|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
271-511 |
5.40e-73 |
|
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: 231.40 E-value: 5.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 271 IIGGSDADIKNFPWQVFFDNP----WAGGALINEYWVLTAAHVVEGN--REPTMYVGSTSVqTSRLAKSKMLTPEHVFIH 344
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTggrhFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDL-SSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 345 PGWKLlevpegrTNFDNDIALVRLKDPVKMGPTVSPICLPgtSSDYNLMDGDLGLISGWGRTEKRDR-AVRLKAARLPVA 423
Cdd:cd00190 80 PNYNP-------STYDNDIALLKLKRPVTLSDNVRPICLP--SSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 424 PLRKCKEvkvekptADAEAYVFTPNMICAGGEK-GMDSCKGDSGGAFAVQDPNdktKFYAAGLVSWGPQCG---TYGLYT 499
Cdd:cd00190 151 SNAECKR-------AYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCArpnYPGVYT 220
|
250
....*....|..
gi 1098385908 500 RVKNYVDWIMKT 511
Cdd:cd00190 221 RVSSYLDWIQKT 232
|
|
| CUB |
pfam00431 |
CUB domain; |
8-120 |
2.33e-32 |
|
CUB domain;
:
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 119.71 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 8 CSGdVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQvvVTLRREDFDVEAADSAGNclDSLVFVAGDR----QFGPY 83
Cdd:pfam00431 1 CGG-VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFR--VKLTFQDFELEDHDECGY--DYVEIRDGPSasspLLGRF 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 1098385908 84 CGHGfpGPLNIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:pfam00431 76 CGSG--IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
127-188 |
1.26e-07 |
|
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: 48.23 E-value: 1.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098385908 127 CPK-EDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEgrvgatSFYSTCQSNGKWSNSKLKCQ 188
Cdd:cd00033 1 CPPpPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVG------SSTITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
192-254 |
3.27e-07 |
|
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: 47.14 E-value: 3.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098385908 192 CGIPESIENGKVEDPEST-LFGSVIRYTCEEPYYYMengGGGEYHCAGNGSWVnevlgPELPKC 254
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTySYGDTVTYSCDPGYTLI---GSSTITCLENGTWS-----PPPPTC 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
271-511 |
5.40e-73 |
|
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: 231.40 E-value: 5.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 271 IIGGSDADIKNFPWQVFFDNP----WAGGALINEYWVLTAAHVVEGN--REPTMYVGSTSVqTSRLAKSKMLTPEHVFIH 344
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTggrhFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDL-SSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 345 PGWKLlevpegrTNFDNDIALVRLKDPVKMGPTVSPICLPgtSSDYNLMDGDLGLISGWGRTEKRDR-AVRLKAARLPVA 423
Cdd:cd00190 80 PNYNP-------STYDNDIALLKLKRPVTLSDNVRPICLP--SSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 424 PLRKCKEvkvekptADAEAYVFTPNMICAGGEK-GMDSCKGDSGGAFAVQDPNdktKFYAAGLVSWGPQCG---TYGLYT 499
Cdd:cd00190 151 SNAECKR-------AYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCArpnYPGVYT 220
|
250
....*....|..
gi 1098385908 500 RVKNYVDWIMKT 511
Cdd:cd00190 221 RVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
270-508 |
2.61e-70 |
|
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: 224.48 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 270 RIIGGSDADIKNFPWQVFFDNPWA----GGALINEYWVLTAAHVVEG--NREPTMYVGSTSVQTSRlaKSKMLTPEHVFI 343
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGrhfcGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGE--EGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 344 HPGWKllevpegRTNFDNDIALVRLKDPVKMGPTVSPICLPgtSSDYNLMDGDLGLISGWGRTEKRDR--AVRLKAARLP 421
Cdd:smart00020 79 HPNYN-------PSTYDNDIALLKLKEPVTLSDNVRPICLP--SSNYNVPAGTTCTVSGWGRTSEGAGslPDTLQEVNVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 422 VAPLRKCKEVKVEKPtadaeayVFTPNMICAGG-EKGMDSCKGDSGGAFAVQDPndktKFYAAGLVSWGPQCG---TYGL 497
Cdd:smart00020 150 IVSNATCRRAYSGGG-------AITDNMLCAGGlEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCArpgKPGV 218
|
250
....*....|.
