|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
336-598 |
1.04e-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: 253.75 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 336 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSESWILTAAHVLRSQRRDTtvipvskeyVTVYLGLHDVRDK 415
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPSPYMLGLVAGWGisnpnvtvdeIISS 495
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsqRWMVQGLVSWGG 575
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
|
250 260
....*....|....*....|...
gi 795477829 576 PeeCGSKQVYGVYTKVSNYVDWV 598
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
|
|
| CUB |
pfam00431 |
CUB domain; |
72-181 |
5.15e-39 |
|
CUB domain;
:
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 138.97 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 72 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 147
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 795477829 148 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 181
Cdd:pfam00431 77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
188-249 |
1.75e-11 |
|
Sushi repeat (SCR repeat);
:
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.44 E-value: 1.75e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 249
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
40-68 |
1.17e-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: 1.17e-08
10 20
....*....|....*....|....*....
gi 795477829 40 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 68
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 super family |
cl31493 |
EEV host range protein; Provisional |
187-320 |
7.45e-07 |
|
EEV host range protein; Provisional
The actual alignment was detected with superfamily member PHA02639:
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 51.20 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 187 ECPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLVT 266
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 795477829 267 FSTRNNLTTYKSEIRYSCQEPYYKMLNNITgiyTCSAQGVWMNkvlgrSLPTCL 320
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| vWFA super family |
cl00057 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
8-67 |
5.09e-03 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
The actual alignment was detected with superfamily member cd01475:
Pssm-ID: 469594 [Multi-domain] Cd Length: 224 Bit Score: 38.91 E-value: 5.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 8 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 67
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
336-598 |
1.04e-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: 253.75 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 336 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSESWILTAAHVLRSQRRDTtvipvskeyVTVYLGLHDVRDK 415
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPSPYMLGLVAGWGisnpnvtvdeIISS 495
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsqRWMVQGLVSWGG 575
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
|
250 260
....*....|....*....|...
gi 795477829 576 PeeCGSKQVYGVYTKVSNYVDWV 598
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
337-598 |
7.72e-80 |
|
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: 251.81 E-value: 7.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 337 IIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSESWILTAAHVLRSQRRDTtvipvskeyVTVYLGLHDV-RDK 415
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSL------QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---------YTVRLGSHDLsSNE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPSPYMLGLVAGWGISNPNVtvdeiiss 495
Cdd:cd00190 66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS-SGYNLPAGTTCTVSGWGRTSEGG-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 gtrTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsQRWMVQGLVSWGg 575
Cdd:cd00190 137 ---PLPDVLQEVNVPIVSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWG- 207
|
250 260
....*....|....*....|...
gi 795477829 576 pEECGSKQVYGVYTKVSNYVDWV 598
Cdd:cd00190 208 -SGCARPNYPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
337-598 |
7.51e-59 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 196.12 E-value: 7.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 337 IIGGRNAEPGLFPWQALIVVEdtsrvpNDKWFGSGALLSESWILTAAHVLRSQRRdttvipvskeyVTVYLGLHDVRDKS 416
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASD-----------VKVVLGAHNIVLRE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 417 GAVNS-SAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPSPYMlGLVAGWGISNPNVTvdeiiss 495
Cdd:pfam00089 64 GGEQKfDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT-CTVSGWGNTKTLGP------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 gtrtlSDVLQYVKLPVVPHAECKTSYesrsgNYSVTENMFCAGYyeGGKDTCLGDSGGAFVILDDlsqrwMVQGLVSWGG 575
Cdd:pfam00089 136 -----SDTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGY 198
|
250 260
....*....|....*....|...
