|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
36-268 |
7.50e-106 |
|
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: 337.73 E-value: 7.50e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 36 RIVGGQSAQPGSWPWQASLRLNGG-HTCGGTLINSQWVLTAAHCFSGSTtPSQWTVYLGVTDTGSSTNTVSRGVQQIIKH 114
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 115 PNYDSSTNNNDIALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTTLPSTLQEVQLPIIGNRQCgcl 194
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 195 NDVVFGANSVTGNMICAGVLQGGKDSCQGDSGGPLVCkQGSVWVQAGVVSFGEGCARPSLPGVYTRVSQYQDWI 268
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
37-269 |
3.27e-104 |
|
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: 333.09 E-value: 3.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 37 IVGGQSAQPGSWPWQASLRLN-GGHTCGGTLINSQWVLTAAHCFSGSTtPSQWTVYLGVTDTGSSTNT-VSRGVQQIIKH 114
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGgQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 115 PNYDSSTNNNDIALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTtLPSTLQEVQLPIIGNRQCgcl 194
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAEC--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 195 NDVVFGANSVTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSVWVQAGVVSFGEGCARPSLPGVYTRVSQYQDWIN 269
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
337-572 |
1.32e-102 |
|
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: 328.47 E-value: 1.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 337 IVGGNPAQEGSWPWQASLHYY-GQHMCGGSLINQQWVLTAAHCIPDPlNTYPWTVYLGRLTQFSSSPNELSRSVQQIIVH 415
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 416 PAYNSVTEDNDIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTGWGYTAEDGaTLPTTLQEVQLSIIGNRQCgcl 495
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAEC--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973216831 496 NDVVFGVNSVTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSSWVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWINTQ 572
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
336-569 |
5.01e-102 |
|
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: 326.56 E-value: 5.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 336 RIVGGNPAQEGSWPWQASLHYYG-QHMCGGSLINQQWVLTAAHCIPDPLNTyPWTVYLGRLTQFSSSPNELsRSVQQIIV 414
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSSGEEGQV-IKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 415 HPAYNSVTEDNDIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTGWGYTAEDGATLPTTLQEVQLSIIGNRQCgc 494
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 495 lNDVVFGVNSVTGNMICAGVLQGGKDSCQGDSGGPLVCkQGSSWVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWI 569
Cdd:smart00020 157 -RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1463-1698 |
1.08e-96 |
|
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: 311.52 E-value: 1.08e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1463 IVGGDSAPEGYWPWQASLQYY-GYHFCGGSLINNQWVLTAAHCTYWISSMMVQVYLGKESQEGSNPHQVSRGVERIILHP 1541
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1542 NFDYMTLNNDIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTGWGNIADGVSLPNnkTLQEVQLPIIGKSQCgci 1621
Cdd:cd00190 81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAEC--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973216831 1622 SNLTFGVNFITDNMICAGVLDNRKSPCNGDSGGPLVCKQGSAWVQAGIVSFGYGCARPNVPGVYTRMSQYQDWINRQ 1698
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1462-1695 |
1.63e-93 |
|
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: 302.29 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1462 RIVGGDSAPEGYWPWQASLQYYG-YHFCGGSLINNQWVLTAAHCTYWISSMMVQVYLGKESQEGSNPHQVsRGVERIILH 1540
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1541 PNFDYMTLNNDIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTGWGNIADGvSLPNNKTLQEVQLPIIGKSQCgc 1620
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVSNATC-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1621 iSNLTFGVNFITDNMICAGVLDNRKSPCNGDSGGPLVCkQGSAWVQAGIVSFGYGCARPNVPGVYTRMSQYQDWI 1695
Cdd:smart00020 157 -RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1177-1411 |
7.52e-93 |
|
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: 300.73 E-value: 7.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1177 IVGGDSAPEGYWPWQASLHHY-GQHICGGSLINHQWVLTAAHCVNGiSDGRQLTVYLGRQSQLGSNTHEVSRMVTMVIPH 1255
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1256 PGY--LNFDKDVALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTGWGNIAEGVFLtgNQALQEVQLSIIGNRQCTC 1333
Cdd:cd00190 80 PNYnpSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973216831 1334 LYnmiPVPDLITDNMICAGDLEGGKGSCQGDSGGPLVCKQGSSWVQAGVVSFAVGCARPSFPSVFARVSRFQDWINEQ 1411
Cdd:cd00190 158 AY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1176-1408 |
3.56e-90 |
|
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: 292.66 E-value: 3.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1176 RIVGGDSAPEGYWPWQASLH-HYGQHICGGSLINHQWVLTAAHCVNGiSDGRQLTVYLGRqSQLGSNTHEVSRMVTMVIP 1254
