|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
449-711 |
1.44e-80 |
|
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: 256.45 E-value: 1.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDVRDK 528
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGisnpnvtvdeIISS 608
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsqRWVVQGLVSWGG 688
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
|
250 260
....*....|....*....|...
gi 21264359 689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
|
|
| CUB |
pfam00431 |
CUB domain; |
185-294 |
7.76e-39 |
|
CUB domain; :
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 139.35 E-value: 7.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 21264359 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 |
3.75e-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: 114.82 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041 10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
|
90 100 110
....*....|....*....|....*....|....
gi 21264359 104 qEVVLSPGSFMSITFRSDFSNeeRFTGFDAHYMA 137
Cdd:cd00041 83 -PPIISSGNSLTVRFRSDSSV--TGRGFKATYSA 113
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
301-362 |
1.79e-11 |
|
Sushi repeat (SCR repeat); :
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.82 E-value: 1.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359 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 |
8.28e-09 |
|
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: 51.47 E-value: 8.28e-09
10 20
....*....|....*....|....*....
gi 21264359 153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 super family |
cl31493 |
EEV host range protein; Provisional |
300-433 |
1.33e-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: 50.82 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 21264359 380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
449-711 |
1.44e-80 |
|
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: 256.45 E-value: 1.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDVRDK 528
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGisnpnvtvdeIISS 608
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsqRWVVQGLVSWGG 688
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
|
250 260
....*....|....*....|...
gi 21264359 689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
450-711 |
3.51e-79 |
|
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: 252.97 E-value: 3.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 450 IIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDV-RDK 528
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSL------QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---------YTVRLGSHDLsSNE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGISNPNVtvdeiiss 608
Cdd:cd00190 66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS-SGYNLPAGTTCTVSGWGRTSEGG-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 gtrTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGg 688
Cdd:cd00190 137 ---PLPDVLQEVNVPIVSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWG- 207
|
250 260
....*....|....*....|...
gi 21264359 689 pEECGSKQVYGVYTKVSNYVDWV 711
Cdd:cd00190 208 -SGCARPNYPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
450-711 |
1.18e-59 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 200.36 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 450 IIGGRNAEPGLFPWQALIVVEdtsrvpNDKWFGSGALLSASWILTAAHVLRSQRRdttvipvskehVTVYLGLHDVRDKS 529
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASD-----------VKVVLGAHNIVLRE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 530 GAVNS-SAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMlGLVAGWGISNPNVTvdeiiss 608
Cdd:pfam00089 64 GGEQKfDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT-CTVSGWGNTKTLGP------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 gtrtlSDVLQYVKLPVVPHAECKTSYesrsgNYSVTENMFCAGYyeGGKDTCLGDSGGAFVifdDLSQRwvVQGLVSWGG 688
Cdd:pfam00089 136 -----SDTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLV---CSDGE--LIGIVSWGY 198
|
250 260
....*....|....*....|...
gi 21264359 689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:pfam00089 199 G--CASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
449-716 |
1.25e-57 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 196.41 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIVVEDTSRvpndKWFGSGALLSASWILTAAHvlrsqrrdtTVIPVSKEHVTVYLGLHDVRDK 528
Cdd:COG5640 30 AIVGGTPATVGEYPWMVALQSSNGPS----GQFCGGTLIAPRWVLTAAH---------CVDGDGPSDLRVVIGSTDLSTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVnSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLgphVMPVCLPRlEPEGPAPHMLGLVAGWGIsnpnvtvdeiISS 608
Cdd:COG5640 97 GGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLAT-SADAAAPGTPATVAGWGR----------TSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECktsyesRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGG 688
Cdd:COG5640 162 GPGSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG--GGWVLVGVVSWGG 233
|
250 260
....*....|....*....|....*...
gi 21264359 689 pEECGsKQVYGVYTKVSNYVDWVWEQMG 716
Cdd:COG5640 234 -GPCA-AGYPGVYTRVSAYRDWIKSTAG 259
|
|
| CUB |
pfam00431 |
CUB domain; |
185-294 |
7.76e-39 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 139.35 E-value: 7.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 21264359 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 |
1.95e-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: 129.84 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 21264359 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 |
3.04e-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: 117.49 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
|
90 100
....*....|....*....|....*
gi 21264359 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 |
3.75e-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: 114.82 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041 10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
|
90 100 110
....*....|....*....|....*....|....
gi 21264359 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 |
8.41e-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: 113.25 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
|
90 100 110
....*....|....*....|....*....|.
gi 21264359 105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042 74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
|
|
| CUB |
pfam00431 |
CUB domain; |
23-135 |
2.15e-22 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 92.74 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431 4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 21264359 99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431 80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
301-362 |
1.79e-11 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.82 E-value: 1.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359 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 |
6.10e-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: 6.10e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264359 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 |
1.22e-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: 1.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359 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 |
8.28e-09 |
|
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: 51.47 E-value: 8.28e-09
10 20
....*....|....*....|....*....