gi 795477829 576 PeeCGSKQVYGVYTKVSNYVDWV 598
Cdd:pfam00089 199 G--CASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
336-605 |
5.94e-56 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 190.25 E-value: 5.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 336 RIIGGRNAEPGLFPWQALIVVEDTSRvpndKWFGSGALLSESWILTAAHvlrsqrrdtTVIPVSKEYVTVYLGLHDVRDK 415
Cdd:COG5640 30 AIVGGTPATVGEYPWMVALQSSNGPS----GQFCGGTLIAPRWVLTAAH---------CVDGDGPSDLRVVIGSTDLSTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVnSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLgphVMPVCLPRlEPEGPSPYMLGLVAGWGIsnpnvtvdeiISS 495
Cdd:COG5640 97 GGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLAT-SADAAAPGTPATVAGWGR----------TSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 GTRTLSDVLQYVKLPVVPHAECktsyesRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsQRWMVQGLVSWGG 575
Cdd:COG5640 162 GPGSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG--GGWVLVGVVSWGG 233
|
250 260 270
....*....|....*....|....*....|
gi 795477829 576 pEECGsKQVYGVYTKVSNYVDWVWEQMGSP 605
Cdd:COG5640 234 -GPCA-AGYPGVYTRVSAYRDWIKSTAGGL 261
|
|
| CUB |
pfam00431 |
CUB domain; |
72-181 |
5.15e-39 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 138.97 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 72 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 147
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 795477829 148 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 181
Cdd:pfam00431 77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
72-183 |
1.07e-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: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 72 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 147
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 795477829 148 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRA 183
Cdd:cd00041 78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
82-181 |
1.84e-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: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 82 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 156
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
|
90 100
....*....|....*....|....*
gi 795477829 157 TQSHSVLILFHSDNSGENRGWRLSY 181
Cdd:smart00042 78 SSSNSLTLTFVSDSSVQKRGFSARY 102
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
188-249 |
1.75e-11 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.44 E-value: 1.75e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 249
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
188-250 |
1.88e-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: 59.40 E-value: 1.88e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 250
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
188-249 |
1.26e-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: 1.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 249
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSST------ITCLENGTWSPPPPTC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
40-68 |
1.17e-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: 1.17e-08
10 20
....*....|....*....|....*....
gi 795477829 40 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 68
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
187-320 |
7.45e-07 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 51.20 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 187 ECPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLVT 266
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 795477829 267 FSTRNNLTTYKSEIRYSCQEPYYKMLNNITgiyTCSAQGVWMNkvlgrSLPTCL 320
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| PHA02817 |
PHA02817 |
EEV Host range protein; Provisional |
193-288 |
1.15e-05 |
|
EEV Host range protein; Provisional
Pssm-ID: 165167 [Multi-domain] Cd Length: 225 Bit Score: 46.86 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 193 PP--VHGKIEPSQAKYSFKDQVLISCDTG-----YKVLKDNVemdtfqIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLV 265
Cdd:PHA02817 27 PPsiKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKN------IICEKDGKWNKEFPVCKIIRCRFPA-LQNGFV 99
|
90 100
....*....|....*....|...
gi 795477829 266 TFSTRNNLTTYKSEIRYSCQEPY 288
Cdd:PHA02817 100 NGIPDSKKFYYESEVSFSCKPGF 122
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
26-68 |
3.64e-05 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 41.08 E-value: 3.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 795477829 26 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 68
Cdd:smart00179 1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
254-319 |
5.36e-05 |
|
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: 41.29 E-value: 5.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795477829 254 CRAPGELEHGLVTFSTRNnlTTYKSEIRYSCqEPYYKMLNNitGIYTCSAQGVWMNkvlgrSLPTC 319
Cdd:cd00033 1 CPPPPVPENGTVTGSKGS--YSYGSTVTYSC-NEGYTLVGS--STITCTENGGWSP-----PPPTC 56
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
254-319 |
9.38e-05 |
|
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: 40.59 E-value: 9.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795477829 254 CRAPGELEHGLVTFSTRNnlTTYKSEIRYSCQEPYYKMLNNITgiyTCSAQGVWMNkvlgrSLPTC 319
Cdd:smart00032 1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTI---TCLENGTWSP-----PPPTC 56
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
26-63 |
1.45e-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: 39.54 E-value: 1.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 795477829 26 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 63
Cdd:cd00054 1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
|
|
| vWA_Matrilin |
cd01475 |
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
8-67 |
5.09e-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: 5.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 8 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 67
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
336-598 |
1.04e-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: 253.75 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 336 RIIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSESWILTAAHVLRSQRRDTtvipvskeyVTVYLGLHDVRDK 415
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSL------QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGSHDLSSG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPSPYMLGLVAGWGisnpnvtvdeIISS 495
Cdd:smart00020 66 EEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS-SNYNVPAGTTCTVSGWG----------RTSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 GTRTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsqRWMVQGLVSWGG 575
Cdd:smart00020 135 GAGSLPDTLQEVNVPIVSNATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGS 208
|
250 260
....*....|....*....|...
