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Conserved domains on  [gi|568941753|ref|XP_006506132|]
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SCO-spondin isoform X5 [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 ...
 1017-1166 1.71e-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: 1.71e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  1017 CQASGAPHYVTFDGLVFTFPGACEYLLVREAGGR--FSVSVQNLPCGASGL-TCTKALVVRLDSTVVHMLRGQAVTVNGV 1093
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdFSFSVTNKNCNGGASgVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753  1094 SIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQGV 1166
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 556-716 4.94e-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: 4.94e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    556 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 633
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    634 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 711
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 568941753    712 LTPAG 716
Cdd:smart00216  159 RTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 192-341 2.15e-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: 2.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    192 SATCATWSGFHYQTFDGHHYHFLGQCTYLLAGAMDS--TWAVHLRPSVHCPQHRHCWLVQVVMGPEEVLIQDGEVSVKGQ 269
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSepTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941753    270 PVPVGEPQLLHGMSLQWQ--GDWLVLSGGLGVV-VRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 341
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRssGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
FA58C super family cl25480
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2105-2225 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 568941753 2105 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2181
Cdd:cd00057    31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568941753 2182 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2225
Cdd:cd00057   106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 754-826 3.83e-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: 3.83e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753    754 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 826
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1202-1275 2.84e-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: 2.84e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   1202 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1275
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2528-2580 6.67e-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: 6.67e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   2528 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2580
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3225-3277 8.06e-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: 8.06e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3225 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3277
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4237-4288 3.15e-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: 3.15e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   4237 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4288
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 396-468 4.31e-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: 4.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941753   396 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 468
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2688-2737 5.89e-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: 5.89e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568941753   2688 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 2737
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2957-3008 2.32e-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: 2.32e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   2957 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3008
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1700-1751 3.39e-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: 3.39e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   1700 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 1751
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
2804-2852 1.14e-08

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 1.14e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  2804 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2852
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1566-1602 4.77e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 4.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568941753  1566 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1602
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1419-1453 9.17e-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: 9.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1453
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 829-882 1.76e-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: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  829 CPGGQVYQECAPVCGHHCGEPE---DCKElgICVAGCNCPPGLLWDLEGQCVPPSMC 882
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNappPCTK--QCVEGCFCPEGYVRNSGGKCVPPSQC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3618-3662 5.32e-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: 5.32e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   3618 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3662
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3795-3847 5.37e-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: 5.37e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3795 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3847
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1379-1414 7.68e-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: 7.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568941753 1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1414
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1278-1334 7.75e-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: 7.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  1278 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 1334
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 472-527 8.63e-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: 8.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  472 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 527
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3285-3335 1.14e-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: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568941753 3285 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 3335
Cdd:cd19941     3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4043-4098 1.65e-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: 1.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  4043 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4098
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4754-4803 1.71e-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: 1.71e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   4754 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 4803
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4805-4859 2.61e-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: 2.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753  4805 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4859
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3930-3983 3.56e-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: 3.56e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   3930 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 3983
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3060-3112 5.25e-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: 46.61  E-value: 5.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753  3060 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3112
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2434-2468 5.61e-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: 5.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2468
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 ...
 3375-3421 7.09e-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: 7.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568941753  3375 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3421
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3988-4040 1.12e-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: 1.12e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3988 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 4040
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2602-2645 1.21e-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: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568941753 2602 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2645
Cdd:cd19941    11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1815-1871 1.29e-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: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 1815 CFGELVFRTCAP-CPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1871
Cdd:cd19941     1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4407-4462 1.69e-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: 45.00  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753 4407 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4462
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4664-4710 2.84e-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: 2.84e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  4664 DCANQCPRSCADLWDGVQCLqGPCSPGCRCPPGQLVQ-DGHCVPISSC 4710
Cdd:pfam01826    9 ECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2377-2411 4.67e-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: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2377 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2411
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4143-4193 5.05e-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: 5.05e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   4143 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 4193
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2238-2272 7.41e-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: 7.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2272
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3156-3219 8.75e-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: 8.75e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753   3156 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 3219
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1455-1489 9.29e-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: 9.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1455 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1489
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 ...
 2471-2522 1.07e-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: 1.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  2471 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 2522
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3499-3555 2.44e-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: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  3499 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3555
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4602-4650 4.10e-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: 4.10e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   4602 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4650
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1495-1526 7.09e-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: 7.09e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1495 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1526
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2917-2964 7.39e-04

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214565  Cd Length: 67  Bit Score: 41.01  E-value: 7.39e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753   2917 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 2964
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3864-3912 1.16e-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: 1.16e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   3864 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 3912
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2856-2915 1.71e-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: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568941753 2856 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2915
Cdd:cd19941     1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3445-3489 2.46e-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: 2.46e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568941753   3445 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 3489
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4352-4403 4.80e-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: 4.80e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   4352 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4403
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1915-1968 5.84e-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: 5.84e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   1915 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 1968
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 ...
 4971-5026 7.11e-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: 7.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  4971 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5026
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 ...
 3014-3052 8.50e-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: 8.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  3014 AWSSWTPCSVPCGGGYRNRT-------QGSGPHSPI--EFSTCSLQPC 3052
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPEllERRPCNLPPC 52
TIL super family cl20226
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4911-4969 9.40e-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: 9.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568941753  4911 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 4969
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 ...
