244 RCEVIL-QPIFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELC 1311
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2151-2260 3.89e-14

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 72.09  E-value: 3.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2151 WH----TQPLYLQLDLRRPRNLTGIIVQ-RAGSSAAYVSTLSLQFSSDNLQWHNYVNSLSSTlsppkpspeSSNHMAPEV 2225
Cdd:pfam00754   26 WSawsgDDPQWIQVDLGKPKKITGVVTQgRQDGSNGYVTSYKIEYSLDGENWTTVKDEKIPG---------NNDNNTPVT 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1720417875 2226 WTFDQMVQARYIRVWPhsghLRDNNQHDIFLWVEL 2260
Cdd:pfam00754   97 NTFDPPIKARYVRIVP----TSWNGGNGIALRAEL 127
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2107-2263 3.23e-13

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.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 69.85  E-value: 3.23e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2107 CYSPLGLAGLPMWAPSQH--WEHITRADPVEApmagpgpregasAEWH----TQPLYLQLDLRRPRNLTGIIVQRAGSSA 2180
Cdd:smart00231    2 CNEPLGLESDSQITASSSywAAKIARLNGGSD------------GGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2181 AYVsTLSLQFSSDNLQWHNYVNSLSSTLSPPKpspessNHMAPEVWTFDQMVQARYIRVWPHSGHlrdnnqHDIFLWVEL 2260
Cdd:smart00231   70 DWV-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN------GNIILRVEL 136


                    ...
gi 1720417875  2261 LGC 2263
Cdd:smart00231  137 LGC 139
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3262-3314 7.71e-12

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.99  E-value: 7.71e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  3262 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3314
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 800-862 1.28e-11

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 62.78  E-value: 1.28e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  800 ILHGHAFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLC 862
Cdd:pfam08742    5 LSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4274-4325 3.01e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 58.37  E-value: 3.01e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  4274 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4325
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 433-505 4.04e-10

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 58.55  E-value: 4.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875  433 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 505
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2725-2774 5.53e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 57.60  E-value: 5.53e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2725 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 2774
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2567-2616 1.25e-09

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 56.52  E-value: 1.25e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2567 EWGPWTACSVSCGGGHQSRQRScVDPPPKNGGAPCPgPSHEKAPCNLQLC 2616
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRT-VIVEPQNGGRPCP-ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2994-3045 2.17e-09

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 56.06  E-value: 2.17e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  2994 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3045
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1737-1788 3.25e-09

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.67  E-value: 3.25e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  1737 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 1788
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
2841-2889 1.13e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 2841 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2889
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2840-2889 1.25e-08

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 54.13  E-value: 1.25e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  2840 WGLWASWSTCSASCNGGIQTRGRSCSGSAPGNP--VCLGPHTQTRDCNMHPC 2889
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
3263-3313 1.52e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 1.52e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 3263 SPWSPWSGCSRSCGGGLRSRTRACDQPSPQglGDFCEGPQAQGEACQAQPC 3313
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1603-1639 4.43e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 4.43e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1720417875 1603 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1639
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1456-1490 8.68e-08

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 8.68e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1490
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 866-919 1.61e-07

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 50.78  E-value: 1.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  866 CPGGQVYQECAPVCGHHCGEPE---DCKElgICVAGCNCPPGLLWDLEGQCVPPSMC 919
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNappPCTK--QCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 866-919 1.74e-07

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 50.85  E-value: 1.74e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875  866 CPGGQVYQECAPVCGHHCGEPE-DCKELGICVAGCNCPPGLLWDLEGQCVPPSMC 919
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 427-505 1.94e-07

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 51.19  E-value: 1.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   427 QAQAQDMCHQLL--EGPFWQCHGQVQPDEYHETCLFAYCVGatagngpEGQLEAVCATFANYAQACARQHIYVH-WRKPG 503
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCAC-------GGDCECLCDALAAYAAACAEAGVCISpWRTPT 73


                    ..
gi 1720417875   504 FC 505
Cdd:smart00832   74 FC 75
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1605-1639 2.48e-07

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 49.51  E-value: 2.48e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1605 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1639
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP_1 pfam00090
Thrombospondin type 1 domain;
4275-4325 4.68e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.34  E-value: 4.68e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 4275 TLWSSWSYCSVSCGGGSQVRTRSCtvSAPPHGSLSCEGPDTQTRHCGQQLC 4325
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTC--KSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3655-3699 4.94e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 4.94e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  3655 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3699
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3832-3884 5.13e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 5.13e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  3832 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3884
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1315-1371 7.06e-07