gi 795477829 576 PeeCGSKQVYGVYTKVSNYVDWV 598
Cdd:smart00020 209 G--CARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
337-598 |
7.72e-80 |
|
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: 251.81 E-value: 7.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 337 IIGGRNAEPGLFPWQALIvvedtsRVPNDKWFGSGALLSESWILTAAHVLRSQRRDTtvipvskeyVTVYLGLHDV-RDK 415
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSL------QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN---------YTVRLGSHDLsSNE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRlEPEGPSPYMLGLVAGWGISNPNVtvdeiiss 495
Cdd:cd00190 66 GGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS-SGYNLPAGTTCTVSGWGRTSEGG-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 gtrTLSDVLQYVKLPVVPHAECKTSYesrSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsQRWMVQGLVSWGg 575
Cdd:cd00190 137 ---PLPDVLQEVNVPIVSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWG- 207
|
250 260
....*....|....*....|...
gi 795477829 576 pEECGSKQVYGVYTKVSNYVDWV 598
Cdd:cd00190 208 -SGCARPNYPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
337-598 |
7.51e-59 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 196.12 E-value: 7.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 337 IIGGRNAEPGLFPWQALIVVEdtsrvpNDKWFGSGALLSESWILTAAHVLRSQRRdttvipvskeyVTVYLGLHDVRDKS 416
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASD-----------VKVVLGAHNIVLRE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 417 GAVNS-SAARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPSPYMlGLVAGWGISNPNVTvdeiiss 495
Cdd:pfam00089 64 GGEQKfDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTT-CTVSGWGNTKTLGP------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 gtrtlSDVLQYVKLPVVPHAECKTSYesrsgNYSVTENMFCAGYyeGGKDTCLGDSGGAFVILDDlsqrwMVQGLVSWGG 575
Cdd:pfam00089 136 -----SDTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGY 198
|
250 260
....*....|....*....|...
gi 795477829 576 PeeCGSKQVYGVYTKVSNYVDWV 598
Cdd:pfam00089 199 G--CASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
336-605 |
5.94e-56 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 190.25 E-value: 5.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 336 RIIGGRNAEPGLFPWQALIVVEDTSRvpndKWFGSGALLSESWILTAAHvlrsqrrdtTVIPVSKEYVTVYLGLHDVRDK 415
Cdd:COG5640 30 AIVGGTPATVGEYPWMVALQSSNGPS----GQFCGGTLIAPRWVLTAAH---------CVDGDGPSDLRVVIGSTDLSTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 416 SGAVnSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLgphVMPVCLPRlEPEGPSPYMLGLVAGWGIsnpnvtvdeiISS 495
Cdd:COG5640 97 GGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLAT-SADAAAPGTPATVAGWGR----------TSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 496 GTRTLSDVLQYVKLPVVPHAECktsyesRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVILDDlsQRWMVQGLVSWGG 575
Cdd:COG5640 162 GPGSQSGTLRKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG--GGWVLVGVVSWGG 233
|
250 260 270
....*....|....*....|....*....|
gi 795477829 576 pEECGsKQVYGVYTKVSNYVDWVWEQMGSP 605
Cdd:COG5640 234 -GPCA-AGYPGVYTRVSAYRDWIKSTAGGL 261
|
|
| CUB |
pfam00431 |
CUB domain; |
72-181 |
5.15e-39 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 138.97 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 72 CSDNlFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGPK----VLGPFC 147
Cdd:pfam00431 1 CGGV-LTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQD-FELEDHDE--CGYDYVEIRDGPSasspLLGRFC 76
|
90 100 110
....*....|....*....|....*....|....