gi 1098385908 498 YTRVKNYVDWI 508
Cdd:smart00020 219 YTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
271-508 |
1.77e-55 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 185.34 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 271 IIGGSDADIKNFPWQVFFDN----PWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQtSRLAKSKMLTPEHVFIHPG 346
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLssgkHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 347 WkllevpeGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDynLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLR 426
Cdd:pfam00089 80 Y-------NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSD--LPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 427 KCKEvkvekptadAEAYVFTPNMICAGGeKGMDSCKGDSGGAFAVQDPndktkfYAAGLVSWGPQCG---TYGLYTRVKN 503
Cdd:pfam00089 151 TCRS---------AYGGTVTDTMICAGA-GGKDACQGDSGGPLVCSDG------ELIGIVSWGYGCAsgnYPGVYTPVSS 214
|
....*
gi 1098385908 504 YVDWI 508
Cdd:pfam00089 215 YLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
269-516 |
2.41e-50 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 173.30 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 269 QRIIGGSDADIKNFPWQVF------FDNPWAGGALINEYWVLTAAHVVEGNREPTMYV--GSTSVQTSRlakSKMLTPEH 340
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVAlqssngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVviGSTDLSTSG---GTVVKVAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 341 VFIHPGWkllevpeGRTNFDNDIALVRLKDPVkmgPTVSPICLPGTSSDYNlmDGDLGLISGWGRTE--KRDRAVRLKAA 418
Cdd:COG5640 106 IVVHPDY-------DPATPGNDIALLKLATPV---PGVAPAPLATSADAAA--PGTPATVAGWGRTSegPGSQSGTLRKA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 419 RLPVAPLRKCKevkvekptadAEAYVFTPNMICAGGEKG-MDSCKGDSGGAFAVQDPNDktkFYAAGLVSWGP-QC--GT 494
Cdd:COG5640 174 DVPVVSDATCA----------AYGGFDGGTMLCAGYPEGgKDACQGDSGGPLVVKDGGG---WVLVGVVSWGGgPCaaGY 240
|
250 260
....*....|....*....|..
gi 1098385908 495 YGLYTRVKNYVDWIMKTMQENS 516
Cdd:COG5640 241 PGVYTRVSAYRDWIKSTAGGLG 262
|
|
| CUB |
pfam00431 |
CUB domain; |
8-120 |
2.33e-32 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 119.71 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 8 CSGdVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQvvVTLRREDFDVEAADSAGNclDSLVFVAGDR----QFGPY 83
Cdd:pfam00431 1 CGG-VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFR--VKLTFQDFELEDHDECGY--DYVEIRDGPSasspLLGRF 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 1098385908 84 CGHGfpGPLNIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:pfam00431 76 CGSG--IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
8-120 |
6.83e-25 |
|
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: 99.02 E-value: 6.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 8 CSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLrrEDFDVEaadSAGNC-LDSLVFVAGD----RQFGP 82
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTF--EDFDLE---SSPNCsYDYLEIYDGPstssPLLGR 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1098385908 83 YCGHGFPGPlnIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:cd00041 76 FCGSTLPPP--IISSGNSLTVRFRSDSSVTGRGFKATY 111
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
18-120 |
9.17e-25 |
|
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: 98.23 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 18 GEIASPNYPKPYPENSRCEYQIRLEKGFQvvVTLRREDFDVEAADsagNCLDSLVFV-----AGDRQFGPYCGHGFPGPL 92
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYR--IELQFTDFDLESSD---NCEYDYVEIydgpsASSPLLGRFCGSEAPPPV 75
|
90 100
....*....|....*....|....*...