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.92  E-value: 7.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1315 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 1371
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1416-1451 7.20e-07

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 48.36  E-value: 7.20e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720417875 1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1451
Cdd:cd00112      1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 509-564 7.56e-07

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 48.85  E-value: 7.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  509 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 564
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3322-3372 1.03e-06

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 48.47  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 3322 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 3372
Cdd:cd19941      3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 509-564 1.25e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  509 CPGGQLYSDCVSSCPPSCSAVAQGEEgsCGKECVSGCECPTGLFWD-GALCVPAAHC 564
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV--CPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4080-4135 1.55e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4080 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4135
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4791-4840 1.65e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 47.97  E-value: 1.65e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4791 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 4840
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1315-1371 1.79e-06

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.70  E-value: 1.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1315 CEGGQVYEPCGSTCPPTCHDHHSELRwhCqVITCVEGCFCPEGTLLH-GGACMKLAAC 1371
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPP--C-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1456-1487 1.96e-06

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 47.24  E-value: 1.96e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDE 1487
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4842-4896 2.45e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.38  E-value: 2.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875 4842 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4896
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1605-1636 2.95e-06

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.47  E-value: 2.95e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1605 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDE 1636
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 4789-4839 3.28e-06

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.89  E-value: 3.28e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875 4789 VLGPWSAWSECSAVCGKGTMVRHRSCEEHPDR--EPCQalDLQQWQECNLQAC 4839
Cdd:pfam19028    2 VVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNggRPCP--ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3967-4020 3.37e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 47.20  E-value: 3.37e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  3967 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 4020
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3097-3149 4.97e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 4.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875 3097 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3149
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2471-2505 5.26e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 5.26e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2505
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3322-3372 5.87e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 5.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 3322 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGAiCVKPSYC 3372
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLsppDVCPEPCVEGCVCPPGFVRNSGGK-CVPPSDC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3412-3458 6.98e-06

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.12  E-value: 6.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720417875 3412 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3458
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42
TSP_1 pfam00090
Thrombospondin type 1 domain;
3656-3699 9.14e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 9.14e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 3656 SSWGPWEKCSVSCGGGEQLRSRQCARP-----PCPGLAQQSRICHIHVC 3699
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPfpggePCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4025-4077 1.04e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 1.04e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4025 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 4077
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2639-2682 1.10e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.77  E-value: 1.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720417875 2639 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2682
Cdd:cd19941     11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1852-1908 1.14e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.77  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1852 CFGELVFRTCAP-CPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1908
Cdd:cd19941      1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2992-3045 1.21e-05

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.35  E-value: 1.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 2992 CGWSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAfGGAECqGPNLDAEFCSLRPC 3045
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4080-4135 1.39e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4080 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4135
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQ--CVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4444-4499 1.55e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4444 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4499
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1416-1448 1.94e-05

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 44.16  E-value: 1.94e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1720417875  1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDE 1448
Cdd:smart00192    2 CPPGEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4701-4747 2.58e-05

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 44.69  E-value: 2.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 4701 DCANQCPRSCADLWDGVQCLqGPCSPGCRCPPGQLVQ-DGHCVPISSC 4747
Cdd:pfam01826    9 ECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1738-1792 3.01e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.35  E-value: 3.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1738 GSWGPWAPCSQTCGSGTRSRNR-----NCSTsslqvlqncpglqHQSQACFTEACPVDGE 1792
Cdd:PTZ00441   241 GPWDEWTPCSVTCGKGTHSRSRpilheGCTT-------------HMVEECEEEECPVEPE 287
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2414-2448 4.42e-05

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 43.35  E-value: 4.42e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2414 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2448
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4180-4230 4.83e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 43.73  E-value: 4.83e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  4180 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 4230
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4842-4896 5.14e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.84  E-value: 5.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875 4842 CPPGQVLSTCATMCPSLCSHLWPGTICVrEPCQLGCGCPGGQLL-YNGTCIPPEAC 4896
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCT-KQCVEGCFCPEGYVRnSGGKCVPPSQC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2275-2309 7.09e-05

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.58  E-value: 7.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2309
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3193-3256 8.37e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.96  E-value: 8.37e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  3193 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 3256
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1492-1526 8.71e-05

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.58  E-value: 8.71e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1492 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1526
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2639-2682 9.83e-05