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-HDLSSGEEGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1255 HPGY--LNFDKDVALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTGWGNIAEGVfLTGNQALQEVQLSIIGNRQCT 1332
Cdd:smart00020 79 HPNYnpSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGA-GSLPDTLQEVNVPIVSNATCR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973216831 1333 CLYnmiPVPDLITDNMICAGDLEGGKGSCQGDSGGPLVCkQGSSWVQAGVVSFAVGCARPSFPSVFARVSRFQDWI 1408
Cdd:smart00020 158 RAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
897-1130 |
1.65e-86 |
|
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: 282.24 E-value: 1.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 897 IAGGQSAQEGYWPWQASLHYS-GYYMCGGSLINHQWVLSAAGCVYRiSDNRQLTVYLGRQNQMNSNPNEVSRRITRVIPH 975
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 976 PDFNSTTFTNDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTGWGNTDDYSFYAQILQEAQVPIMGNRQCGCLY 1055
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1056 aeaFGVNSITENMICGGVPDGGNATCLGDSGGPLVCKQGSAWIQAGVVKYRDGCTPSSLPGVYTRVSQYQDWINE 1130
Cdd:cd00190 160 ---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
896-1128 |
2.18e-84 |
|
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: 276.10 E-value: 2.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 896 RIAGGQSAQEGYWPWQASLHYSGYYM-CGGSLINHQWVLSAAGCVYRiSDNRQLTVYLGRQNqMNSNPNEVSRRITRVIP 974
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHD-LSSGEEGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 975 HPDFNSTTFTNDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTGWGNTDDYSF-YAQILQEAQVPIMGNRQCGC 1053
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSNATCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1054 LYaeaFGVNSITENMICGGVPDGGNATCLGDSGGPLVCkQGSAWIQAGVVKYRDGCTPSSLPGVYTRVSQYQDWI 1128
Cdd:smart00020 159 AY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
618-850 |
1.68e-82 |
|
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: 270.69 E-value: 1.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 618 IVGGVSAPEGYWPWQVRIYYF-GYYRCGGSLINQQWVLTAATCVYSAWVSELKVYLGRQTQAGPNSQELSKKVKQVLLHP 696
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 697 DYSSS--NNDIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAGWGFTAEFMSLPgnQTLQEVQLPIIGNRQCGCL 774
Cdd:cd00190 81 NYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECKRA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973216831 775 YdlnYGPGSVNDSMICAGQPNGGKDTCWGDEGGPLICKQGSSWVQAGIVRPGEGCGQTDLPGLYTRVSQYEDWIYQ 850
Cdd:cd00190 159 Y---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
617-848 |
4.98e-82 |
|
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: 269.55 E-value: 4.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 617 RIVGGVSAPEGYWPWQVRIYYFGYY-RCGGSLINQQWVLTAATCVYSAWVSELKVYLGR-QTQAGPNSQELskKVKQVLL 694
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShDLSSGEEGQVI--KVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 695 HPDYSSSN--NDIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAGWGFTAEfMSLPGNQTLQEVQLPIIGNRQCG 772
Cdd:smart00020 79 HPNYNPSTydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973216831 773 CLYdlnYGPGSVNDSMICAGQPNGGKDTCWGDEGGPLICkQGSSWVQAGIVRPGEGCGQTDLPGLYTRVSQYEDWI 848
Cdd:smart00020 158 RAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
35-274 |
1.70e-80 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 266.52 E-value: 1.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 35 TRIVGGQSAQPGSWPWQASLRLNGG---HTCGGTLINSQWVLTAAHCFSGsTTPSQWTVYLGVTDTGSSTNTVsRGVQQI 111
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTV-VKVARI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 112 IKHPNYDSSTNNNDIALMKLSSSVSFnnyIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTTLPSTLQEVQLPIIGNRQC 191
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 192 GCLNDVVfgansvTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSVWVQAGVVSFGEGCARPSLPGVYTRVSQYQDWINGQ 271
Cdd:COG5640 184 AAYGGFD------GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257
|
...
gi 973216831 272 VGS 274
Cdd:COG5640 258 AGG 260
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
335-574 |
1.44e-78 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 260.74 E-value: 1.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 335 PRIVGGNPAQEGSWPWQASLHY---YGQHMCGGSLINQQWVLTAAHCIPDPLNTyPWTVYLGRLTQFSSSPNElsRSVQQ 411
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIGSTDLSTSGGTV--VKVAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 412 IIVHPAYNSVTEDNDIALMRLSSPVSFtsyIQPICLADNSSSFYNGTSCWVTGWGYTAEDGATLPTTLQEVQLSIIGNRQ 491
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDAT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 492 CGCLNDVVfgvnsvTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSSWVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWINT 571
Cdd:COG5640 183 CAAYGGFD------GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256
|
...