gi 1098385908 93 nIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:smart00042 76 -ISSSSNSLTLTFVSDSSVQKRGFSARY 102
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
127-188 |
1.26e-07 |
|
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: 48.23 E-value: 1.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098385908 127 CPK-EDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEgrvgatSFYSTCQSNGKWSNSKLKCQ 188
Cdd:cd00033 1 CPPpPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVG------SSTITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
192-254 |
3.27e-07 |
|
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: 47.14 E-value: 3.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098385908 192 CGIPESIENGKVEDPEST-LFGSVIRYTCEEPYYYMengGGGEYHCAGNGSWVnevlgPELPKC 254
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTySYGDTVTYSCDPGYTLI---GSSTITCLENGTWS-----PPPPTC 56
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
192-255 |
1.12e-06 |
|
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: 45.53 E-value: 1.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098385908 192 CGIPESIENGKVEDP-ESTLFGSVIRYTCEEPYYYMengGGGEYHCAGNGSWVnevlgPELPKCV 255
Cdd:cd00033 1 CPPPPVPENGTVTGSkGSYSYGSTVTYSCNEGYTLV---GSSTITCTENGGWS-----PPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
127-187 |
1.38e-06 |
|
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: 45.60 E-value: 1.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098385908 127 CPKEDTP-NSVWEPAKAKYVFRDVVQITCLDGFEVVEgrvgatSFYSTCQSNGKWSNSKLKC 187
Cdd:smart00032 1 CPPPPDIeNGTVTSSSGTYSYGDTVTYSCDPGYTLIG------SSTITCLENGTWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
127-187 |
2.42e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.80 E-value: 2.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098385908 127 CPK-EDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVegrvgaTSFYSTCQSNGKWSNSKLKC 187
Cdd:pfam00084 1 CPPpPDIPNGKVSATKNEYNYGASVSYECDPGYRLV------GSPTITCQEDGTWSPPFPEC 56
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
134-261 |
4.04e-06 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 48.50 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 134 NSVWEPAKAKYVFRDVVQITCLDGFEvvEGRVGatSFYSTCQSNGkWSNSKlKCQPVDCGIPESIENGKVeDPESTLFGS 213
Cdd:PHA02927 34 NSVETDANANYNIGDTIEYLCLPGYR--KQKMG--PIYAKCTGTG-WTLFN-QCIKRRCPSPRDIDNGQL-DIGGVDFGS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1098385908 214 VIRYTCEEPYYYMengGGGEYHCAgNGSWVNEVLGPELPKCVPV-CGVP 261
Cdd:PHA02927 107 SITYSCNSGYQLI---GESKSYCE-LGSTGSMVWNPEAPICESVkCQSP 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
271-511 |
5.40e-73 |
|
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: 231.40 E-value: 5.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 271 IIGGSDADIKNFPWQVFFDNP----WAGGALINEYWVLTAAHVVEGN--REPTMYVGSTSVqTSRLAKSKMLTPEHVFIH 344
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTggrhFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDL-SSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 345 PGWKLlevpegrTNFDNDIALVRLKDPVKMGPTVSPICLPgtSSDYNLMDGDLGLISGWGRTEKRDR-AVRLKAARLPVA 423
Cdd:cd00190 80 PNYNP-------STYDNDIALLKLKRPVTLSDNVRPICLP--SSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 424 PLRKCKEvkvekptADAEAYVFTPNMICAGGEK-GMDSCKGDSGGAFAVQDPNdktKFYAAGLVSWGPQCG---TYGLYT 499
Cdd:cd00190 151 SNAECKR-------AYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCArpnYPGVYT 220
|
250
....*....|..
gi 1098385908 500 RVKNYVDWIMKT 511
Cdd:cd00190 221 RVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
270-508 |
2.61e-70 |
|
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: 224.48 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 270 RIIGGSDADIKNFPWQVFFDNPWA----GGALINEYWVLTAAHVVEG--NREPTMYVGSTSVQTSRlaKSKMLTPEHVFI 343
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGrhfcGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGE--EGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 344 HPGWKllevpegRTNFDNDIALVRLKDPVKMGPTVSPICLPgtSSDYNLMDGDLGLISGWGRTEKRDR--AVRLKAARLP 421
Cdd:smart00020 79 HPNYN-------PSTYDNDIALLKLKEPVTLSDNVRPICLP--SSNYNVPAGTTCTVSGWGRTSEGAGslPDTLQEVNVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 422 VAPLRKCKEVKVEKPtadaeayVFTPNMICAGG-EKGMDSCKGDSGGAFAVQDPndktKFYAAGLVSWGPQCG---TYGL 497
Cdd:smart00020 150 IVSNATCRRAYSGGG-------AITDNMLCAGGlEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCArpgKPGV 218
|
250
....*....|.