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 43.14  E-value: 9.83e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720417875 2639 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLLQ-DSHCLPLSEC 2682
Cdd:pfam01826   11 GSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1456-1490 9.83e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.24  E-value: 9.83e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1490
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2508-2559 1.04e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 42.65  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 2508 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 2559
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
2726-2771 1.16e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.41  E-value: 1.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720417875 2726 SAWSPWTACDRSCGSGVRARFRSPTNPPVafGGSPCEGDRQELQAC 2771
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1857-1908 1.21e-04

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 42.76  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875 1857 VFRTCA-PCPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1908
Cdd:pfam01826    6 VYSECGsACPPTCANLSPPDVCP--EPCV-EGCVCPPGFVRNSGGKCVPPSDC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1738-1787 2.30e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.88  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1738 GSWGPWAPCSQTCGSGTRSRNRNCSTSSLQVLQNCPGLQhQSQACFTEAC 1787
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELL-ERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3536-3592 2.33e-04

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.99  E-value: 2.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 3536 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3592
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3418-3458 2.35e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.80  E-value: 2.35e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1720417875  3418 WCPWSKWTACSQPCRGQTRTRSRACVCPAPQHGGSPCPEES 3458
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGED 41
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4444-4499 2.63e-04

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.60  E-value: 2.63e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4444 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4499
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGfVRNSGGKCVPPSDC 55
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2275-2309 3.59e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.69  E-value: 3.59e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2309
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4639-4687 3.99e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.03  E-value: 3.99e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4639 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4687
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2471-2505 5.33e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 5.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2505
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2471-2502 5.57e-04

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 40.31  E-value: 5.57e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDE 2502
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1532-1563 6.85e-04

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.92  E-value: 6.85e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1532 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1563
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2954-3001 7.28e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 41.01  E-value: 7.28e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875  2954 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 3001
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4701-4747 7.82e-04

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 40.38  E-value: 7.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 4701 DCANQCPRSCADLWDGVQCLQgPCSPGCRCPPGQ-LVQDGHCVPISSC 4747
Cdd:cd19941      9 ECGSACPPTCANPNAPPPCTK-QCVEGCFCPEGYvRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3097-3149 8.38e-04

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 40.38  E-value: 8.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875 3097 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLL-LNNVCVPVQDC 3149
Cdd:cd19941      1 CPPNEVYSECGSAcPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
3832-3883 1.11e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 3832 GPWGMWSLCSRSCGGlGTRTRTRQCVLPtlAPGGLSCRGPLQDLEYCFSPEC 3883
Cdd:pfam00090    1 SPWSPWSPCSVTCGK-GIQVRQRTCKSP--FPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3901-3949 1.11e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.88  E-value: 1.11e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  3901 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 3949
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 3972-4019 1.15e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 40.13  E-value: 1.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 3972 PWEPCSRSCGVGQQRRL----RAYHPPGPGGHWCpDILTAYQERRFCNLRAC 4019
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLvqcvQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1532-1563 1.16e-03

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 39.50  E-value: 1.16e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720417875 1532 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1563
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1416-1451 1.34e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 1.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720417875 1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1451
Cdd:pfam00057    3 CSPNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2893-2952 1.54e-03

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 39.61  E-value: 1.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 2893 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2952
Cdd:cd19941      1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2414-2445 1.87e-03

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.77  E-value: 1.87e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  2414 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDE 2445
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP_1 pfam00090
Thrombospondin type 1 domain;
4640-4686 2.03e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.94  E-value: 2.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 4640 GPWGPWSPCQMPCSGGFKLRWRV--ARDTSAGECPGPWAQTESCNMGSC 4686
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTckSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3482-3526 2.30e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.11  E-value: 2.30e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1720417875  3482 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 3526
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1492-1523 2.68e-03

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.38  E-value: 2.68e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1492 CPHGSLACADGRCLPPALLCNGHPDCLDAADE 1523
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3536-3592 3.81e-03

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 38.45  E-value: 3.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 3536 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3592
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC---TKQCVEGCFCPEGYvRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2275-2306 4.30e-03

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 37.61  E-value: 4.30e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDE 2306
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4389-4440 4.63e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 4.63e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  4389 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4440
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1952-2005 5.64e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.95  E-value: 5.64e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  1952 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 2005
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 5008-5063 6.28e-03