gi 795477829 148 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSY 181
Cdd:pfam00431 77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
72-183 |
1.07e-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: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 72 CSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFC 147
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFED-FDLESSPN--CSYDYLEIYDGPstssPLLGRFC 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 795477829 148 GEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRA 183
Cdd:cd00041 78 GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
82-181 |
1.84e-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: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 82 GVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDiFDIEDHPEvpCPYDYIKIKVGP----KVLGPFCGEKAPEP-IS 156
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTD-FDLESSDN--CEYDYVEIYDGPsassPLLGRFCGSEAPPPvIS 77
|
90 100
....*....|....*....|....*
gi 795477829 157 TQSHSVLILFHSDNSGENRGWRLSY 181
Cdd:smart00042 78 SSSNSLTLTFVSDSSVQKRGFSARY 102
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
188-249 |
1.75e-11 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 59.44 E-value: 1.75e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 249
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPT------ITCQEDGTWSPPFPEC 56
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
188-250 |
1.88e-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: 59.40 E-value: 1.88e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNvemdtfQIECLKDGTWSNKIPTCK 250
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSS------TITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
188-249 |
1.26e-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: 1.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795477829 188 CPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVemdtfqIECLKDGTWSNKIPTC 249
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSST------ITCLENGTWSPPPPTC 56
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
363-577 |
8.01e-10 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 58.53 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 363 PNDKWFGSGALLSESWILTAAHVLRSQRRDTTVipvskEYVTVYLGlhdvRDKSGAVNSSAARVVLHPDFNIQ-NYNHDI 441
Cdd:COG3591 8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWA-----TNIVFVPG----YNGGPYGTATATRFRVPPGWVASgDAGYDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 442 ALVQLQEPVPlgphvmpvclprlEPEGPSPYmlglvagwgISNPNVTVDEIISsgtrtlsdVLQYvklpvvPHAECKTSY 521
Cdd:COG3591 79 ALLRLDEPLG-------------DTTGWLGL---------AFNDAPLAGEPVT--------IIGY------PGDRPKDLS 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 795477829 522 ESRSGN-YSVTENMFcagYYEGgkDTCLGDSGGAfvILDDLSQRWMVQGLVSWGGPE 577
Cdd:COG3591 123 LDCSGRvTGVQGNRL---SYDC--DTTGGSSGSP--VLDDSDGGGRVVGVHSAGGAD 172
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
40-68 |
1.17e-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: 1.17e-08
10 20
....*....|....*....|....*....
gi 795477829 40 CDHYCHNYIGGYYCSCRFGYILHTDNRTC 68
Cdd:pfam14670 8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
187-320 |
7.45e-07 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 51.20 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 187 ECPELQPPVHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVEMDtfQIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLVT 266
Cdd:PHA02639 84 ECNDPPSIINGKIYNKREMYKVGDEIYYVCNEHKGVQYSLVGNE--KITCIQDKSWKPDPPICKMINCRFPA-LQNGYIN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 795477829 267 FSTRNNLTTYKSEIRYSCQEPYYKMLNNITgiyTCSAQGVWMNkvlgrSLPTCL 320
Cdd:PHA02639 161 GIPSNKKFYYKTRVGFSCKSGFDLVGEKYS---TCNINATWFP-----SIPTCV 206
|
|
| PHA02817 |
PHA02817 |
EEV Host range protein; Provisional |
193-288 |
1.15e-05 |
|
EEV Host range protein; Provisional
Pssm-ID: 165167 [Multi-domain] Cd Length: 225 Bit Score: 46.86 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 193 PP--VHGKIEPSQAKYSFKDQVLISCDTG-----YKVLKDNVemdtfqIECLKDGTWSNKIPTCKIVDCRAPGeLEHGLV 265
Cdd:PHA02817 27 PPsiKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKN------IICEKDGKWNKEFPVCKIIRCRFPA-LQNGFV 99
|
90 100
....*....|....*....|...
gi 795477829 266 TFSTRNNLTTYKSEIRYSCQEPY 288
Cdd:PHA02817 100 NGIPDSKKFYYESEVSFSCKPGF 122
|
|
| PHA02954 |
PHA02954 |
EEV membrane glycoprotein; Provisional |
166-269 |
2.68e-05 |
|
EEV membrane glycoprotein; Provisional
Pssm-ID: 165263 [Multi-domain] Cd Length: 317 Bit Score: 46.62 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 166 FHSDNSGENRGWRLSYRAAGNECPELQPPvHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVemdtfqIECLKDgTWsNK 245
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNAECQPLQLE-HGSCQPVKEKYSFGEHITINCDVGYEVIGASY------ISCTAN-SW-NV 178
|
90 100
....*....|....*....|....