 1017-1166 1.71e-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: 1.71e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  1017 CQASGAPHYVTFDGLVFTFPGACEYLLVREAGGR--FSVSVQNLPCGASGL-TCTKALVVRLDSTVVHMLRGQAVTVNGV 1093
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdFSFSVTNKNCNGGASgVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753  1094 SIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQGV 1166
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1006-1165 2.88e-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: 125.21  E-value: 2.88e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   1006 WHCTGQRCSGWCQASGAPHYVTFDGLVFTFPGACEYLLVREA--GGRFSVSVQNLPCGaSGLTCTKALVVRLDSTVVHML 1083
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   1084 RGQ-AVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGLTL-LWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLR 1161
Cdd:smart00216   80 DDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQvTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159


                    ....
gi 568941753   1162 SRQG 1165
Cdd:smart00216  160 TPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 556-716 4.94e-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: 4.94e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    556 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 633
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    634 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 711
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 568941753    712 LTPAG 716
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 567-716 2.44e-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: 2.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   567 CAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACD---TGSCLHALSVFLGNTHIQLRYSGAVLVD 642
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGT--CTYVLAKDcSEEPDFSFSVTNKNCNggaSGVCLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   643 GEDVDLP-WIGVEGFNISWASSTFLLLHwPGAWVLW-GVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDFLTPAG 716
Cdd:pfam00094   79 GQKVSLPyKSDGGEVEILGSGFVVVDLS-PGVGLQVdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 192-341 2.15e-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: 2.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    192 SATCATWSGFHYQTFDGHHYHFLGQCTYLLAGAMDS--TWAVHLRPSVHCPQHRHCWLVQVVMGPEEVLIQDGEVSVKGQ 269
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSepTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941753    270 PVPVGEPQLLHGMSLQWQ--GDWLVLSGGLGVV-VRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 341
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRssGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 195-341 1.20e-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: 94.36  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   195 CATWSGFHYQTFDGHHYHFLGQCTYLLA----GAMDSTWAVHLRPsVHCPQHRHCW-LVQVVMGPEEVLIQDG-EVSVKG 268
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAkdcsEEPDFSFSVTNKN-CNGGASGVCLkSVTVIVGDLEITLQKGgTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   269 QPVPVgePQLLHGMSLQ--WQGDWLV-LSGGLGVVVRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 341
Cdd:pfam00094   80 QKVSL--PYKSDGGEVEilGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2105-2225 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 568941753 2105 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2181
Cdd:cd00057    31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568941753 2182 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2225
Cdd:cd00057   106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 754-826 3.83e-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: 3.83e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753    754 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 826
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1202-1275 2.84e-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: 2.84e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   1202 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1275
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2528-2580 6.67e-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: 6.67e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   2528 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2580
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1207-1274 8.22e-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: 8.22e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  1207 RCEVIL-QPIFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELC 1274
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.
 2114-2223 3.87e-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: 3.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  2114 WH----TQPLYLQLDLRRPRNLTGIIVQ-RAGSSAAYVSTLSLQFSSDNLQWHNYVNSLSSTlsppkpspeSSNHMAPEV 2188
Cdd:pfam00754   26 WSawsgDDPQWIQVDLGKPKKITGVVTQgRQDGSNGYVTSYKIEYSLDGENWTTVKDEKIPG---------NNDNNTPVT 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568941753  2189 WTFDQMVQARYIRVWPhsghLRDNNQHDIFLWVEL 2223
Cdd:pfam00754   97 NTFDPPIKARYVRIVP----TSWNGGNGIALRAEL 127
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2070-2226 2.92e-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: 2.92e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   2070 CYSPLGLAGLPMWAPSQH--WEHITRADPVEApmagpgpregasAEWH----TQPLYLQLDLRRPRNLTGIIVQRAGSSA 2143
Cdd:smart00231    2 CNEPLGLESDSQITASSSywAAKIARLNGGSD------------GGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   2144 AYVsTLSLQFSSDNLQWHNYVNSLSSTLSPPKpspessNHMAPEVWTFDQMVQARYIRVWPHSGHlrdnnqHDIFLWVEL 2223
Cdd:smart00231   70 DWV-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN------GNIILRVEL 136


                    ...
gi 568941753   2224 LGC 2226
Cdd:smart00231  137 LGC 139
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3225-3277 8.06e-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: 8.06e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3225 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3277
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 763-825 1.37e-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: 1.37e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753   763 ILHGHAFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLC 825
Cdd:pfam08742    5 LSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4237-4288 3.15e-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: 3.15e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   4237 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4288
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 396-468 4.31e-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: 4.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941753   396 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 468
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2688-2737 5.89e-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: 5.89e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568941753   2688 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 2737
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2530-2579 1.28e-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: 1.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  2530 EWGPWTACSVSCGGGHQSRQRScVDPPPKNGGAPCPgPSHEKAPCNLQLC 2579
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRT-VIVEPQNGGRPCP-ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2957-3008 2.32e-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: 2.32e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   2957 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3008
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1700-1751 3.39e-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: 3.39e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   1700 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 1751
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
2804-2852 1.14e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 1.14e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  2804 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2852
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2803-2852 1.32e-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: 53.74  E-value: 1.32e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   2803 WGLWASWSTCSASCNGGIQTRGRSCSGSAPGNP--VCLGPHTQTRDCNMHPC 2852
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
3226-3276 1.51e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 1.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941753  3226 SPWSPWSGCSRSCGGGLRSRTRACDQPSPQglGDFCEGPQAQGEACQAQPC 3276
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1566-1602 4.77e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 4.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568941753  1566 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1602
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1419-1453 9.17e-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: 9.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1453
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 829-882 1.76e-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: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  829 CPGGQVYQECAPVCGHHCGEPE---DCKElgICVAGCNCPPGLLWDLEGQCVPPSMC 882
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNappPCTK--QCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 829-882 1.87e-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: 1.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753   829 CPGGQVYQECAPVCGHHCGEPE-DCKELGICVAGCNCPPGLLWDLEGQCVPPSMC 882
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 390-468 2.13e-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: 2.13e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    390 QAQAQDMCHQLL--EGPFWQCHGQVQPDEYHETCLFAYCVGatagngpEGQLEAVCATFANYAQACARQHIYVH-WRKPG 466
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCAC-------GGDCECLCDALAAYAAACAEAGVCISpWRTPT 73


                    ..