gi 973216831 572 QVG 574
Cdd:COG5640 257 TAG 259
|
|
| Trypsin |
pfam00089 |
Trypsin; |
337-569 |
5.26e-78 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 257.37 E-value: 5.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 337 IVGGNPAQEGSWPWQASLHYY-GQHMCGGSLINQQWVLTAAHCIPDPLNtypWTVYLGRLTQFSSSPNELSRSVQQIIVH 415
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 416 PAYNSVTEDNDIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTGWGYTAEDGatLPTTLQEVQLSIIGNRQCGCL 495
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 496 NDvvfgvNSVTGNMICAGVlqGGKDSCQGDSGGPLVCKQGsswVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWI 569
Cdd:pfam00089 156 YG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
37-268 |
1.51e-76 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 253.13 E-value: 1.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 37 IVGGQSAQPGSWPWQASLRLNGG-HTCGGTLINSQWVLTAAHCFSGSttpSQWTVYLGVTDTGSSTNTVSRG-VQQIIKH 114
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFdVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 115 PNYDSSTNNNDIALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTtlPSTLQEVQLPIIGNRQCGCl 194
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRS- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 195 ndvvFGANSVTGNMICAGVlqGGKDSCQGDSGGPLVCKQGSVwvqAGVVSFGEGCARPSLPGVYTRVSQYQDWI 268
Cdd:pfam00089 155 ----AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGEL---IGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
1463-1695 |
4.70e-74 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 246.20 E-value: 4.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1463 IVGGDSAPEGYWPWQASLQYY-GYHFCGGSLINNQWVLTAAHCTYwiSSMMVQVYLGKESQEGSNPHQVSRGVERIILHP 1541
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1542 NFDYMTLNNDIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTGWGNIADGVSlpnNKTLQEVQLPIIGKSQCGCI 1621
Cdd:pfam00089 79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 1622 SNLTfgvnfITDNMICAGvlDNRKSPCNGDSGGPLVCKQGSAwvqAGIVSFGYGCARPNVPGVYTRMSQYQDWI 1695
Cdd:pfam00089 156 YGGT-----VTDTMICAG--AGGKDACQGDSGGPLVCSDGEL---IGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1461-1699 |
3.06e-68 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 231.08 E-value: 3.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1461 PRIVGGDSAPEGYWPWQASLQY---YGYHFCGGSLINNQWVLTAAHCTYWISSMMVQVYLGKESQEGSNPhqVSRGVERI 1537
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG--TVVKVARI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1538 ILHPNFDYMTLNNDIALLKLSSPVTFtdyIQPICLAANSSSFHTGTSCWVTGWGNIADGVSLPNNkTLQEVQLPIIGKSQ 1617
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSG-TLRKADVPVVSDAT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1618 CGCISNltfgvnFITDNMICAGVLDNRKSPCNGDSGGPLVCKQGSAWVQAGIVSFGYGCARPNVPGVYTRMSQYQDWINR 1697
Cdd:COG5640 183 CAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256
|
..
gi 973216831 1698 QV 1699
Cdd:COG5640 257 TA 258
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1157-1416 |
1.90e-67 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 228.77 E-value: 1.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1157 ALGTTPVTPSECGKAPLSPRIVGGDSAPEGYWPWQASLHH---YGQHICGGSLINHQWVLTAAHCVNGISDGrQLTVYLG 1233
Cdd:COG5640 11 AAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1234 RQSqLGSNTHEVSRmVTMVIPHPGYLN--FDKDVALLRLNKPVSFtayIQPICLASNISSFQNGTQCWVTGWGNIAEGVf 1311
Cdd:COG5640 90 STD-LSTSGGTVVK-VARIVVHPDYDPatPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGP- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1312 ltGNQA--LQEVQLSIIGNRQCTclynmiPVPDLITDNMICAGDLEGGKGSCQGDSGGPLVCKQGSSWVQAGVVSFAVGC 1389
Cdd:COG5640 164 --GSQSgtLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGP 235
|
250 260
....*....|....*....|....*..