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 37.79  E-value: 6.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 5008 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5063
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDDGKVLCDKiICPPLDCPNPRLE-IPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
5008-5063 6.72e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.88  E-value: 6.72e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  5008 CWHHGSPHLPGSEWQ-EACESCRCLHGKSVCIRH--CPE-LSCAQGEViMQEPGSCCPIC 5063
Cdd:smart00214    1 CVHNGRVYNDGETWKpDPCQICTCLDGTTVLCDPveCPPpPDCPNPER-VKPPGECCPRC 59
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3051-3089 8.37e-03

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 37.26  E-value: 8.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 3051 AWSSWTPCSVPCGGGYRNRT-------QGSGPHSPI--EFSTCSLQPC 3089
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPEllERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4948-5006 8.72e-03

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 37.37  E-value: 8.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417875 4948 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 5006
Cdd:pfam01826    1 CPANEVYSECG-SACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1054-1203 1.59e-32

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.56  E-value: 1.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1054 CQASGAPHYVTFDGLVFTFPGACEYLLVREAGGR--FSVSVQNLPCGASGL-TCTKALVVRLDSTVVHMLRGQAVTVNGV 1130
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdFSFSVTNKNCNGGASgVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 1131 SIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQGV 1203
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1043-1202 2.63e-32

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 125.59  E-value: 2.63e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  1043 WHCTGQRCSGWCQASGAPHYVTFDGLVFTFPGACEYLLVREA--GGRFSVSVQNLPCGaSGLTCTKALVVRLDSTVVHML 1120
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  1121 RGQ-AVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGLTL-LWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLR 1198
Cdd:smart00216   80 DDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQvTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159


                    ....
gi 1720417875  1199 SRQG 1202
Cdd:smart00216  160 TPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 593-753 4.55e-26

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 107.49  E-value: 4.55e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   593 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 670
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   671 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 748
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1720417875   749 LTPAG 753
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 604-753 2.22e-24

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 102.45  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  604 CAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACD---TGSCLHALSVFLGNTHIQLRYSGAVLVD 679
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGT--CTYVLAKDcSEEPDFSFSVTNKNCNggaSGVCLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  680 GEDVDLP-WIGVEGFNISWASSTFLLLHwPGAWVLW-GVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDFLTPAG 753
Cdd:pfam00094   79 GQKVSLPyKSDGGEVEILGSGFVVVDLS-PGVGLQVdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 229-378 2.04e-22

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 97.09  E-value: 2.04e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   229 SATCATWSGFHYQTFDGHHYHFLGQCTYLLAGAMDS--TWAVHLRPSVHCPQHRHCWLVQVVMGPEEVLIQDGEVSVKGQ 306
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSepTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875   307 PVPVGEPQLLHGMSLQWQ--GDWLVLSGGLGVV-VRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 378
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRssGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 232-378 1.06e-21

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 94.74  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  232 CATWSGFHYQTFDGHHYHFLGQCTYLLA----GAMDSTWAVHLRPsVHCPQHRHCW-LVQVVMGPEEVLIQDG-EVSVKG 305
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAkdcsEEPDFSFSVTNKN-CNGGASGVCLkSVTVIVGDLEITLQKGgTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  306 QPVPVgePQLLHGMSLQ--WQGDWLV-LSGGLGVVVRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 378
Cdd:pfam00094   80 QKVSL--PYKSDGGEVEilGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2142-2262 1.54e-17

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.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 82.40  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2142 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2218
Cdd:cd00057     31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720417875 2219 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2262
Cdd:cd00057    106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 791-863 3.52e-17

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 78.92  E-value: 3.52e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875   791 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 863
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1239-1312 2.54e-15

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 73.53  E-value: 2.54e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  1239 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1312
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2565-2617 6.19e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 6.19e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  2565 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2617
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1244-1311 7.56e-15

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 72.03  E-value: 7.56e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1244 RCEVIL-QPIFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELC 1311
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2151-2260 3.89e-14

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 72.09  E-value: 3.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2151 WH----TQPLYLQLDLRRPRNLTGIIVQ-RAGSSAAYVSTLSLQFSSDNLQWHNYVNSLSSTlsppkpspeSSNHMAPEV 2225
Cdd:pfam00754   26 WSawsgDDPQWIQVDLGKPKKITGVVTQgRQDGSNGYVTSYKIEYSLDGENWTTVKDEKIPG---------NNDNNTPVT 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1720417875 2226 WTFDQMVQARYIRVWPhsghLRDNNQHDIFLWVEL 2260
Cdd:pfam00754   97 NTFDPPIKARYVRIVP----TSWNGGNGIALRAEL 127
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2107-2263 3.23e-13