gi 568941753    467 FC 468
Cdd:smart00832   74 FC 75
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1568-1602 2.59e-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: 2.59e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1568 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1602
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP_1 pfam00090
Thrombospondin type 1 domain;
4238-4288 4.75e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.34  E-value: 4.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941753  4238 TLWSSWSYCSVSCGGGSQVRTRSCtvSAPPHGSLSCEGPDTQTRHCGQQLC 4288
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTC--KSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3618-3662 5.32e-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: 5.32e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   3618 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3662
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3795-3847 5.37e-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: 5.37e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3795 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3847
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1379-1414 7.68e-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: 7.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568941753 1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1414
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1278-1334 7.75e-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: 7.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  1278 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 1334
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 472-527 8.63e-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: 8.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  472 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 527
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3285-3335 1.14e-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: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568941753 3285 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 3335
Cdd:cd19941     3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 472-527 1.32e-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: 1.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   472 CPGGQLYSDCVSSCPPSCSAVAQGEEgsCGKECVSGCECPTGLFWD-GALCVPAAHC 527
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV--CPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4043-4098 1.65e-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: 1.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  4043 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4098
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4754-4803 1.71e-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: 1.71e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   4754 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 4803
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1278-1334 2.05e-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: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 1278 CEGGQVYEPCGSTCPPTCHDHHSELRwhCqVITCVEGCFCPEGTLLH-GGACMKLAAC 1334
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP--C-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1419-1450 2.15e-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: 46.86  E-value: 2.15e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDE 1450
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4805-4859 2.61e-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: 2.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753  4805 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4859
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1568-1599 3.09e-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: 3.09e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1568 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDE 1599
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 4752-4802 3.33e-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: 3.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568941753  4752 VLGPWSAWSECSAVCGKGTMVRHRSCEEHPDR--EPCQalDLQQWQECNLQAC 4802
Cdd:pfam19028    2 VVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNggRPCP--ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3930-3983 3.56e-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: 3.56e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   3930 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 3983
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTG---EDVETRACNEQPCP 53
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3060-3112 5.25e-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: 46.61  E-value: 5.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753  3060 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3112
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2434-2468 5.61e-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: 5.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2468
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3285-3335 6.38e-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: 46.23  E-value: 6.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568941753  3285 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGAiCVKPSYC 3335
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 ...
 3375-3421 7.09e-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: 7.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568941753  3375 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3421
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42
TSP_1 pfam00090
Thrombospondin type 1 domain;
3619-3662 9.28e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 9.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  3619 SSWGPWEKCSVSCGGGEQLRSRQCARP-----PCPGLAQQSRICHIHVC 3662
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPfpggePCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3988-4040 1.12e-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: 1.12e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3988 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 4040
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2602-2645 1.21e-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: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568941753 2602 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2645
Cdd:cd19941    11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2955-3008 1.23e-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: 1.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568941753  2955 CGWSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAfGGAECqGPNLDAEFCSLRPC 3008
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1815-1871 1.29e-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: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 1815 CFGELVFRTCAP-CPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1871
Cdd:cd19941     1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4043-4098 1.57e-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: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753 4043 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4098
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQ--CVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4407-4462 1.69e-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: 45.00  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753 4407 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4462
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1379-1411 2.13e-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: 2.13e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 568941753   1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDE 1411
Cdd:smart00192    2 CPPGEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4664-4710 2.84e-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: 2.84e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  4664 DCANQCPRSCADLWDGVQCLqGPCSPGCRCPPGQLVQ-DGHCVPISSC 4710
Cdd:pfam01826    9 ECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1701-1755 3.02e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.35  E-value: 3.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753 1701 GSWGPWAPCSQTCGSGTRSRNR-----NCSTsslqvlqncpglqHQSQACFTEACPVDGE 1755
Cdd:PTZ00441  241 GPWDEWTPCSVTCGKGTHSRSRpilheGCTT-------------HMVEECEEEECPVEPE 287
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2377-2411 4.67e-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: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2377 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2411
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4143-4193 5.05e-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: 5.05e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   4143 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 4193
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4805-4859 5.70e-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: 43.46  E-value: 5.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753 4805 CPPGQVLSTCATMCPSLCSHLWPGTICVrEPCQLGCGCPGGQLL-YNGTCIPPEAC 4859
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCT-KQCVEGCFCPEGYVRnSGGKCVPPSQC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2238-2272 7.41e-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: 7.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2272
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3156-3219 8.75e-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: 8.75e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753   3156 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 3219
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1455-1489 9.29e-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: 9.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1455 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1489
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1419-1453 1.05e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.24  E-value: 1.05e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568941753  1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1453
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2471-2522 1.07e-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: 1.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  2471 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 2522
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2602-2645 1.07e-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: 1.07e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568941753  2602 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLLQ-DSHCLPLSEC 2645
Cdd:pfam01826   11 GSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
2689-2734 1.18e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.41  E-value: 1.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568941753  2689 SAWSPWTACDRSCGSGVRARFRSPTNPPVafGGSPCEGDRQELQAC 2734
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1820-1871 1.34e-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: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568941753  1820 VFRTCA-PCPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1871
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 ...