gi 795477829 246 IPTCKiVDCRAPgELEHGLVTFST 269
Cdd:PHA02954 179 IPSCQ-QKCDIP-SLSNGLISGST 200
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
26-68 |
3.64e-05 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 41.08 E-value: 3.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 795477829 26 DVDECKEREDeelsCDH--YCHNYIGGYYCSCRFGYilhTDNRTC 68
Cdd:smart00179 1 DIDECASGNP----CQNggTCVNTVGSYRCECPPGY---TDGRNC 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
254-319 |
5.36e-05 |
|
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: 41.29 E-value: 5.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795477829 254 CRAPGELEHGLVTFSTRNnlTTYKSEIRYSCqEPYYKMLNNitGIYTCSAQGVWMNkvlgrSLPTC 319
Cdd:cd00033 1 CPPPPVPENGTVTGSKGS--YSYGSTVTYSC-NEGYTLVGS--STITCTENGGWSP-----PPPTC 56
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
254-319 |
9.38e-05 |
|
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: 40.59 E-value: 9.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795477829 254 CRAPGELEHGLVTFSTRNnlTTYKSEIRYSCQEPYYKMLNNITgiyTCSAQGVWMNkvlgrSLPTC 319
Cdd:smart00032 1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTI---TCLENGTWSP-----PPPTC 56
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
26-63 |
1.45e-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: 39.54 E-value: 1.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 795477829 26 DVDECKEREdeelSCDHY--CHNYIGGYYCSCRFGYILHT 63
Cdd:cd00054 1 DIDECASGN----PCQNGgtCVNTVGSYRCSCPPGYTGRN 36
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
176-327 |
5.41e-04 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 42.33 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 176 GWRLSYRAAGNECPELQPPVHGKIEPSQAKysFKDQVLISCDTGYKVLKDNveMDTFQIECLKDGTWSNKIPTCKIVDCR 255
Cdd:PHA02927 74 GWTLFNQCIKRRCPSPRDIDNGQLDIGGVD--FGSSITYSCNSGYQLIGES--KSYCELGSTGSMVWNPEAPICESVKCQ 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795477829 256 APGELEHGlvTFSTRNNLTTYKSEIRYSCQEPYYKMLNniTGIyTCSAqGVWMNKvlgrslPTC-LPECGQPS 327
Cdd:PHA02927 150 SPPSISNG--RHNGYEDFYTDGSVVTYSCNSGYSLIGN--SGV-LCSG-GEWSDP------PTCqIVKCPHPT 210
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
26-58 |
3.94e-03 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 35.29 E-value: 3.94e-03
10 20 30
....*....|....*....|....*....|....*
gi 795477829 26 DVDECkerEDEELSCDH--YCHNYIGGYYCSCRFG 58
Cdd:pfam07645 1 DVDEC---ATGTHNCPAntVCVNTIGSFECRCPDG 32
|
|
| vWA_Matrilin |
cd01475 |
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
8-67 |
5.09e-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: 5.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 8 DFSNEERFTGFDAHYMAVDVDECKEredEELSCDHYCHNYIGGYYCSCRFGYILHTDNRT 67
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCAT---LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
|
|
| PHA02831 |
PHA02831 |
EEV host range protein; Provisional |
195-322 |
5.27e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165176 [Multi-domain] Cd Length: 268 Bit Score: 39.21 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795477829 195 VHGKIEPSQAKYSFKDQVLISCDTGYKVLKDNVEMDTfqIECLkDGTWSNKIPTCKIVDCRAPGeLEHGLV-TFSTRnnl 273
Cdd:PHA02831 85 LNGYIKNKKDQYSFGDSVTYACKVNKLEKYSIVGNET--VKCI-NKQWVPKYPVCKLIRCKYPA-LQNGFLnVFEKK--- 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 795477829 274 TTYKSEIRYSCQEPyYKMLNNITGiyTCSAQGVWMNkvlgrSLPTCLPE 322
Cdd:PHA02831 158 FYYGDIVNFKCKKG-FILLGSSVS--TCDINSIWYP-----GIPKCVKD 198
|
|
| |