gi 973216831 1390 ARPSFPSVFARVSRFQDWINEQVGSAT 1416
Cdd:COG5640 236 CAAGYPGVYTRVSAYRDWIKSTAGGLG 262
|
|
| Trypsin |
pfam00089 |
Trypsin; |
1177-1408 |
6.67e-65 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 220.01 E-value: 6.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1177 IVGGDSAPEGYWPWQASLHHY-GQHICGGSLINHQWVLTAAHCVngiSDGRQLTVYLGRQSQLGSNTHEVSRMVTMVIPH 1255
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1256 PGY--LNFDKDVALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTGWGNIAEGVFltgNQALQEVQLSIIGNRQCTC 1333
Cdd:pfam00089 78 PNYnpDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1334 LYnmipvPDLITDNMICAGdlEGGKGSCQGDSGGPLVCKQGsswVQAGVVSFAVGCARPSFPSVFARVSRFQDWI 1408
Cdd:pfam00089 155 AY-----GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
897-1128 |
1.34e-64 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 218.85 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 897 IAGGQSAQEGYWPWQASLHY-SGYYMCGGSLINHQWVLSAAGCVYrisDNRQLTVYLGRQNQMNSNPNEVSRRITRVIPH 975
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 976 PDFNSTTFTNDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTGWGNTDDYSfYAQILQEAQVPIMGNRQCGCLY 1055
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973216831 1056 AeafgvNSITENMICGGvpDGGNATCLGDSGGPLVCKQGsawIQAGVVKYRDGCTPSSLPGVYTRVSQYQDWI 1128
Cdd:pfam00089 157 G-----GTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
604-853 |
2.12e-62 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 214.51 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 604 VASSECGKAPLSTRIVGGVSAPEGYWPWQVRIYY---FGYYRCGGSLINQQWVLTAATCVYSAWVSELKVYLGRQTQAGP 680
Cdd:COG5640 17 LALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 681 NSQELskKVKQVLLHPDYSSS--NNDIALLELRSPVTFtnyIQPICLAANSSSFYTGTSCWVAGWGFTAEFMSlPGNQTL 758
Cdd:COG5640 97 GGTVV--KVARIVVHPDYDPAtpGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 759 QEVQLPIIGNRQCgclydlNYGPGSVNDSMICAGQPNGGKDTCWGDEGGPLICKQGSSWVQAGIVRPGEGCGQTDLPGLY 838
Cdd:COG5640 171 RKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVY 244
|
250
....*....|....*
gi 973216831 839 TRVSQYEDWIYQMVG 853
Cdd:COG5640 245 TRVSAYRDWIKSTAG 259
|
|
| Trypsin |
pfam00089 |
Trypsin; |
618-848 |
4.95e-62 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 211.53 E-value: 4.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 618 IVGGVSAPEGYWPWQVRIYYF-GYYRCGGSLINQQWVLTAATCVYSAwvSELKVYLGRQTQAGPNSQELSKKVKQVLLHP 696
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 697 DYSSS--NNDIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAGWGFTAEFMSlpgNQTLQEVQLPIIGNRQCGCL 774
Cdd:pfam00089 79 NYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 775 YdlnygPGSVNDSMICAGqpNGGKDTCWGDEGGPLICKQGsswVQAGIVRPGEGCGQTDLPGLYTRVSQYEDWI 848
Cdd:pfam00089 156 Y-----GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
888-1130 |
1.39e-61 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 212.20 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 888 CGQAPLRTRIAGGQSAQEGYWPWQASLHYSG---YYMCGGSLINHQWVLSAAGCVYRISdNRQLTVYLGRqNQMNSNPNE 964
Cdd:COG5640 22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGS-TDLSTSGGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 965 VsRRITRVIPHPDFNSTTFTNDIALLRLQTPVNFtnyIQPICLADNSSSFSTGTSCWVTGWGNTD-DYSFYAQILQEAQV 1043
Cdd:COG5640 100 V-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1044 PIMGNRQCgclyaeAFGVNSITENMICGGVPDGGNATCLGDSGGPLVCKQGSAWIQAGVVKY-RDGCTPSSlPGVYTRVS 1122
Cdd:COG5640 176 PVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCAAGY-PGVYTRVS 248
|
....*...
gi 973216831 1123 QYQDWINE 1130
Cdd:COG5640 249 AYRDWIKS 256
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1745-1961 |
1.27e-35 |
|
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: 136.25 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1745 GGQYAQEEYWPWMVSLHQN-GNYVCGGTLIASDWVMTAAQCLPSSvDVSEWSVGLGLTVHNISYGFKGSVRVLDVTT--- 1820
Cdd:cd00190 3 GGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVhpn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1821 --SSLSGSNIALLRLDTNVSYTGFILPICLAGASVSFPTGTECWVTSWDKVWENL----VLKEVKMKITP---CENVSST 1891
Cdd:cd00190 82 ynPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplpdVLQEVNVPIVSnaeCKRAYSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1892 DS------ICTEPLNLE----QRDSGSPLVCKQGSVWIQAsvidvnqtAIT--GNRSStavRALSPGVFTRVSRYESFLR 1959
Cdd:cd00190 162 GGtitdnmLCAGGLEGGkdacQGDSGGPLVCNDNGRGVLV--------GIVswGSGCA---RPNYPGVYTRVSSYLDWIQ 230
|
..