 1701-1750 2.36e-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: 2.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  1701 GSWGPWAPCSQTCGSGTRSRNRNCSTSSLQVLQNCPGLQhQSQACFTEAC 1750
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELL-ERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3381-3421 2.41e-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: 2.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 568941753   3381 WCPWSKWTACSQPCRGQTRTRSRACVCPAPQHGGSPCPEES 3421
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGED 41
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3499-3555 2.44e-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: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  3499 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3555
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4407-4462 2.83e-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: 2.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  4407 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4462
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGfVRNSGGKCVPPSDC 55
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2238-2272 3.87e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.69  E-value: 3.87e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568941753  2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2272
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4602-4650 4.10e-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: 4.10e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   4602 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4650
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2434-2468 5.74e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 5.74e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568941753  2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2468
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2434-2465 5.88e-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: 5.88e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDE 2465
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1495-1526 7.09e-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: 7.09e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1495 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1526
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2917-2964 7.39e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 41.01  E-value: 7.39e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753   2917 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 2964
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4664-4710 8.50e-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: 8.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568941753 4664 DCANQCPRSCADLWDGVQCLQgPCSPGCRCPPGQ-LVQDGHCVPISSC 4710
Cdd:cd19941     9 ECGSACPPTCANPNAPPPCTK-QCVEGCFCPEGYvRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3060-3112 9.11e-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: 9.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753 3060 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLL-LNNVCVPVQDC 3112
Cdd:cd19941     1 CPPNEVYSECGSAcPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
3795-3846 1.12e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  3795 GPWGMWSLCSRSCGGlGTRTRTRQCVLPtlAPGGLSCRGPLQDLEYCFSPEC 3846
Cdd:pfam00090    1 SPWSPWSPCSVTCGK-GIQVRQRTCKSP--FPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3864-3912 1.16e-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: 1.16e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   3864 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 3912
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 3935-3982 1.17e-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: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  3935 PWEPCSRSCGVGQQRRL----RAYHPPGPGGHWCpDILTAYQERRFCNLRAC 3982
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLvqcvQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1495-1526 1.23e-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: 39.11  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568941753 1495 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1526
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1379-1414 1.43e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568941753  1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1414
Cdd:pfam00057    3 CSPNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2856-2915 1.71e-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: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568941753 2856 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2915
Cdd:cd19941     1 CPPNEVYSE---C---GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2377-2408 1.95e-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: 1.95e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   2377 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDE 2408
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP_1 pfam00090
Thrombospondin type 1 domain;
4603-4649 2.05e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.94  E-value: 2.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  4603 GPWGPWSPCQMPCSGGFKLRWRV--ARDTSAGECPGPWAQTESCNMGSC 4649
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTckSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3445-3489 2.46e-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: 2.46e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568941753   3445 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 3489
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1455-1486 2.81e-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: 2.81e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1455 CPHGSLACADGRCLPPALLCNGHPDCLDAADE 1486
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3499-3555 4.19e-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: 4.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 3499 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3555
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPC---TKQCVEGCFCPEGYvRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2238-2269 4.54e-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: 4.54e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDE 2269
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4352-4403 4.80e-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: 4.80e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   4352 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4403
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1915-1968 5.84e-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: 5.84e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   1915 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 1968
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 4971-5026 7.11e-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: 7.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  4971 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5026
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDDGKVLCDKiICPPLDCPNPRLE-IPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
4971-5026 7.31e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.88  E-value: 7.31e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   4971 CWHHGSPHLPGSEWQ-EACESCRCLHGKSVCIRH--CPE-LSCAQGEViMQEPGSCCPIC 5026
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 ...
 3014-3052 8.50e-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: 8.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  3014 AWSSWTPCSVPCGGGYRNRT-------QGSGPHSPI--EFSTCSLQPC 3052
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPEllERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4911-4969 9.40e-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: 9.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568941753  4911 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 4969
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 ...
 1017-1166 1.71e-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: 1.71e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  1017 CQASGAPHYVTFDGLVFTFPGACEYLLVREAGGR--FSVSVQNLPCGASGL-TCTKALVVRLDSTVVHMLRGQAVTVNGV 1093
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdFSFSVTNKNCNGGASgVCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753  1094 SIRLPKVYTGPGLSLHHAGLFLLLTTRLGL-TLLWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLRSRQGV 1166
Cdd:pfam00094   81 KVSLPYKSDGGEVEILGSGFVVVDLSPGVGlQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1006-1165 2.88e-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: 125.21  E-value: 2.88e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   1006 WHCTGQRCSGWCQASGAPHYVTFDGLVFTFPGACEYLLVREA--GGRFSVSVQNLPCGaSGLTCTKALVVRLDSTVVHML 1083
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   1084 RGQ-AVTVNGVSIRLPKVYTGPGLSLHHAGLFLLLTTRLGLTL-LWDGGTRVLVQLSPHFHGRVAGLCGNFDSDASNDLR 1161
Cdd:smart00216   80 DDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQvTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159


                    ....
gi 568941753   1162 SRQG 1165
Cdd:smart00216  160 TPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 556-716 4.94e-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: 4.94e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    556 WHCAQALCPAECAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACDTG-SCLHALSVFLGNTHIQL 633
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGN--CYYVLAQDcSSEPTFSVLLKNVPCGGGaTCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    634 RYSG-AVLVDGEDVDLPWI-GVEGFNISWASSTFLLLHWPGAWVLWGVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDF 711
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 568941753    712 LTPAG 716
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 567-716 2.44e-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: 2.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   567 CAVGGDGHYFTFDGRSFFFRGTpgCHYSLVQD-SVKGQLLVVLEHGACD---TGSCLHALSVFLGNTHIQLRYSGAVLVD 642
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGT--CTYVLAKDcSEEPDFSFSVTNKNCNggaSGVCLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   643 GEDVDLP-WIGVEGFNISWASSTFLLLHwPGAWVLW-GVAEPAAYITLDPRHAYQVQGLCGTFTWKQQDDFLTPAG 716
Cdd:pfam00094   79 GQKVSLPyKSDGGEVEILGSGFVVVDLS-PGVGLQVdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 192-341 2.15e-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: 2.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    192 SATCATWSGFHYQTFDGHHYHFLGQCTYLLAGAMDS--TWAVHLRPSVHCPQHRHCWLVQVVMGPEEVLIQDGEVSVKGQ 269
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSepTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKVTVN 88

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941753    270 PVPVGEPQLLHGMSLQWQ--GDWLVLSGGLGVV-VRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 341
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRssGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 195-341 1.20e-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: 94.36  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   195 CATWSGFHYQTFDGHHYHFLGQCTYLLA----GAMDSTWAVHLRPsVHCPQHRHCW-LVQVVMGPEEVLIQDG-EVSVKG 268
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAkdcsEEPDFSFSVTNKN-CNGGASGVCLkSVTVIVGDLEITLQKGgTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   269 QPVPVgePQLLHGMSLQ--WQGDWLV-LSGGLGVVVRLDRSSSISISVDHEFWGRTQGLCGLYNGRPEDDFVEPGG 341
Cdd:pfam00094   80 QKVSL--PYKSDGGEVEilGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2105-2225 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 568941753 2105 GPREGA-SAEWHTQPLYLQLDLRRPRNLTGIIVQRA--GSSAAYVSTLSLQFSSDNLQWHNYVNslsstLSPPKPSPESS 2181
Cdd:cd00057    31 LNSDNAwTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEWVTSYKVQYSLDGETWTTYKD-----KGEEKVFTGNS 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568941753 2182 NHMAPEVWTFDQMVQARYIRVWPHSghlrdnNQHDIFLWVELLG 2225
Cdd:cd00057   106 DGSTPVTNDFPPPIVARYIRILPTT------WNGNISLRLELYG 143
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 754-826 3.83e-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: 3.83e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753    754 LTFTEAACAILHGH--AFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLCP 826
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1202-1275 2.84e-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: 2.84e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   1202 NWARARCEVILQP--IFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELCP 1275
Cdd:smart00832    2 YYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2528-2580 6.67e-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: 6.67e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   2528 WAEWGPWTACSVSCGGGHQSRQRSCVDPPPKNGGAPCPGPSHEKAPCNLQLCP 2580
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1207-1274 8.22e-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: 8.22e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  1207 RCEVIL-QPIFAPCHTEVPPQQYYEWCVYDACGCdtGGDCECLCSAIATYADECARHRHHVR-WRSQELC 1274
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.
