|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
449-694 |
1.51e-85 |
|
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. :
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 268.76 E-value: 1.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 605
Cdd:cd00190 67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 606 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 685
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223
|
....*....
gi 21264357 686 HNKDWIQRV 694
Cdd:cd00190 224 SYLDWIQKT 232
|
|
| CUB |
pfam00431 |
CUB domain; |
185-294 |
5.91e-39 |
|
CUB domain; :
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 139.35 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:pfam00431 77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
28-137 |
2.44e-30 |
|
CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast. :
Pssm-ID: 238001 [Multi-domain] Cd Length: 113 Bit Score: 115.20 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041 10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
|
90 100 110
....*....|....*....|....*....|....
gi 21264357 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041 83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
301-362 |
1.67e-11 |
|
Sushi repeat (SCR repeat); :
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.82 E-value: 1.67e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
153-181 |
1.62e-08 |
|
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442. :
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 50.70 E-value: 1.62e-08
10 20
....*....|....*....|....*....
gi 21264357 153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 super family |
cl31493 |
EEV host range protein; Provisional |
300-433 |
1.60e-06 |
|
EEV host range protein; Provisional The actual alignment was detected with superfamily member PHA02639:
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 50.43 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 21264357 380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
449-694 |
1.51e-85 |
|
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 268.76 E-value: 1.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 605
Cdd:cd00190 67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 606 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 685
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223
|
....*....
gi 21264357 686 HNKDWIQRV 694
Cdd:cd00190 224 SYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
448-691 |
6.42e-83 |
|
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 261.84 E-value: 6.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 448 RIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRlRSD 527
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--------------DPSNIRVRLGSHDL-SSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 528 ENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQ--EGAMVIVSGWGKQFL--QRFPETLME 603
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEgaGSLPDTLQE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 604 IEIPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNrerGQWYLVGTVSWGDDCGKKDRYGVYSY 683
Cdd:smart00020 146 VNVPIVSNATCRRAY-SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTR 221
|
....*...
gi 21264357 684 IHHNKDWI 691
Cdd:smart00020 222 VSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
449-691 |
3.26e-71 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 230.79 E-value: 3.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqsldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS----------------GASDVKVVLGAHNIVLREG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGKQFLQRFPETLMEIEI 606
Cdd:pfam00089 65 GEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 607 PIVDHSTCQKAYaplKKKVTRDMICAGekEGGKDACAGDSGGPMVTLNRergqwYLVGTVSWGDDCGKKDRYGVYSYIHH 686
Cdd:pfam00089 145 PVVSRETCRSAY---GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSS 214
|
....*
gi 21264357 687 NKDWI 691
Cdd:pfam00089 215 YLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
447-697 |
1.44e-64 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 214.51 E-value: 1.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 447 ARIFNGRPAQKGTTPWIAMLSHLNG--QPFCGGSLLGSSWIVTAAHCLhqsldpedptlrdsDLLSPSDFKIILGKHwRL 524
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCV--------------DGDGPSDLRVVIGST-DL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 525 RSDENEQHlGVKHTTLHPQYDPNTFENDVALVELlESPVlnAFVMPICLPEGPQQ--EGAMVIVSGWGK--QFLQRFPET 600
Cdd:COG5640 94 STSGGTVV-KVARIVVHPDYDPATPGNDIALLKL-ATPV--PGVAPAPLATSADAaaPGTPATVAGWGRtsEGPGSQSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 601 LMEIEIPIVDHSTCQkAYAPLkkkVTRDMICAGEKEGGKDACAGDSGGPMVtlNRERGQWYLVGTVSWGDDCGKKDRYGV 680
Cdd:COG5640 170 LRKADVPVVSDATCA-AYGGF---DGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGV 243
|
250
....*....|....*..
gi 21264357 681 YSYIHHNKDWIQRVTGV 697
Cdd:COG5640 244 YTRVSAYRDWIKSTAGG 260
|
|
| CUB |
pfam00431 |
CUB domain; |
185-294 |
5.91e-39 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 139.35 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:pfam00431 77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
185-296 |
1.22e-35 |
|
CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.
Pssm-ID: 238001 [Multi-domain] Cd Length: 113 Bit Score: 130.22 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRA 296
Cdd:cd00041 78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
195-294 |
2.41e-31 |
|
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 117.88 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
|
90 100
....*....|....*....|....*
gi 21264357 270 TQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:smart00042 78 SSSNSLTLTFVSDSSVQKRGFSARY 102
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
28-137 |
2.44e-30 |
|
CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.