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.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 69.85  E-value: 3.23e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2107 CYSPLGLAGLPMWAPSQH--WEHITRADPVEApmagpgpregasAEWH----TQPLYLQLDLRRPRNLTGIIVQRAGSSA 2180
Cdd:smart00231    2 CNEPLGLESDSQITASSSywAAKIARLNGGSD------------GGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2181 AYVsTLSLQFSSDNLQWHNYVNSLSSTLSPPKpspessNHMAPEVWTFDQMVQARYIRVWPHSGHlrdnnqHDIFLWVEL 2260
Cdd:smart00231   70 DWV-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN------GNIILRVEL 136


                    ...
gi 1720417875  2261 LGC 2263
Cdd:smart00231  137 LGC 139
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3262-3314 7.71e-12

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.99  E-value: 7.71e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  3262 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3314
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 800-862 1.28e-11

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 62.78  E-value: 1.28e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  800 ILHGHAFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLC 862
Cdd:pfam08742    5 LSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4274-4325 3.01e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 58.37  E-value: 3.01e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  4274 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4325
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 433-505 4.04e-10

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 58.55  E-value: 4.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875  433 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 505
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2725-2774 5.53e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 57.60  E-value: 5.53e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720417875  2725 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 2774
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2567-2616 1.25e-09

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 56.52  E-value: 1.25e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2567 EWGPWTACSVSCGGGHQSRQRScVDPPPKNGGAPCPgPSHEKAPCNLQLC 2616
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRT-VIVEPQNGGRPCP-ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2994-3045 2.17e-09

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 56.06  E-value: 2.17e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  2994 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3045
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
2567-2616 3.11e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.50  E-value: 3.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 2567 EWGPWTACSVSCGGGHQSRQRSCVDPPPknGGAPCPGPSHEKAPCNLQLC 2616
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1737-1788 3.25e-09

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.67  E-value: 3.25e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  1737 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 1788
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
2841-2889 1.13e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 2841 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2889
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2840-2889 1.25e-08

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 54.13  E-value: 1.25e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  2840 WGLWASWSTCSASCNGGIQTRGRSCSGSAPGNP--VCLGPHTQTRDCNMHPC 2889
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
3263-3313 1.52e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 1.52e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 3263 SPWSPWSGCSRSCGGGLRSRTRACDQPSPQglGDFCEGPQAQGEACQAQPC 3313
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1603-1639 4.43e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 4.43e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1720417875 1603 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1639
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1456-1490 8.68e-08

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 8.68e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1490
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 866-919 1.61e-07

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 50.78  E-value: 1.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  866 CPGGQVYQECAPVCGHHCGEPE---DCKElgICVAGCNCPPGLLWDLEGQCVPPSMC 919
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNappPCTK--QCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 866-919 1.74e-07

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 50.85  E-value: 1.74e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875  866 CPGGQVYQECAPVCGHHCGEPE-DCKELGICVAGCNCPPGLLWDLEGQCVPPSMC 919
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 427-505 1.94e-07

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 51.19  E-value: 1.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875   427 QAQAQDMCHQLL--EGPFWQCHGQVQPDEYHETCLFAYCVGatagngpEGQLEAVCATFANYAQACARQHIYVH-WRKPG 503
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCAC-------GGDCECLCDALAAYAAACAEAGVCISpWRTPT 73


                    ..
gi 1720417875   504 FC 505
Cdd:smart00832   74 FC 75
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1605-1639 2.48e-07

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 49.51  E-value: 2.48e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1605 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1639
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP_1 pfam00090
Thrombospondin type 1 domain;
4275-4325 4.68e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.34  E-value: 4.68e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 4275 TLWSSWSYCSVSCGGGSQVRTRSCtvSAPPHGSLSCEGPDTQTRHCGQQLC 4325
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTC--KSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3655-3699 4.94e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 4.94e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  3655 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3699
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3832-3884 5.13e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 5.13e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  3832 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3884
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1315-1371 7.06e-07

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.92  E-value: 7.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1315 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 1371
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1416-1451 7.20e-07

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 48.36  E-value: 7.20e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720417875 1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1451
Cdd:cd00112      1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 509-564 7.56e-07