gi 973216831 1960 SI 1961
Cdd:cd00190 231 KT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1745-1954 |
3.87e-34 |
|
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: 132.03 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1745 GGQYAQEEYWPWMVSLHQNGNY-VCGGTLIASDWVMTAAQCLPSSvDVSEWSVGLGltVHNISYGfkGSVRVLDVTT--- 1820
Cdd:smart00020 4 GGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLG--SHDLSSG--EEGQVIKVSKvii 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1821 -----SSLSGSNIALLRLDTNVSYTGFILPICLAGASVSFPTGTECWVTSW-----DKVWENLVLKEVKMKITP---CEN 1887
Cdd:smart00020 79 hpnynPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWgrtseGAGSLPDTLQEVNVPIVSnatCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973216831 1888 VSS-----TDS-ICTEPLNLE----QRDSGSPLVCkQGSVWIQAsvidvnqtAITGNRSSTAvRALSPGVFTRVSRY 1954
Cdd:smart00020 159 AYSgggaiTDNmLCAGGLEGGkdacQGDSGGPLVC-NDGRWVLV--------GIVSWGSGCA-RPGKPGVYTRVSSY 225
|
|
| Trypsin |
pfam00089 |
Trypsin; |
1745-1954 |
2.37e-27 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 112.15 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1745 GGQYAQEEYWPWMVSLH-QNGNYVCGGTLIASDWVMTAAQCLPSSVDVSewsVGLGLTVHNISYGFKGSVRVLDVTTSSL 1823
Cdd:pfam00089 3 GGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVHPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1824 SGSN-----IALLRLDTNVSYTGFILPICLAGASVSFPTGTECWVTSWDKVWEN---LVLKEVKMKITPCENVSS----- 1890
Cdd:pfam00089 80 YNPDtldndIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLgpsDTLQEVTVPVVSRETCRSayggt 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973216831 1891 --TDSICTEPLNL--EQRDSGSPLVCKQGSVWIQASVIDVNQtaiTGNRsstavralsPGVFTRVSRY 1954
Cdd:pfam00089 160 vtDTMICAGAGGKdaCQGDSGGPLVCSDGELIGIVSWGYGCA---SGNY---------PGVYTPVSSY 215
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1725-1964 |
4.52e-27 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 112.44 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1725 TAGALATQVCGRPRLNPLLTGGQYAQEEYWPWMVSLHQNG---NYVCGGTLIASDWVMTAAQCLpSSVDVSEWSVGLGLT 1801
Cdd:COG5640 13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1802 VHNISYGFKgsVRVLDVTT-----SSLSGSNIALLRLDTNVSytgFILPICLAGASVSFPTGTECWVTSWDKVWENL--- 1873
Cdd:COG5640 92 DLSTSGGTV--VKVARIVVhpdydPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPgsq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1874 --VLKEVKMKITP---CENVSSTDS---ICTEPLNLE----QRDSGSPLVCKQGSVWIQASVIdvnqtaitgNRSSTAVR 1941
Cdd:COG5640 167 sgTLRKADVPVVSdatCAAYGGFDGgtmLCAGYPEGGkdacQGDSGGPLVVKDGGGWVLVGVV---------SWGGGPCA 237
|
250 260
....*....|....*....|...
gi 973216831 1942 ALSPGVFTRVSRYESFLRSIVGS 1964
Cdd:COG5640 238 AGYPGVYTRVSAYRDWIKSTAGG 260
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
36-268 |
7.50e-106 |
|
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: 337.73 E-value: 7.50e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 36 RIVGGQSAQPGSWPWQASLRLNGG-HTCGGTLINSQWVLTAAHCFSGSTtPSQWTVYLGVTDTGSSTNTVSRGVQQIIKH 114
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 115 PNYDSSTNNNDIALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTTLPSTLQEVQLPIIGNRQCgcl 194
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 195 NDVVFGANSVTGNMICAGVLQGGKDSCQGDSGGPLVCkQGSVWVQAGVVSFGEGCARPSLPGVYTRVSQYQDWI 268
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
37-269 |
3.27e-104 |
|
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: 333.09 E-value: 3.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 37 IVGGQSAQPGSWPWQASLRLN-GGHTCGGTLINSQWVLTAAHCFSGSTtPSQWTVYLGVTDTGSSTNT-VSRGVQQIIKH 114
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGgQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 115 PNYDSSTNNNDIALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTtLPSTLQEVQLPIIGNRQCgcl 194
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAEC--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 195 NDVVFGANSVTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSVWVQAGVVSFGEGCARPSLPGVYTRVSQYQDWIN 269
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
337-572 |
1.32e-102 |
|
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: 328.47 E-value: 1.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 337 IVGGNPAQEGSWPWQASLHYY-GQHMCGGSLINQQWVLTAAHCIPDPlNTYPWTVYLGRLTQFSSSPNELSRSVQQIIVH 415
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 416 PAYNSVTEDNDIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTGWGYTAEDGaTLPTTLQEVQLSIIGNRQCgcl 495
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAEC--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973216831 496 NDVVFGVNSVTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSSWVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWINTQ 572
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
336-569 |
5.01e-102 |
|
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: 326.56 E-value: 5.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 336 RIVGGNPAQEGSWPWQASLHYYG-QHMCGGSLINQQWVLTAAHCIPDPLNTyPWTVYLGRLTQFSSSPNELsRSVQQIIV 414
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGSHDLSSGEEGQV-IKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 415 HPAYNSVTEDNDIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTGWGYTAEDGATLPTTLQEVQLSIIGNRQCgc 494