 2114-2223 3.87e-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: 3.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753  2114 WH----TQPLYLQLDLRRPRNLTGIIVQ-RAGSSAAYVSTLSLQFSSDNLQWHNYVNSLSSTlsppkpspeSSNHMAPEV 2188
Cdd:pfam00754   26 WSawsgDDPQWIQVDLGKPKKITGVVTQgRQDGSNGYVTSYKIEYSLDGENWTTVKDEKIPG---------NNDNNTPVT 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568941753  2189 WTFDQMVQARYIRVWPhsghLRDNNQHDIFLWVEL 2223
Cdd:pfam00754   97 NTFDPPIKARYVRIVP----TSWNGGNGIALRAEL 127
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2070-2226 2.92e-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: 2.92e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   2070 CYSPLGLAGLPMWAPSQH--WEHITRADPVEApmagpgpregasAEWH----TQPLYLQLDLRRPRNLTGIIVQRAGSSA 2143
Cdd:smart00231    2 CNEPLGLESDSQITASSSywAAKIARLNGGSD------------GGWCpaknDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   2144 AYVsTLSLQFSSDNLQWHNYVNSLSSTLSPPKpspessNHMAPEVWTFDQMVQARYIRVWPHSGHlrdnnqHDIFLWVEL 2223
Cdd:smart00231   70 DWV-TYKLEYSDDGVNWTTYKDGNSKVFPGNS------DAGTVVLNDFPPPIVARYVRILPTGWN------GNIILRVEL 136


                    ...
gi 568941753   2224 LGC 2226
Cdd:smart00231  137 LGC 139
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3225-3277 8.06e-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: 8.06e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3225 WSPWSPWSGCSRSCGGGLRSRTRACDQPSPQGLGDFCEGPQAQGEACQAQPCP 3277
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 763-825 1.37e-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: 1.37e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753   763 ILHGHAFQECHGLVDREPFRLRCLEAVCGCAPGRDCLCPVLSAYTRHCAQEGVLLQ-WRNETLC 825
Cdd:pfam08742    5 LSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4237-4288 3.15e-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: 3.15e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   4237 WTLWSSWSYCSVSCGGGSQVRTRSCTVSAPPHGSLSCEGPDTQTRHCGQQLC 4288
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 396-468 4.31e-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: 4.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941753   396 MCHQLL-EGPFWQCHGQVQPDEYHETCLFAYCvgatagnGPEGQLEAVCATFANYAQACARQHIYV-HWRKPGFC 468
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMC-------SCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2688-2737 5.89e-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: 5.89e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568941753   2688 WSAWSPWTACDRSCGSGVRARFRSPTNPPVAFGGSPCEGDRQELQACYTD 2737
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2530-2579 1.28e-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: 1.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  2530 EWGPWTACSVSCGGGHQSRQRScVDPPPKNGGAPCPgPSHEKAPCNLQLC 2579
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRT-VIVEPQNGGRPCP-ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2957-3008 2.32e-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: 2.32e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   2957 WSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAFGGAECQGPNLDAEFCSLRPC 3008
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
2530-2579 3.12e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.50  E-value: 3.12e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  2530 EWGPWTACSVSCGGGHQSRQRSCVDPPPknGGAPCPGPSHEKAPCNLQLC 2579
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1700-1751 3.39e-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: 3.39e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   1700 WGSWGPWAPCSQTCGSGTRSRNRNC-STSSLQVLQNCPGLQHQSQACFTEACP 1751
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
2804-2852 1.14e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 1.14e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  2804 GLWASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2852
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 2803-2852 1.32e-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: 53.74  E-value: 1.32e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   2803 WGLWASWSTCSASCNGGIQTRGRSCSGSAPGNP--VCLGPHTQTRDCNMHPC 2852
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
3226-3276 1.51e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 1.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941753  3226 SPWSPWSGCSRSCGGGLRSRTRACDQPSPQglGDFCEGPQAQGEACQAQPC 3276
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1566-1602 4.77e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 4.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568941753  1566 SPCSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1602
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1419-1453 9.17e-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: 9.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1453
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 829-882 1.76e-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: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  829 CPGGQVYQECAPVCGHHCGEPE---DCKElgICVAGCNCPPGLLWDLEGQCVPPSMC 882
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNappPCTK--QCVEGCFCPEGYVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 829-882 1.87e-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: 1.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753   829 CPGGQVYQECAPVCGHHCGEPE-DCKELGICVAGCNCPPGLLWDLEGQCVPPSMC 882
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSpPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 390-468 2.13e-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: 2.13e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753    390 QAQAQDMCHQLL--EGPFWQCHGQVQPDEYHETCLFAYCVGatagngpEGQLEAVCATFANYAQACARQHIYVH-WRKPG 466
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCAC-------GGDCECLCDALAAYAAACAEAGVCISpWRTPT 73


                    ..