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 48.85  E-value: 7.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  509 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 564
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3322-3372 1.03e-06

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 48.47  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 3322 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 3372
Cdd:cd19941      3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 509-564 1.25e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  509 CPGGQLYSDCVSSCPPSCSAVAQGEEgsCGKECVSGCECPTGLFWD-GALCVPAAHC 564
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV--CPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4080-4135 1.55e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4080 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4135
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4791-4840 1.65e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 47.97  E-value: 1.65e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4791 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 4840
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1315-1371 1.79e-06

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.70  E-value: 1.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1315 CEGGQVYEPCGSTCPPTCHDHHSELRwhCqVITCVEGCFCPEGTLLH-GGACMKLAAC 1371
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPP--C-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1456-1487 1.96e-06

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 47.24  E-value: 1.96e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDE 1487
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4842-4896 2.45e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.38  E-value: 2.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875 4842 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4896
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1605-1636 2.95e-06

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.47  E-value: 2.95e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1605 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDE 1636
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 4789-4839 3.28e-06

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.89  E-value: 3.28e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875 4789 VLGPWSAWSECSAVCGKGTMVRHRSCEEHPDR--EPCQalDLQQWQECNLQAC 4839
Cdd:pfam19028    2 VVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNggRPCP--ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3967-4020 3.37e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 47.20  E-value: 3.37e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875  3967 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 4020
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3263-3313 3.58e-06

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.89  E-value: 3.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 3263 SPWSPWSGCSRSCGGGLRSRTRACDQPsPQGLGDFCeGPQAQGEACQAQPC 3313
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3097-3149 4.97e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 4.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875 3097 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3149
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2471-2505 5.26e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 5.26e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2505
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3322-3372 5.87e-06

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 5.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 3322 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGAiCVKPSYC 3372
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLsppDVCPEPCVEGCVCPPGFVRNSGGK-CVPPSDC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3412-3458 6.98e-06

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.12  E-value: 6.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720417875 3412 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3458
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42
TSP_1 pfam00090
Thrombospondin type 1 domain;
3656-3699 9.14e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 9.14e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 3656 SSWGPWEKCSVSCGGGEQLRSRQCARP-----PCPGLAQQSRICHIHVC 3699
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPfpggePCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
4791-4839 9.23e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 9.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 4791 GPWSAWSECSAVCGKGTMVRHRSCE-EHPDREPCqALDLQQWQECNLQAC 4839
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKsPFPGGEPC-TGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 4277-4325 9.75e-06

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.73  E-value: 9.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 4277 WSSWSYCSVSCGGGSQVRTRSCTVsAPPHGSLSCeGPDTQTRHCGQQLC 4325
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIV-EPQNGGRPC-PELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4025-4077 1.04e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 1.04e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4025 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 4077
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2639-2682 1.10e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.77  E-value: 1.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720417875 2639 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2682
Cdd:cd19941     11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1852-1908 1.14e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.77  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 1852 CFGELVFRTCAP-CPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1908
Cdd:cd19941      1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2992-3045 1.21e-05

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.35  E-value: 1.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875 2992 CGWSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAfGGAECqGPNLDAEFCSLRPC 3045
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4080-4135 1.39e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4080 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4135
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQ--CVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4444-4499 1.55e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4444 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4499
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1416-1448 1.94e-05

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 44.16  E-value: 1.94e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1720417875  1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDE 1448
Cdd:smart00192    2 CPPGEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4701-4747 2.58e-05

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 44.69  E-value: 2.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 4701 DCANQCPRSCADLWDGVQCLqGPCSPGCRCPPGQLVQ-DGHCVPISSC 4747
Cdd:pfam01826    9 ECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1738-1792 3.01e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.35  E-value: 3.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1738 GSWGPWAPCSQTCGSGTRSRNR-----NCSTsslqvlqncpglqHQSQACFTEACPVDGE 1792
Cdd:PTZ00441   241 GPWDEWTPCSVTCGKGTHSRSRpilheGCTT-------------HMVEECEEEECPVEPE 287
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2414-2448 4.42e-05

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 43.35  E-value: 4.42e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2414 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2448
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4180-4230 4.83e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 43.73  E-value: 4.83e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  4180 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 4230
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4842-4896 5.14e-05

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.84  E-value: 5.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417875 4842 CPPGQVLSTCATMCPSLCSHLWPGTICVrEPCQLGCGCPGGQLL-YNGTCIPPEAC 4896
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCT-KQCVEGCFCPEGYVRnSGGKCVPPSQC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2275-2309 7.09e-05