gi 21264359 153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
300-433 |
1.33e-06 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 50.82 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 21264359 380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
139-181 |
2.61e-05 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 41.85 E-value: 2.61e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 21264359 139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179 1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
139-176 |
1.06e-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: 39.93 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 21264359 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054 1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
|
|
| PHA02954 |
PHA02954 |
EEV membrane glycoprotein; Provisional |
279-382 |
2.07e-04 |
|
EEV membrane glycoprotein; Provisional
Pssm-ID: 165263 [Multi-domain] Cd Length: 317 Bit Score: 43.92 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
|
90 100
....*....|....*....|....
gi 21264359 359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
449-711 |
1.44e-80 |
|
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: 256.45 E-value: 1.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDVRDK 528
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGisnpnvtvdeIISS 608
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsqRWVVQGLVSWGG 688
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
|
250 260
....*....|....*....|...
gi 21264359 689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
450-711 |
3.51e-79 |
|
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: 252.97 E-value: 3.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 450 IIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTtvipvskehVTVYLGLHDV-RDK 528
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSL------QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---------YTVRLGSHDLsSNE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPAPHMLGLVAGWGISNPNVtvdeiiss 608
Cdd:cd00190 66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS-SGYNLPAGTTCTVSGWGRTSEGG-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 gtrTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGg 688
Cdd:cd00190 137 ---PLPDVLQEVNVPIVSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWG- 207
|
250 260
....*....|....*....|...
gi 21264359 689 pEECGSKQVYGVYTKVSNYVDWV 711
Cdd:cd00190 208 -SGCARPNYPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
450-711 |
1.18e-59 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 200.36 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 450 IIGGRNAEPGLFPWQALIVVEdtsrvpNDKWFGSGALLSASWILTAAHVLRSQRRdttvipvskehVTVYLGLHDVRDKS 529
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASD-----------VKVVLGAHNIVLRE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 530 GAVNS-SAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMlGLVAGWGISNPNVTvdeiiss 608
Cdd:pfam00089 64 GGEQKfDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT-CTVSGWGNTKTLGP------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 gtrtlSDVLQYVKLPVVPHAECKTSYesrsgNYSVTENMFCAGYyeGGKDTCLGDSGGAFVifdDLSQRwvVQGLVSWGG 688
Cdd:pfam00089 136 -----SDTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLV---CSDGE--LIGIVSWGY 198
|
250 260
....*....|....*....|...
gi 21264359 689 PeeCGSKQVYGVYTKVSNYVDWV 711
Cdd:pfam00089 199 G--CASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
449-716 |
1.25e-57 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 196.41 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 449 RIIGGRNAEPGLFPWQALIVVEDTSRvpndKWFGSGALLSASWILTAAHvlrsqrrdtTVIPVSKEHVTVYLGLHDVRDK 528
Cdd:COG5640 30 AIVGGTPATVGEYPWMVALQSSNGPS----GQFCGGTLIAPRWVLTAAH---------CVDGDGPSDLRVVIGSTDLSTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 529 SGAVnSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLgphVMPVCLPRlEPEGPAPHMLGLVAGWGIsnpnvtvdeiISS 608
Cdd:COG5640 97 GGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLAT-SADAAAPGTPATVAGWGR----------TSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 609 GTRTLSDVLQYVKLPVVPHAECktsyesRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDlsQRWVVQGLVSWGG 688
Cdd:COG5640 162 GPGSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG--GGWVLVGVVSWGG 233
|
250 260
....*....|....*....|....*...
gi 21264359 689 pEECGsKQVYGVYTKVSNYVDWVWEQMG 716
Cdd:COG5640 234 -GPCA-AGYPGVYTRVSAYRDWIKSTAG 259
|
|
| CUB |
pfam00431 |
CUB domain; |
185-294 |
7.76e-39 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 139.35 E-value: 7.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 260
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 21264359 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 |
1.95e-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: 129.84 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 185 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 260
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 21264359 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 |
3.04e-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: 117.49 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 195 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 269
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
|
90 100
....*....|....*....|....*
gi 21264359 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 |
3.75e-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: 114.82 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 28 FGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGRETTdteqtpg 103
Cdd:cd00041 10 SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydgpSTSSPLLGRFCGSTLP------- 82
|
90 100 110
....*....|....*....|....*....|....
gi 21264359 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 |
8.41e-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: 113.25 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 29 GQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdteqtPGQ 104
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydgpSASSPLLGRFCGSE-------APP 73
|
90 100 110
....*....|....*....|....*....|.