gi 1098385908 498 YTRVKNYVDWI 508
Cdd:smart00020 219 YTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
271-508 |
1.77e-55 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 185.34 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 271 IIGGSDADIKNFPWQVFFDN----PWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQtSRLAKSKMLTPEHVFIHPG 346
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLssgkHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 347 WkllevpeGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDynLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLR 426
Cdd:pfam00089 80 Y-------NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSD--LPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 427 KCKEvkvekptadAEAYVFTPNMICAGGeKGMDSCKGDSGGAFAVQDPndktkfYAAGLVSWGPQCG---TYGLYTRVKN 503
Cdd:pfam00089 151 TCRS---------AYGGTVTDTMICAGA-GGKDACQGDSGGPLVCSDG------ELIGIVSWGYGCAsgnYPGVYTPVSS 214
|
....*
gi 1098385908 504 YVDWI 508
Cdd:pfam00089 215 YLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
269-516 |
2.41e-50 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 173.30 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 269 QRIIGGSDADIKNFPWQVF------FDNPWAGGALINEYWVLTAAHVVEGNREPTMYV--GSTSVQTSRlakSKMLTPEH 340
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVAlqssngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVviGSTDLSTSG---GTVVKVAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 341 VFIHPGWkllevpeGRTNFDNDIALVRLKDPVkmgPTVSPICLPGTSSDYNlmDGDLGLISGWGRTE--KRDRAVRLKAA 418
Cdd:COG5640 106 IVVHPDY-------DPATPGNDIALLKLATPV---PGVAPAPLATSADAAA--PGTPATVAGWGRTSegPGSQSGTLRKA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 419 RLPVAPLRKCKevkvekptadAEAYVFTPNMICAGGEKG-MDSCKGDSGGAFAVQDPNDktkFYAAGLVSWGP-QC--GT 494
Cdd:COG5640 174 DVPVVSDATCA----------AYGGFDGGTMLCAGYPEGgKDACQGDSGGPLVVKDGGG---WVLVGVVSWGGgPCaaGY 240
|
250 260
....*....|....*....|..
gi 1098385908 495 YGLYTRVKNYVDWIMKTMQENS 516
Cdd:COG5640 241 PGVYTRVSAYRDWIKSTAGGLG 262
|
|
| CUB |
pfam00431 |
CUB domain; |
8-120 |
2.33e-32 |
|
CUB domain;
Pssm-ID: 395345 [Multi-domain] Cd Length: 110 Bit Score: 119.71 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 8 CSGdVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQvvVTLRREDFDVEAADSAGNclDSLVFVAGDR----QFGPY 83
Cdd:pfam00431 1 CGG-VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFR--VKLTFQDFELEDHDECGY--DYVEIRDGPSasspLLGRF 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 1098385908 84 CGHGfpGPLNIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:pfam00431 76 CGSG--IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
|
|
| CUB |
cd00041 |
CUB domain; extracellular domain; present in proteins mostly known to be involved in ... |
8-120 |
6.83e-25 |
|
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: 99.02 E-value: 6.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 8 CSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLrrEDFDVEaadSAGNC-LDSLVFVAGD----RQFGP 82
Cdd:cd00041 1 CGGTLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTF--EDFDLE---SSPNCsYDYLEIYDGPstssPLLGR 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1098385908 83 YCGHGFPGPlnIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:cd00041 76 FCGSTLPPP--IISSGNSLTVRFRSDSSVTGRGFKATY 111
|
|
| CUB |
smart00042 |
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ... |
18-120 |
9.17e-25 |
|
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: 98.23 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 18 GEIASPNYPKPYPENSRCEYQIRLEKGFQvvVTLRREDFDVEAADsagNCLDSLVFV-----AGDRQFGPYCGHGFPGPL 92
Cdd:smart00042 1 GTITSPNYPQSYPNNLDCVWTIRAPPGYR--IELQFTDFDLESSD---NCEYDYVEIydgpsASSPLLGRFCGSEAPPPV 75
|
90 100
....*....|....*....|....*...