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATC-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 495 lNDVVFGVNSVTGNMICAGVLQGGKDSCQGDSGGPLVCkQGSSWVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWI 569
Cdd:smart00020 157 -RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1463-1698 |
1.08e-96 |
|
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: 311.52 E-value: 1.08e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1463 IVGGDSAPEGYWPWQASLQYY-GYHFCGGSLINNQWVLTAAHCTYWISSMMVQVYLGKESQEGSNPHQVSRGVERIILHP 1541
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1542 NFDYMTLNNDIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTGWGNIADGVSLPNnkTLQEVQLPIIGKSQCgci 1621
Cdd:cd00190 81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAEC--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973216831 1622 SNLTFGVNFITDNMICAGVLDNRKSPCNGDSGGPLVCKQGSAWVQAGIVSFGYGCARPNVPGVYTRMSQYQDWINRQ 1698
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1462-1695 |
1.63e-93 |
|
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: 302.29 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1462 RIVGGDSAPEGYWPWQASLQYYG-YHFCGGSLINNQWVLTAAHCTYWISSMMVQVYLGKESQEGSNPHQVsRGVERIILH 1540
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1541 PNFDYMTLNNDIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTGWGNIADGvSLPNNKTLQEVQLPIIGKSQCgc 1620
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVSNATC-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1621 iSNLTFGVNFITDNMICAGVLDNRKSPCNGDSGGPLVCkQGSAWVQAGIVSFGYGCARPNVPGVYTRMSQYQDWI 1695
Cdd:smart00020 157 -RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1177-1411 |
7.52e-93 |
|
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: 300.73 E-value: 7.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1177 IVGGDSAPEGYWPWQASLHHY-GQHICGGSLINHQWVLTAAHCVNGiSDGRQLTVYLGRQSQLGSNTHEVSRMVTMVIPH 1255
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1256 PGY--LNFDKDVALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTGWGNIAEGVFLtgNQALQEVQLSIIGNRQCTC 1333
Cdd:cd00190 80 PNYnpSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973216831 1334 LYnmiPVPDLITDNMICAGDLEGGKGSCQGDSGGPLVCKQGSSWVQAGVVSFAVGCARPSFPSVFARVSRFQDWINEQ 1411
Cdd:cd00190 158 AY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1176-1408 |
3.56e-90 |
|
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: 292.66 E-value: 3.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1176 RIVGGDSAPEGYWPWQASLH-HYGQHICGGSLINHQWVLTAAHCVNGiSDGRQLTVYLGRqSQLGSNTHEVSRMVTMVIP 1254
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-HDLSSGEEGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1255 HPGY--LNFDKDVALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTGWGNIAEGVfLTGNQALQEVQLSIIGNRQCT 1332
Cdd:smart00020 79 HPNYnpSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGA-GSLPDTLQEVNVPIVSNATCR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973216831 1333 CLYnmiPVPDLITDNMICAGDLEGGKGSCQGDSGGPLVCkQGSSWVQAGVVSFAVGCARPSFPSVFARVSRFQDWI 1408
Cdd:smart00020 158 RAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
897-1130 |
1.65e-86 |
|
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: 282.24 E-value: 1.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 897 IAGGQSAQEGYWPWQASLHYS-GYYMCGGSLINHQWVLSAAGCVYRiSDNRQLTVYLGRQNQMNSNPNEVSRRITRVIPH 975
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 976 PDFNSTTFTNDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTGWGNTDDYSFYAQILQEAQVPIMGNRQCGCLY 1055
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1056 aeaFGVNSITENMICGGVPDGGNATCLGDSGGPLVCKQGSAWIQAGVVKYRDGCTPSSLPGVYTRVSQYQDWINE 1130
Cdd:cd00190 160 ---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
896-1128 |
2.18e-84 |
|
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: 276.10 E-value: 2.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 896 RIAGGQSAQEGYWPWQASLHYSGYYM-CGGSLINHQWVLSAAGCVYRiSDNRQLTVYLGRQNqMNSNPNEVSRRITRVIP 974
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHD-LSSGEEGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 975 HPDFNSTTFTNDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTGWGNTDDYSF-YAQILQEAQVPIMGNRQCGC 1053
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSNATCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1054 LYaeaFGVNSITENMICGGVPDGGNATCLGDSGGPLVCkQGSAWIQAGVVKYRDGCTPSSLPGVYTRVSQYQDWI 1128
Cdd:smart00020 159 AY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
618-850 |
1.68e-82 |
|
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: 270.69 E-value: 1.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 618 IVGGVSAPEGYWPWQVRIYYF-GYYRCGGSLINQQWVLTAATCVYSAWVSELKVYLGRQTQAGPNSQELSKKVKQVLLHP 696
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 697 DYSSS--NNDIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAGWGFTAEFMSLPgnQTLQEVQLPIIGNRQCGCL 774
Cdd:cd00190 81 NYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECKRA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973216831 775 YdlnYGPGSVNDSMICAGQPNGGKDTCWGDEGGPLICKQGSSWVQAGIVRPGEGCGQTDLPGLYTRVSQYEDWIYQ 850
Cdd:cd00190 159 Y---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
617-848 |
4.98e-82 |
|