gi 21264359 105 EVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:smart00042 74 PVISSSSNSLTLTFVSDSSVQKR--GFSARY 102
|
|
| CUB |
pfam00431 |
CUB domain; |
23-135 |
2.15e-22 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 92.74 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 23 ELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKV----ETEDQVLATFCGREttdt 98
Cdd:pfam00431 4 VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdgpSASSPLLGRFCGSG---- 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 21264359 99 eqtpGQEVVLSPGSFMSITFRSDFSNEERftGFDAHY 135
Cdd:pfam00431 80 ----IPEDIVSSSNQMTIKFVSDASVQKR--GFKATY 110
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
301-362 |
1.79e-11 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.82 E-value: 1.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359 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 |
6.10e-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: 6.10e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264359 301 CPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 363
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
476-690 |
8.68e-11 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 61.62 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 476 PNDKWFGSGALLSASWILTAAHVLRSQRRDTTVipvskEHVTVYLGlhdvRDKSGAVNSSAARVVLHPDFNIQ-NYNHDI 554
Cdd:COG3591 8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWA-----TNIVFVPG----YNGGPYGTATATRFRVPPGWVASgDAGYDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 555 ALVQLQEPVPlgphvmpvclprlEPEGPAPhmlglvagwgisnpnVTVDEIISSGTRTlsDVLQYvklpvvPHAECKTSY 634
Cdd:COG3591 79 ALLRLDEPLG-------------DTTGWLG---------------LAFNDAPLAGEPV--TIIGY------PGDRPKDLS 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21264359 635 ESRSGN-YSVTENMFcagYYEGgkDTCLGDSGGAfvIFDDLSQRWVVQGLVSWGGPE 690
Cdd:COG3591 123 LDCSGRvTGVQGNRL---SYDC--DTTGGSSGSP--VLDDSDGGGRVVGVHSAGGAD 172
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
301-362 |
1.22e-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: 1.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21264359 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 |
8.28e-09 |
|
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: 51.47 E-value: 8.28e-09
10 20
....*....|....*....|....*....
gi 21264359 153 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 181
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
300-433 |
1.33e-06 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 50.82 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 300 ECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLIT 379
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 21264359 380 FSTRNNLTTYKSEIKYSCQEPYYKMLNNNTgiyTCSAQGVWMNkvlgrSLPTCL 433
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
139-181 |
2.61e-05 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 41.85 E-value: 2.61e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 21264359 139 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 181
Cdd:smart00179 1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
289-440 |
5.17e-05 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 45.80 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 289 GWRLSYRAAGNECPELQPPVHGKIEPSQAKyfFKDQVLVSCDTGYKVLKDNveMDTFQIECLKDGTWSNKIPTCKIVDCR 368
Cdd:PHA02927 74 GWTLFNQCIKRRCPSPRDIDNGQLDIGGVD--FGSSITYSCNSGYQLIGES--KSYCELGSTGSMVWNPEAPICESVKCQ 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21264359 369 APGELEHGliTFSTRNNLTTYKSEIKYSCQEPYykMLNNNTGIyTCSAqGVWMNKvlgrslPTC-LPECGQPS 440
Cdd:PHA02927 150 SPPSISNG--RHNGYEDFYTDGSVVTYSCNSGY--SLIGNSGV-LCSG-GEWSDP------PTCqIVKCPHPT 210
|
|
| PHA02817 |
PHA02817 |
EEV Host range protein; Provisional |
347-432 |
5.31e-05 |
|
EEV Host range protein; Provisional
Pssm-ID: 165167 [Multi-domain] Cd Length: 225 Bit Score: 45.32 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 347 IECLKDGTWSNKIPTCKIVDCRAPGeLEHGLITFSTRNNLTTYKSEIKYSCQEPYykmLNNNTGIYTCSAQGVWMNKVlg 426
Cdd:PHA02817 69 IICEKDGKWNKEFPVCKIIRCRFPA-LQNGFVNGIPDSKKFYYESEVSFSCKPGF---VLIGTKYSVCGINSSWIPKV-- 142
|
....*.
gi 21264359 427 rslPTC 432
Cdd:PHA02817 143 ---PIC 145
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
139-176 |
1.06e-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: 39.93 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 21264359 139 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 176
Cdd:cd00054 1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
|
|
| PHA02954 |
PHA02954 |
EEV membrane glycoprotein; Provisional |
279-382 |
2.07e-04 |
|
EEV membrane glycoprotein; Provisional
Pssm-ID: 165263 [Multi-domain] Cd Length: 317 Bit Score: 43.92 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 279 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVemdtfqIECLKDgTWsNK 358
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
|
90 100
....*....|....*....|....
gi 21264359 359 IPTCKiVDCRAPgELEHGLITFST 382
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
139-171 |
3.37e-03 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 35.68 E-value: 3.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 21264359 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 |
6.23e-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: 6.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 121 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 180
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
309-420 |
8.69e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 38.88 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21264359 309 HGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMdtfqieCLKD---GTWSNKIPTCKIVDCRAPGELEHGLITfstrNN 385
Cdd:PHA02639 30 NGFITELMEKYEIGKLIEYTCNTDYALIGDRFRT------CIKDknnAIWSNKAPFCMLKECNDPPSIINGKIY----NK 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 21264359 386 LTTYK--SEIKYSCQEP---YYKMLNNNTgiYTCSAQGVW 420
Cdd:PHA02639 100 REMYKvgDEIYYVCNEHkgvQYSLVGNEK--ITCIQDKSW 137
|
|
|