gi 1098385908 93 nIETKSNALDIIFQTDLTGQKKGWKLRY 120
Cdd:smart00042 76 -ISSSSNSLTLTFVSDSSVQKRGFSARY 102
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
127-188 |
1.26e-07 |
|
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: 48.23 E-value: 1.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098385908 127 CPK-EDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEgrvgatSFYSTCQSNGKWSNSKLKCQ 188
Cdd:cd00033 1 CPPpPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVG------SSTITCTENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
192-254 |
3.27e-07 |
|
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: 47.14 E-value: 3.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098385908 192 CGIPESIENGKVEDPEST-LFGSVIRYTCEEPYYYMengGGGEYHCAGNGSWVnevlgPELPKC 254
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTySYGDTVTYSCDPGYTLI---GSSTITCLENGTWS-----PPPPTC 56
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
192-255 |
1.12e-06 |
|
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: 45.53 E-value: 1.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098385908 192 CGIPESIENGKVEDP-ESTLFGSVIRYTCEEPYYYMengGGGEYHCAGNGSWVnevlgPELPKCV 255
Cdd:cd00033 1 CPPPPVPENGTVTGSkGSYSYGSTVTYSCNEGYTLV---GSSTITCTENGGWS-----PPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
127-187 |
1.38e-06 |
|
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: 45.60 E-value: 1.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098385908 127 CPKEDTP-NSVWEPAKAKYVFRDVVQITCLDGFEVVEgrvgatSFYSTCQSNGKWSNSKLKC 187
Cdd:smart00032 1 CPPPPDIeNGTVTSSSGTYSYGDTVTYSCDPGYTLIG------SSTITCLENGTWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
127-187 |
2.42e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.80 E-value: 2.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098385908 127 CPK-EDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVegrvgaTSFYSTCQSNGKWSNSKLKC 187
Cdd:pfam00084 1 CPPpPDIPNGKVSATKNEYNYGASVSYECDPGYRLV------GSPTITCQEDGTWSPPFPEC 56
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
134-261 |
4.04e-06 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 48.50 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 134 NSVWEPAKAKYVFRDVVQITCLDGFEvvEGRVGatSFYSTCQSNGkWSNSKlKCQPVDCGIPESIENGKVeDPESTLFGS 213
Cdd:PHA02927 34 NSVETDANANYNIGDTIEYLCLPGYR--KQKMG--PIYAKCTGTG-WTLFN-QCIKRRCPSPRDIDNGQL-DIGGVDFGS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1098385908 214 VIRYTCEEPYYYMengGGGEYHCAgNGSWVNEVLGPELPKCVPV-CGVP 261
Cdd:PHA02927 107 SITYSCNSGYQLI---GESKSYCE-LGSTGSMVWNPEAPICESVkCQSP 151
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
285-514 |
1.31e-03 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 40.04 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 285 QVFFDNPWAG--GALINEYWVLTAAHVV---EGNREPTMYVGSTSVQTSRLAKSkmlTPEHVFIHPGWKLlevpegRTNF 359
Cdd:COG3591 4 RLETDGGGGVctGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYGTA---TATRFRVPPGWVA------SGDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 360 DNDIALVRLKDPVkmGPTVSPIclpGTSSDYNLMDGDLGLISGWGrtekRDRAVRLKAARlpvaplrkckevkvekptaD 439
Cdd:COG3591 75 GYDYALLRLDEPL--GDTTGWL---GLAFNDAPLAGEPVTIIGYP----GDRPKDLSLDC-------------------S 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098385908 440 AEAYVFTPNMICAggekGMDSCKGDSGGAFAVQDPNdktKFYAAGLVSWGPqCGTYGLYTRV-KNYVDWIMKTMQE 514
Cdd:COG3591 127 GRVTGVQGNRLSY----DCDTTGGSSGSPVLDDSDG---GGRVVGVHSAGG-ADRANTGVRLtSAIVAALRAWASA 194
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
146-234 |
8.34e-03 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 38.10 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 146 FRDVVQITCLDGFEVVegrvGATSFYSTCQSNGK--WSNSKLKCQPVDCGIPESIENGKVEDPESTLF-GSVIRYTCEEP 222
Cdd:PHA02927 104 FGSSITYSCNSGYQLI----GESKSYCELGSTGSmvWNPEAPICESVKCQSPPSISNGRHNGYEDFYTdGSVVTYSCNSG 179
|
90
....*....|....*.
gi 1098385908 223 YYYMENGG----GGEY 234
Cdd:PHA02927 180 YSLIGNSGvlcsGGEW 195
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
121-254 |
8.49e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 38.49 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098385908 121 HG-DPMPCPK-EDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRvgatsfYSTC---QSNGKWSNSKLKCQPVDCGIP 195
Cdd:PHA02639 15 HGvKSIYCDKpDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDR------FRTCikdKNNAIWSNKAPFCMLKECNDP 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098385908 196 ESIENGKVEDP-ESTLFGSVIRYTCEEPYYYMENGGGGE-YHCAGNGSWvnevlGPELPKC 254
Cdd:PHA02639 89 PSIINGKIYNKrEMYKVGDEIYYVCNEHKGVQYSLVGNEkITCIQDKSW-----KPDPPIC 144
|
|
| |