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: 269.55 E-value: 4.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 617 RIVGGVSAPEGYWPWQVRIYYFGYY-RCGGSLINQQWVLTAATCVYSAWVSELKVYLGR-QTQAGPNSQELskKVKQVLL 694
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShDLSSGEEGQVI--KVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 695 HPDYSSSN--NDIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAGWGFTAEfMSLPGNQTLQEVQLPIIGNRQCG 772
Cdd:smart00020 79 HPNYNPSTydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973216831 773 CLYdlnYGPGSVNDSMICAGQPNGGKDTCWGDEGGPLICkQGSSWVQAGIVRPGEGCGQTDLPGLYTRVSQYEDWI 848
Cdd:smart00020 158 RAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
35-274 |
1.70e-80 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 266.52 E-value: 1.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 35 TRIVGGQSAQPGSWPWQASLRLNGG---HTCGGTLINSQWVLTAAHCFSGsTTPSQWTVYLGVTDTGSSTNTVsRGVQQI 111
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTV-VKVARI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 112 IKHPNYDSSTNNNDIALMKLSSSVSFnnyIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTTLPSTLQEVQLPIIGNRQC 191
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 192 GCLNDVVfgansvTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSVWVQAGVVSFGEGCARPSLPGVYTRVSQYQDWINGQ 271
Cdd:COG5640 184 AAYGGFD------GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257
|
...
gi 973216831 272 VGS 274
Cdd:COG5640 258 AGG 260
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
335-574 |
1.44e-78 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 260.74 E-value: 1.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 335 PRIVGGNPAQEGSWPWQASLHY---YGQHMCGGSLINQQWVLTAAHCIPDPLNTyPWTVYLGRLTQFSSSPNElsRSVQQ 411
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIGSTDLSTSGGTV--VKVAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 412 IIVHPAYNSVTEDNDIALMRLSSPVSFtsyIQPICLADNSSSFYNGTSCWVTGWGYTAEDGATLPTTLQEVQLSIIGNRQ 491
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDAT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 492 CGCLNDVVfgvnsvTGNMICAGVLQGGKDSCQGDSGGPLVCKQGSSWVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWINT 571
Cdd:COG5640 183 CAAYGGFD------GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256
|
...
gi 973216831 572 QVG 574
Cdd:COG5640 257 TAG 259
|
|
| Trypsin |
pfam00089 |
Trypsin; |
337-569 |
5.26e-78 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 257.37 E-value: 5.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 337 IVGGNPAQEGSWPWQASLHYY-GQHMCGGSLINQQWVLTAAHCIPDPLNtypWTVYLGRLTQFSSSPNELSRSVQQIIVH 415
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 416 PAYNSVTEDNDIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTGWGYTAEDGatLPTTLQEVQLSIIGNRQCGCL 495
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 496 NDvvfgvNSVTGNMICAGVlqGGKDSCQGDSGGPLVCKQGsswVQAGVVSFGEGCAQPNFPGVYTRVSQYKDWI 569
Cdd:pfam00089 156 YG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
37-268 |
1.51e-76 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 253.13 E-value: 1.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 37 IVGGQSAQPGSWPWQASLRLNGG-HTCGGTLINSQWVLTAAHCFSGSttpSQWTVYLGVTDTGSSTNTVSRG-VQQIIKH 114
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFdVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 115 PNYDSSTNNNDIALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTGWGTTVEGGTtlPSTLQEVQLPIIGNRQCGCl 194
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRS- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 195 ndvvFGANSVTGNMICAGVlqGGKDSCQGDSGGPLVCKQGSVwvqAGVVSFGEGCARPSLPGVYTRVSQYQDWI 268
Cdd:pfam00089 155 ----AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGEL---IGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
1463-1695 |
4.70e-74 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 246.20 E-value: 4.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1463 IVGGDSAPEGYWPWQASLQYY-GYHFCGGSLINNQWVLTAAHCTYwiSSMMVQVYLGKESQEGSNPHQVSRGVERIILHP 1541
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1542 NFDYMTLNNDIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTGWGNIADGVSlpnNKTLQEVQLPIIGKSQCGCI 1621
Cdd:pfam00089 79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 1622 SNLTfgvnfITDNMICAGvlDNRKSPCNGDSGGPLVCKQGSAwvqAGIVSFGYGCARPNVPGVYTRMSQYQDWI 1695
Cdd:pfam00089 156 YGGT-----VTDTMICAG--AGGKDACQGDSGGPLVCSDGEL---IGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1461-1699 |
3.06e-68 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 231.08 E-value: 3.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1461 PRIVGGDSAPEGYWPWQASLQY---YGYHFCGGSLINNQWVLTAAHCTYWISSMMVQVYLGKESQEGSNPhqVSRGVERI 1537
Cdd:COG5640 29 PAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG--TVVKVARI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1538 ILHPNFDYMTLNNDIALLKLSSPVTFtdyIQPICLAANSSSFHTGTSCWVTGWGNIADGVSLPNNkTLQEVQLPIIGKSQ 1617
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSG-TLRKADVPVVSDAT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1618 CGCISNltfgvnFITDNMICAGVLDNRKSPCNGDSGGPLVCKQGSAWVQAGIVSFGYGCARPNVPGVYTRMSQYQDWINR 1697
Cdd:COG5640 183 CAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256
|
..