gi 568941753    467 FC 468
Cdd:smart00832   74 FC 75
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1568-1602 2.59e-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: 2.59e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1568 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDELDC 1602
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP_1 pfam00090
Thrombospondin type 1 domain;
4238-4288 4.75e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.34  E-value: 4.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941753  4238 TLWSSWSYCSVSCGGGSQVRTRSCtvSAPPHGSLSCEGPDTQTRHCGQQLC 4288
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTC--KSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3618-3662 5.32e-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: 5.32e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   3618 WSSWGPWEKCSVSCGGGEQLRSRQCARPP-------CPGLAQQSRICHIHVC 3662
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3795-3847 5.37e-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: 5.37e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3795 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLAPGGLSCRGPLQDLEYCFSPECP 3847
Cdd:smart00209    2 SEWSEWSPCSVTCGG-GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1379-1414 7.68e-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: 7.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568941753 1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1414
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1278-1334 7.75e-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: 7.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  1278 CEGGQVYEPCGSTCPPTCHDHHSELrwHCQVItCVEGCFCPEGTLLH-GGACMKLAAC 1334
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD--VCPEP-CVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 472-527 8.63e-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: 8.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  472 CPGGQLYSDCVSSCPPSCSAVAQGEegSCGKECVSGCECPTGLFWD-GALCVPAAHC 527
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPP--PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3285-3335 1.14e-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: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568941753 3285 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGaICVKPSYC 3335
Cdd:cd19941     3 PNEVYSECGSACPPTCANPnapPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 472-527 1.32e-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: 1.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   472 CPGGQLYSDCVSSCPPSCSAVAQGEEgsCGKECVSGCECPTGLFWD-GALCVPAAHC 527
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV--CPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4043-4098 1.65e-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: 1.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  4043 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4098
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRNSGGkCVPPSDC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4754-4803 1.71e-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: 1.71e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   4754 GPWSAWSECSAVCGKGTMVRHRSCEEHP---DREPCQALDLQQwQECNLQACP 4803
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPpqnGGGPCTGEDVET-RACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1278-1334 2.05e-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: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 1278 CEGGQVYEPCGSTCPPTCHDHHSELRwhCqVITCVEGCFCPEGTLLH-GGACMKLAAC 1334
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPP--C-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1419-1450 2.15e-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: 46.86  E-value: 2.15e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDE 1450
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4805-4859 2.61e-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: 2.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753  4805 CPPGQVLSTCATMCPSLCSHLWPGTICvREPCQLGCGCPGGQLL-YNGTCIPPEAC 4859
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1568-1599 3.09e-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: 3.09e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1568 CSLLEFQCNSGECTPRGWRCDQEEDCTDGSDE 1599
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 4752-4802 3.33e-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: 3.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568941753  4752 VLGPWSAWSECSAVCGKGTMVRHRSCEEHPDR--EPCQalDLQQWQECNLQAC 4802
Cdd:pfam19028    2 VVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNggRPCP--ELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3930-3983 3.56e-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: 3.56e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753   3930 WTSWAPWEPCSRSCGVGQQRRLRAY--HPPGPGGHWCPDiltAYQERRFCNLRACP 3983
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 ...
 3226-3276 3.64e-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: 3.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941753  3226 SPWSPWSGCSRSCGGGLRSRTRACDQPsPQGLGDFCeGPQAQGEACQAQPC 3276
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3060-3112 5.25e-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: 46.61  E-value: 5.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753  3060 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLLLNN-VCVPVQDC 3112
Cdd:pfam01826    1 CPANEVYSECGSAcPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2434-2468 5.61e-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: 5.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2468
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3285-3335 6.38e-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: 46.23  E-value: 6.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568941753  3285 EGAEYSPCGPPCPRSCDDL---VHCVWRCQPGCYCPLGKVLSADGAiCVKPSYC 3335
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 ...
 3375-3421 7.09e-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: 7.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568941753  3375 CQVSgdwcPWSKWTACSQPCRGQTRTRSRACVCPaPQHGGSPCPEES 3421
Cdd:pfam19028    1 CVVS----EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL 42
TSP_1 pfam00090
Thrombospondin type 1 domain;
3619-3662 9.28e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 9.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  3619 SSWGPWEKCSVSCGGGEQLRSRQCARP-----PCPGLAQQSRICHIHVC 3662
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPfpggePCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
4754-4802 9.37e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.49  E-value: 9.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  4754 GPWSAWSECSAVCGKGTMVRHRSCE-EHPDREPCqALDLQQWQECNLQAC 4802
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 ...