Pssm-ID: 238001 [Multi-domain] Cd Length: 113 Bit Score: 115.20 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041 10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
|
90 100 110
....*....|....*....|....*....|....
gi 21264357 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041 83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
29-135 |
6.80e-30 |
|
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 113.64 E-value: 6.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
|
90 100 110
....*....|....*....|....*....|.
gi 21264357 105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042 74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
|
|
| CUB |
pfam00431 |
CUB domain; |
23-135 |
1.89e-22 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 92.74 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431 4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 21264357 99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431 80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
301-362 |
1.67e-11 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.82 E-value: 1.67e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
301-363 |
5.68e-11 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 58.24 E-value: 5.68e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 363
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
301-362 |
1.24e-10 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 57.15 E-value: 1.24e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSST------ITCLENGTWSPPPPTC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
153-181 |
1.62e-08 |
|
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 50.70 E-value: 1.62e-08
10 20
....*....|....*....|....*....
gi 21264357 153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
300-433 |
1.60e-06 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 50.43 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 21264357 380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
139-181 |
5.35e-05 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 40.69 E-value: 5.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 21264357 139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179 1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
|
|
| PHA02954 |
PHA02954 |
EEV membrane glycoprotein; Provisional |
279-382 |
1.77e-04 |
|
EEV membrane glycoprotein; Provisional
Pssm-ID: 165263 [Multi-domain] Cd Length: 317 Bit Score: 44.31 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
|
90 100
....*....|....*....|....
gi 21264357 359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
139-176 |
1.97e-04 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 39.16 E-value: 1.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 21264357 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054 1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
449-694 |
1.51e-85 |
|
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 268.76 E-value: 1.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 605
Cdd:cd00190 67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 606 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 685
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223
|
....*....
gi 21264357 686 HNKDWIQRV 694
Cdd:cd00190 224 SYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
448-691 |
6.42e-83 |
|
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 261.84 E-value: 6.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 448 RIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpedptlrdsdllSPSDFKIILGKHWRlRSD 527
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--------------DPSNIRVRLGSHDL-SSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 528 ENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQ--EGAMVIVSGWGKQFL--QRFPETLME 603
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEgaGSLPDTLQE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 604 IEIPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNrerGQWYLVGTVSWGDDCGKKDRYGVYSY 683
Cdd:smart00020 146 VNVPIVSNATCRRAY-SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTR 221
|
....*...
gi 21264357 684 IHHNKDWI 691
Cdd:smart00020 222 VSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
449-691 |
3.26e-71 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 230.79 E-value: 3.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 449 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqsldpedptlrdsdllSPSDFKIILGKHWRLRSDE 528
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS----------------GASDVKVVLGAHNIVLREG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 529 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGKQFLQRFPETLMEIEI 606
Cdd:pfam00089 65 GEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 607 PIVDHSTCQKAYaplKKKVTRDMICAGekEGGKDACAGDSGGPMVTLNRergqwYLVGTVSWGDDCGKKDRYGVYSYIHH 686
Cdd:pfam00089 145 PVVSRETCRSAY---GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSS 214
|
....*
gi 21264357 687 NKDWI 691
Cdd:pfam00089 215 YLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
447-697 |
1.44e-64 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 214.51 E-value: 1.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 447 ARIFNGRPAQKGTTPWIAMLSHLNG--QPFCGGSLLGSSWIVTAAHCLhqsldpedptlrdsDLLSPSDFKIILGKHwRL 524
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCV--------------DGDGPSDLRVVIGST-DL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 525 RSDENEQHlGVKHTTLHPQYDPNTFENDVALVELlESPVlnAFVMPICLPEGPQQ--EGAMVIVSGWGK--QFLQRFPET 600
Cdd:COG5640 94 STSGGTVV-KVARIVVHPDYDPATPGNDIALLKL-ATPV--PGVAPAPLATSADAaaPGTPATVAGWGRtsEGPGSQSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 601 LMEIEIPIVDHSTCQkAYAPLkkkVTRDMICAGEKEGGKDACAGDSGGPMVtlNRERGQWYLVGTVSWGDDCGKKDRYGV 680
Cdd:COG5640 170 LRKADVPVVSDATCA-AYGGF---DGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGV 243
|
250
....*....|....*..
gi 21264357 681 YSYIHHNKDWIQRVTGV 697
Cdd:COG5640 244 YTRVSAYRDWIKSTAGG 260
|
|
| CUB |
pfam00431 |
CUB domain; |
185-294 |
5.91e-39 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 139.35 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:pfam00431 77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
185-296 |
1.22e-35 |
|
CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.
Pssm-ID: 238001 [Multi-domain] Cd Length: 113 Bit Score: 130.22 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 21264357 261 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRA 296
Cdd:cd00041 78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
195-294 |
2.41e-31 |
|
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 117.88 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
|
90 100
....*....|....*....|....*
gi 21264357 270 TQSHSVLILFHSDNSGENRGWRLSY 294
Cdd:smart00042 78 SSSNSLTLTFVSDSSVQKRGFSARY 102
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
28-137 |
2.44e-30 |
|
CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.