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.58  E-value: 7.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2309
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3193-3256 8.37e-05

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.96  E-value: 8.37e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  3193 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 3256
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1492-1526 8.71e-05

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.58  E-value: 8.71e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1492 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1526
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2639-2682 9.83e-05

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 43.14  E-value: 9.83e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720417875 2639 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLLQ-DSHCLPLSEC 2682
Cdd:pfam01826   11 GSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1456-1490 9.83e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.24  E-value: 9.83e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 1456 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1490
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2843-2889 1.04e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 42.65  E-value: 1.04e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720417875 2843 WASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2889
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2508-2559 1.04e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 42.65  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 2508 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 2559
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
2726-2771 1.16e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.41  E-value: 1.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720417875 2726 SAWSPWTACDRSCGSGVRARFRSPTNPPVafGGSPCEGDRQELQAC 2771
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1857-1908 1.21e-04

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 42.76  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875 1857 VFRTCA-PCPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1908
Cdd:pfam01826    6 VYSECGsACPPTCANLSPPDVCP--EPCV-EGCVCPPGFVRNSGGKCVPPSDC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2723-2774 1.78e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 42.27  E-value: 1.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 2723 CGWSAWSPWTACDRSCGSGVRARFRSPTNPPvAFGGSPCeGDRQELQACYTD 2774
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEP-QNGGRPC-PELLERRPCNLP 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
2995-3045 1.85e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 1.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 2995 SPWTPWSPCSQSCNVGIRRRFRAGTEPPAafGGAECQGPNLDAEFCSLRPC 3045
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1738-1787 2.30e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.88  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 1738 GSWGPWAPCSQTCGSGTRSRNRNCSTSSLQVLQNCPGLQhQSQACFTEAC 1787
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELL-ERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3536-3592 2.33e-04

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.99  E-value: 2.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 3536 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3592
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3418-3458 2.35e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.80  E-value: 2.35e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1720417875  3418 WCPWSKWTACSQPCRGQTRTRSRACVCPAPQHGGSPCPEES 3458
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGED 41
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3656-3699 2.54e-04

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.88  E-value: 2.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720417875 3656 SSWGPWEKCSVSCGGGEQLRSRQCARPP------CPGLaQQSRICHIHVC 3699
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPqnggrpCPEL-LERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4444-4499 2.63e-04

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.60  E-value: 2.63e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 4444 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4499
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGfVRNSGGKCVPPSDC 55
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2275-2309 3.59e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.69  E-value: 3.59e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2309
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4639-4687 3.99e-04

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.03  E-value: 3.99e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720417875  4639 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4687
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2471-2505 5.33e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 5.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1720417875 2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2505
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2471-2502 5.57e-04

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 40.31  E-value: 5.57e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  2471 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDE 2502
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1532-1563 6.85e-04

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.92  E-value: 6.85e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1532 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1563
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2954-3001 7.28e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 41.01  E-value: 7.28e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875  2954 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 3001
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58
TSP_1 pfam00090
Thrombospondin type 1 domain;
1740-1787 7.53e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 40.48  E-value: 7.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 1740 WGPWAPCSQTCGSGTRSRNRNCStSSLQVLQNCPGLQHQSQACFTEAC 1787
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCK-SPFPGGEPCTGDDIETQACKMDKC 49
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4701-4747 7.82e-04

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 40.38  E-value: 7.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 4701 DCANQCPRSCADLWDGVQCLQgPCSPGCRCPPGQ-LVQDGHCVPISSC 4747
Cdd:cd19941      9 ECGSACPPTCANPNAPPPCTK-QCVEGCFCPEGYvRNSGGKCVPPSQC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 2569-2616 8.33e-04

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 40.51  E-value: 8.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 2569 GPWTACSVSCGGGHQSRQRSCVDPPPK--NGGAPCPGPS--HEKAPCNLQLC 2616
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKkpPETQSCNLKPC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3097-3149 8.38e-04