 4240-4288 9.99e-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: 9.99e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  4240 WSSWSYCSVSCGGGSQVRTRSCTVsAPPHGSLSCeGPDTQTRHCGQQLC 4288
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIV-EPQNGGRPC-PELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3988-4040 1.12e-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: 1.12e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   3988 WSHWSPWSWCDRSCGGGRSLRSRSCSSPPPKNGGTSCVGERHHVRPCNPMPCE 4040
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2602-2645 1.21e-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: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568941753 2602 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLL-QDSHCLPLSEC 2645
Cdd:cd19941    11 GSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2955-3008 1.23e-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: 1.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568941753  2955 CGWSPWTPWSPCSQSCNVGIRRRFRAGTEPPAAfGGAECqGPNLDAEFCSLRPC 3008
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1815-1871 1.29e-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: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 1815 CFGELVFRTCAP-CPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1871
Cdd:cd19941     1 CPPNEVYSECGSaCPPTCANPNAPPPCT--KQCV-EGCFCPEGYVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4043-4098 1.57e-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: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753 4043 CPAGMEMVSCANHCPYSCSDLQEGGMCQEDqaCQLGCRCSEGFLEQDGG-CVPVGHC 4098
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQ--CVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4407-4462 1.69e-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: 45.00  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753 4407 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4462
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGyVRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1379-1411 2.13e-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: 2.13e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 568941753   1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDE 1411
Cdd:smart00192    2 CPPGEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4664-4710 2.84e-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: 2.84e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  4664 DCANQCPRSCADLWDGVQCLqGPCSPGCRCPPGQLVQ-DGHCVPISSC 4710
Cdd:pfam01826    9 ECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1701-1755 3.02e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.35  E-value: 3.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753 1701 GSWGPWAPCSQTCGSGTRSRNR-----NCSTsslqvlqncpglqHQSQACFTEACPVDGE 1755
Cdd:PTZ00441  241 GPWDEWTPCSVTCGKGTHSRSRpilheGCTT-------------HMVEECEEEECPVEPE 287
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2377-2411 4.67e-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: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2377 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDEQHC 2411
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4143-4193 5.05e-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: 5.05e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   4143 WSHWSAWSSCSHSCGpQGQQSRFRSSTSGSWAL---ECQKEQSQSQPCPEVPCP 4193
Cdd:smart00209    1 WSEWSEWSPCSVTCG-GGVQTRTRSCCSPPPQNgggPCTGEDVETRACNEQPCP 53
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4805-4859 5.70e-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: 43.46  E-value: 5.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568941753 4805 CPPGQVLSTCATMCPSLCSHLWPGTICVrEPCQLGCGCPGGQLL-YNGTCIPPEAC 4859
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCT-KQCVEGCFCPEGYVRnSGGKCVPPSQC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 2238-2272 7.41e-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: 7.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2272
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3156-3219 8.75e-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: 8.75e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941753   3156 WSSWTPWSVCSASCNPARRHRHRFCARPPHRAPFSlvllttvaapttLCPGPEAEEEPCLLPGC 3219
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG------------PCTGEDVETRACNEQPC 52
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1455-1489 9.29e-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: 9.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568941753 1455 CPHGSLACADGRCLPPALLCNGHPDCLDAADEESC 1489
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1419-1453 1.05e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.24  E-value: 1.05e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568941753  1419 CGEGQMSCQSGHCLPLSLICDGQDDCGDGTDEQGC 1453
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2471-2522 1.07e-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: 1.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  2471 CVLAPWSGWSDCSRSCGLGLIFQHRELLRLPLPGGSCLLDQFRSQSCFVQAC 2522
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 2806-2852 1.07e-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: 1.07e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568941753  2806 WASWSTCSASCNGGIQTRGRSCSGSAPGNPVCLGPHTQTRDCNMHPC 2852
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELLERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2602-2645 1.07e-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: 1.07e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568941753  2602 VPPCPPSCLDPEANRSCSGHCMEGCRCPPGLLLQ-DSHCLPLSEC 2645
Cdd:pfam01826   11 GSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
2689-2734 1.18e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.41  E-value: 1.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568941753  2689 SAWSPWTACDRSCGSGVRARFRSPTNPPVafGGSPCEGDRQELQAC 2734
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1820-1871 1.34e-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: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568941753  1820 VFRTCA-PCPLTCDDISGQAACPpdRPCSsPGCWCPDGKVLNTEGQCVRPRQC 1871
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 ...
 2686-2737 1.83e-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: 1.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  2686 CGWSAWSPWTACDRSCGSGVRARFRSPTNPPvAFGGSPCeGDRQELQACYTD 2737
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTVIVEP-QNGGRPC-PELLERRPCNLP 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
2958-3008 1.86e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 1.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568941753  2958 SPWTPWSPCSQSCNVGIRRRFRAGTEPPAafGGAECQGPNLDAEFCSLRPC 3008
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 ...
 1701-1750 2.36e-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: 2.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  1701 GSWGPWAPCSQTCGSGTRSRNRNCSTSSLQVLQNCPGLQhQSQACFTEAC 1750
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELL-ERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3381-3421 2.41e-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: 2.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 568941753   3381 WCPWSKWTACSQPCRGQTRTRSRACVCPAPQHGGSPCPEES 3421
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGED 41
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3499-3555 2.44e-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: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  3499 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3555
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC---PEPCVEGCVCPPGFvRNSGGKCVPPSDC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3619-3662 2.56e-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: 2.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568941753  3619 SSWGPWEKCSVSCGGGEQLRSRQCARPP------CPGLaQQSRICHIHVC 3662
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPqnggrpCPEL-LERRPCNLPPC 52
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4407-4462 2.83e-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: 2.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  4407 CPPPFEFQSCGSPCAGLCATHLNHRLCQDlpPCQPGCYCPKG-LLEQAGSCILPEQC 4462
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGfVRNSGGKCVPPSDC 55
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2238-2272 3.87e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.69  E-value: 3.87e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568941753  2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDEEGC 2272
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4602-4650 4.10e-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: 4.10e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568941753   4602 WGPWGPWSPCQMPCSGGFKLRWRV----ARDTSAGECPGPWAQTESCNMGSCP 4650
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSccspPPQNGGGPCTGEDVETRACNEQPCP 53