Pssm-ID: 238001 [Multi-domain] Cd Length: 113 Bit Score: 115.20 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041 10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
|
90 100 110
....*....|....*....|....*....|....
gi 21264357 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041 83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
29-135 |
6.80e-30 |
|
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 113.64 E-value: 6.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
|
90 100 110
....*....|....*....|....*....|.
gi 21264357 105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042 74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
|
|
| CUB |
pfam00431 |
CUB domain; |
23-135 |
1.89e-22 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 92.74 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431 4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 21264357 99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431 80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
301-362 |
1.67e-11 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.82 E-value: 1.67e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
301-363 |
5.68e-11 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 58.24 E-value: 5.68e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 363
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
301-362 |
1.24e-10 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 57.15 E-value: 1.24e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264357 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 362
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSST------ITCLENGTWSPPPPTC 56
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
463-681 |
4.43e-10 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 59.69 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 463 IAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqslDPEDPTLrdsdllsPSDFKIILGkhwrlRSDENEQHLGVKHTTLHP 542
Cdd:COG3591 2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVY---DGAGGGW-------ATNIVFVPG-----YNGGPYGTATATRFRVPP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 543 QYDPNT-FENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVS---GWGKQFLQRFPETLMEIEIPIVDHSTcqkay 618
Cdd:COG3591 67 GWVASGdAGYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGypgDRPKDLSLDCSGRVTGVQGNRLSYDC----- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264357 619 aplkkkvtrdmicagekeggkDACAGDSGGPMvtLNRERGQWYLVGTVSWGDdcGKKDRYGVY 681
Cdd:COG3591 142 ---------------------DTTGGSSGSPV--LDDSDGGGRVVGVHSAGG--ADRANTGVR 179
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
153-181 |
1.62e-08 |
|
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 50.70 E-value: 1.62e-08
10 20
....*....|....*....|....*....
gi 21264357 153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
300-433 |
1.60e-06 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 50.43 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 21264357 380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
139-181 |
5.35e-05 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 40.69 E-value: 5.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 21264357 139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179 1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
|
|
| PHA02817 |
PHA02817 |
EEV Host range protein; Provisional |
347-432 |
5.44e-05 |
|
EEV Host range protein; Provisional
Pssm-ID: 165167 [Multi-domain] Cd Length: 225 Bit Score: 44.93 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 347 IECLKDGTWSNKIPTCKIVDCRAPGeLEHGLITFSTRNNLTTYKSEIKYSCQEPYykmLNNNTGIYTCSAQGVWMNKVlg 426
Cdd:PHA02817 69 IICEKDGKWNKEFPVCKIIRCRFPA-LQNGFVNGIPDSKKFYYESEVSFSCKPGF---VLIGTKYSVCGINSSWIPKV-- 142
|
....*.
gi 21264357 427 rslPTC 432
Cdd:PHA02817 143 ---PIC 145
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
289-450 |
1.24e-04 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 44.26 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 289 GWRLSYRAAGNECPELQPPVHGKIEPSQAKyfFKDQVLVSCDTGYKVLKDNveMDTFQIECLKDGTWSNKIPTCKIVDCR 368
Cdd:PHA02927 74 GWTLFNQCIKRRCPSPRDIDNGQLDIGGVD--FGSSITYSCNSGYQLIGES--KSYCELGSTGSMVWNPEAPICESVKCQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 369 APGELEHGliTFSTRNNLTTYKSEIKYSCQEPYykMLNNNTGIyTCSAqGVWMNKvlgrslPTCLPV-CGLPKFSRKLMA 447
Cdd:PHA02927 150 SPPSISNG--RHNGYEDFYTDGSVVTYSCNSGY--SLIGNSGV-LCSG-GEWSDP------PTCQIVkCPHPTISNGYLS 217
|
...
gi 21264357 448 RIF 450
Cdd:PHA02927 218 SGF 220
|
|
| PHA02954 |
PHA02954 |
EEV membrane glycoprotein; Provisional |
279-382 |
1.77e-04 |
|
EEV membrane glycoprotein; Provisional
Pssm-ID: 165263 [Multi-domain] Cd Length: 317 Bit Score: 44.31 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
|
90 100
....*....|....*....|....
gi 21264357 359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
139-176 |
1.97e-04 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 39.16 E-value: 1.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 21264357 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054 1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
139-171 |
5.34e-03 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 34.91 E-value: 5.34e-03
10 20 30
....*....|....*....|....*....|....*
gi 21264357 139 DVDECkerEDEELSCDH--YCHNYIGGYYCSCRFG 171
Cdd:pfam07645 1 DVDEC---ATGTHNCPAntVCVNTIGSFECRCPDG 32
|
|
| vWA_Matrilin |
cd01475 |
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
121-180 |
5.93e-03 |
|
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.
Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 38.91 E-value: 5.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264357 121 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 180
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
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|
|