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 40.38  E-value: 8.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720417875 3097 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLL-LNNVCVPVQDC 3149
Cdd:cd19941      1 CPPNEVYSECGSAcPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
3832-3883 1.11e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 3832 GPWGMWSLCSRSCGGlGTRTRTRQCVLPtlAPGGLSCRGPLQDLEYCFSPEC 3883
Cdd:pfam00090    1 SPWSPWSPCSVTCGK-GIQVRQRTCKSP--FPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3901-3949 1.11e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.88  E-value: 1.11e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875  3901 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 3949
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 3972-4019 1.15e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 40.13  E-value: 1.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 3972 PWEPCSRSCGVGQQRRL----RAYHPPGPGGHWCpDILTAYQERRFCNLRAC 4019
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLvqcvQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1532-1563 1.16e-03

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 39.50  E-value: 1.16e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720417875 1532 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1563
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1416-1451 1.34e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 1.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720417875 1416 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1451
Cdd:pfam00057    3 CSPNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2893-2952 1.54e-03

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 39.61  E-value: 1.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417875 2893 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2952
Cdd:cd19941      1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3832-3883 1.57e-03

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 1.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875 3832 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLApGGLSCrGPLQDLEYCFSPEC 3883
Cdd:pfam19028    4 SEWSEWSECSVTCGG-GVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3965-4019 1.80e-03

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.18  E-value: 1.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417875 3965 CFWTSWAPWEPCSRSCGVGQQRRLRA--YHPPGpGGHWCPDILtayqERRFCNLRAC 4019
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTviVEPQN-GGRPCPELL----ERRPCNLPPC 52
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2414-2445 1.87e-03

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.77  E-value: 1.87e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  2414 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDE 2445
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP_1 pfam00090
Thrombospondin type 1 domain;
4640-4686 2.03e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.94  E-value: 2.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720417875 4640 GPWGPWSPCQMPCSGGFKLRWRV--ARDTSAGECPGPWAQTESCNMGSC 4686
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTckSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3482-3526 2.30e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.11  E-value: 2.30e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1720417875  3482 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 3526
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1492-1523 2.68e-03

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.38  E-value: 2.68e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  1492 CPHGSLACADGRCLPPALLCNGHPDCLDAADE 1523
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3536-3592 3.81e-03

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.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 38.45  E-value: 3.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 3536 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3592
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC---TKQCVEGCFCPEGYvRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2275-2306 4.30e-03

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.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 37.61  E-value: 4.30e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720417875  2275 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDE 2306
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4389-4440 4.63e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 4.63e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  4389 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4440
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1952-2005 5.64e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.95  E-value: 5.64e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417875  1952 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 2005
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 5008-5063 6.28e-03

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 37.79  E-value: 6.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417875 5008 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5063
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDDGKVLCDKiICPPLDCPNPRLE-IPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
5008-5063 6.72e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.88  E-value: 6.72e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417875  5008 CWHHGSPHLPGSEWQ-EACESCRCLHGKSVCIRH--CPE-LSCAQGEViMQEPGSCCPIC 5063
Cdd:smart00214    1 CVHNGRVYNDGETWKpDPCQICTCLDGTTVLCDPveCPPpPDCPNPER-VKPPGECCPRC 59
TOC159_MAD pfam11886
Translocase of chloroplast 159/132, membrane anchor domain; This is the membrane-anchor domain ...
 300-350 7.34e-03

Translocase of chloroplast 159/132, membrane anchor domain; This is the membrane-anchor domain of translocase of chloroplast 159, TOC159/132. This domain is present in plants at the C-terminus of the GTPase, AIG1, pfam04548, and anchors the GTPas region to the outer membrane of the chloroplast. The domain may carry a very C-terminal sequence motif that resembles a transit peptide.


Pssm-ID: 432163  Cd Length: 267  Bit Score: 41.88  E-value: 7.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720417875  300 EVSVKGQPVPVGEPQLLHGMS-LQWQGDwLVLSGGLGVVVRLDRSSSISISV 350
Cdd:pfam11886  180 EATLRGKDYPVRQDQSTLGLSlMSWRGD-LVLGGNLQSQFRVGRGTKMAVRA 230
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3051-3089 8.37e-03

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.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 37.26  E-value: 8.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720417875 3051 AWSSWTPCSVPCGGGYRNRT-------QGSGPHSPI--EFSTCSLQPC 3089
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPEllERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4948-5006 8.72e-03

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.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 37.37  E-value: 8.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417875 4948 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 5006
Cdd:pfam01826    1 CPANEVYSECG-SACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
3420-3458 9.27e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.40  E-value: 9.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1720417875 3420 PWSKWTACSQPCRGQTRTRSRACVCPAPqhGGSPCPEES 3458
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDD 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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