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
2434-2468 5.74e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 5.74e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568941753  2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDEDNC 2468
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2434-2465 5.88e-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: 5.88e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   2434 CSPSQLRCGSGECLPFEHRCDLQVNCQDGSDE 2465
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1495-1526 7.09e-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: 7.09e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1495 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1526
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2917-2964 7.39e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 41.01  E-value: 7.39e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753   2917 CQLHGQLYAPGAVAHLDCNNCTCISGEMVCTSKRCPVA----------CGWSPWTPWS 2964
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKpcllhnlsgeCPLGQGCVPS 58
TSP_1 pfam00090
Thrombospondin type 1 domain;
1703-1750 7.57e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 40.48  E-value: 7.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  1703 WGPWAPCSQTCGSGTRSRNRNCStSSLQVLQNCPGLQHQSQACFTEAC 1750
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCK-SPFPGGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 2532-2579 8.21e-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: 8.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  2532 GPWTACSVSCGGGHQSRQRSCVDPPPK--NGGAPCPGPS--HEKAPCNLQLC 2579
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKkpPETQSCNLKPC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4664-4710 8.50e-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: 8.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568941753 4664 DCANQCPRSCADLWDGVQCLQgPCSPGCRCPPGQ-LVQDGHCVPISSC 4710
Cdd:cd19941     9 ECGSACPPTCANPNAPPPCTK-QCVEGCFCPEGYvRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3060-3112 9.11e-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: 9.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568941753 3060 CPEDQQWLDCAQG-PASCAHLSIPGEANQTCHPGCYCLSGMLL-LNNVCVPVQDC 3112
Cdd:cd19941     1 CPPNEVYSECGSAcPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
3795-3846 1.12e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  3795 GPWGMWSLCSRSCGGlGTRTRTRQCVLPtlAPGGLSCRGPLQDLEYCFSPEC 3846
Cdd:pfam00090    1 SPWSPWSPCSVTCGK-GIQVRQRTCKSP--FPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3864-3912 1.16e-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: 1.16e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753   3864 WGPWSPWSPCSHSCTDpahpAWRSRTRLCL--------ANCTvGDSSQERPCNLPSC 3912
Cdd:smart00209    1 WSEWSEWSPCSVTCGG----GVQTRTRSCCspppqnggGPCT-GEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 3935-3982 1.17e-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: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  3935 PWEPCSRSCGVGQQRRL----RAYHPPGPGGHWCpDILTAYQERRFCNLRAC 3982
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLvqcvQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1495-1526 1.23e-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: 39.11  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568941753 1495 CISGEVSCVDGTCVRTIQLCDGVWDCPDGADE 1526
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1379-1414 1.43e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568941753  1379 CAEGETLCReNGHCVPLEWLCDNQDDCGDGSDEEGC 1414
Cdd:pfam00057    3 CSPNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 3795-3846 1.58e-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: 1.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753  3795 GPWGMWSLCSRSCGGlGTRTRTRQCVLPTLApGGLSCrGPLQDLEYCFSPEC 3846
Cdd:pfam19028    4 SEWSEWSECSVTCGG-GVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2856-2915 1.71e-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: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568941753 2856 CPGNMVFRSaeqCleeGGPCPQLCLAQDPGVECTGSCAPSCNCPPGLFLH-NASCLPRSQC 2915
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 ...
 3928-3982 1.76e-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: 1.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941753  3928 CFWTSWAPWEPCSRSCGVGQQRRLRA--YHPPGpGGHWCPDILtayqERRFCNLRAC 3982
Cdd:pfam19028    1 CVVSEWSEWSECSVTCGGGVQTRTRTviVEPQN-GGRPCPELL----ERRPCNLPPC 52
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2377-2408 1.95e-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: 1.95e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   2377 CGPGQVPCDVLGCVEQEQLCDGREDCLDGSDE 2408
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP_1 pfam00090
Thrombospondin type 1 domain;
4603-4649 2.05e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.94  E-value: 2.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568941753  4603 GPWGPWSPCQMPCSGGFKLRWRV--ARDTSAGECPGPWAQTESCNMGSC 4649
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTckSPFPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 3445-3489 2.46e-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: 2.46e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568941753   3445 WSPWGPWSSCDA-C-LGQSYRSRVCSHPPISDGGKPCLGGYQQSRPC 3489
Cdd:smart00209    1 WSEWSEWSPCSVtCgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1455-1486 2.81e-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: 2.81e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   1455 CPHGSLACADGRCLPPALLCNGHPDCLDAADE 1486
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3499-3555 4.19e-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: 4.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753 3499 CGGGQDLLPCGQPCPHSCQDLSLGSTCqpgSAGCQSGCGCPPGQ-LSQDGLCVFPVDC 3555
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPC---TKQCVEGCFCPEGYvRNSGGKCVPPSQC 55
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 2238-2269 4.54e-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: 4.54e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568941753   2238 CPGSRHRCASGECAPKGGPCDGAVDCDDGSDE 2269
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 4352-4403 4.80e-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: 4.80e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   4352 WGDWSSWTRCS--CKVLVQQRYRHQVPAPGQAGeGTPCTRLDGHFRPCTIGNCS 4403
Cdd:smart00209    1 WSEWSEWSPCSvtCGGGVQTRTRSCCSPPPQNG-GGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1915-1968 5.84e-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: 5.84e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 568941753   1915 WSSWSPWAECLGPCSSQSlQWSFRSPNNPRLSGHGRQCRGIHRKARRCQTEACE 1968
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGV-QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 4971-5026 7.11e-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: 7.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941753  4971 CWHHGSPHLPGSEWQEA-CESCRCLHGKSVCIR-HCPELSCAQGEVImQEPGSCCPIC 5026
Cdd:pfam00093    1 CVQNGVVYENGETWKPDlCTICTCDDGKVLCDKiICPPLDCPNPRLE-IPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
4971-5026 7.31e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.88  E-value: 7.31e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941753   4971 CWHHGSPHLPGSEWQ-EACESCRCLHGKSVCIRH--CPE-LSCAQGEViMQEPGSCCPIC 5026
Cdd:smart00214    1 CVHNGRVYNDGETWKpDPCQICTCLDGTTVLCDPveCPPpPDCPNPER-VKPPGECCPRC 59
TOC159_MAD pfam11886
Translocase of chloroplast 159/132, membrane anchor domain; This is the membrane-anchor domain ...
 263-313 7.38e-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: 7.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568941753   263 EVSVKGQPVPVGEPQLLHGMS-LQWQGDwLVLSGGLGVVVRLDRSSSISISV 313
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 ...
 3014-3052 8.50e-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: 8.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568941753  3014 AWSSWTPCSVPCGGGYRNRT-------QGSGPHSPI--EFSTCSLQPC 3052
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTrtvivepQNGGRPCPEllERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
3383-3421 9.33e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.40  E-value: 9.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568941753  3383 PWSKWTACSQPCRGQTRTRSRACVCPAPqhGGSPCPEES 3421
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDD 38
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4911-4969 9.40e-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: 9.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568941753  4911 CAPGEIWQHGKlGPCEKTCPEMNmtqAWSNCTEAQAPGCVCQLGYFRSQTGLCVPEDHC 4969
Cdd:pfam01826    1 CPANEVYSECG-SACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
 
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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