gi 973216831 1698 QV 1699
Cdd:COG5640 257 TA 258
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1157-1416 |
1.90e-67 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 228.77 E-value: 1.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1157 ALGTTPVTPSECGKAPLSPRIVGGDSAPEGYWPWQASLHH---YGQHICGGSLINHQWVLTAAHCVNGISDGrQLTVYLG 1233
Cdd:COG5640 11 AAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1234 RQSqLGSNTHEVSRmVTMVIPHPGYLN--FDKDVALLRLNKPVSFtayIQPICLASNISSFQNGTQCWVTGWGNIAEGVf 1311
Cdd:COG5640 90 STD-LSTSGGTVVK-VARIVVHPDYDPatPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGP- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1312 ltGNQA--LQEVQLSIIGNRQCTclynmiPVPDLITDNMICAGDLEGGKGSCQGDSGGPLVCKQGSSWVQAGVVSFAVGC 1389
Cdd:COG5640 164 --GSQSgtLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGP 235
|
250 260
....*....|....*....|....*..
gi 973216831 1390 ARPSFPSVFARVSRFQDWINEQVGSAT 1416
Cdd:COG5640 236 CAAGYPGVYTRVSAYRDWIKSTAGGLG 262
|
|
| Trypsin |
pfam00089 |
Trypsin; |
1177-1408 |
6.67e-65 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 220.01 E-value: 6.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1177 IVGGDSAPEGYWPWQASLHHY-GQHICGGSLINHQWVLTAAHCVngiSDGRQLTVYLGRQSQLGSNTHEVSRMVTMVIPH 1255
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1256 PGY--LNFDKDVALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTGWGNIAEGVFltgNQALQEVQLSIIGNRQCTC 1333
Cdd:pfam00089 78 PNYnpDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973216831 1334 LYnmipvPDLITDNMICAGdlEGGKGSCQGDSGGPLVCKQGsswVQAGVVSFAVGCARPSFPSVFARVSRFQDWI 1408
Cdd:pfam00089 155 AY-----GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
897-1128 |
1.34e-64 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 218.85 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 897 IAGGQSAQEGYWPWQASLHY-SGYYMCGGSLINHQWVLSAAGCVYrisDNRQLTVYLGRQNQMNSNPNEVSRRITRVIPH 975
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 976 PDFNSTTFTNDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTGWGNTDDYSfYAQILQEAQVPIMGNRQCGCLY 1055
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973216831 1056 AeafgvNSITENMICGGvpDGGNATCLGDSGGPLVCKQGsawIQAGVVKYRDGCTPSSLPGVYTRVSQYQDWI 1128
Cdd:pfam00089 157 G-----GTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
604-853 |
2.12e-62 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 214.51 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 604 VASSECGKAPLSTRIVGGVSAPEGYWPWQVRIYY---FGYYRCGGSLINQQWVLTAATCVYSAWVSELKVYLGRQTQAGP 680
Cdd:COG5640 17 LALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 681 NSQELskKVKQVLLHPDYSSS--NNDIALLELRSPVTFtnyIQPICLAANSSSFYTGTSCWVAGWGFTAEFMSlPGNQTL 758
Cdd:COG5640 97 GGTVV--KVARIVVHPDYDPAtpGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 759 QEVQLPIIGNRQCgclydlNYGPGSVNDSMICAGQPNGGKDTCWGDEGGPLICKQGSSWVQAGIVRPGEGCGQTDLPGLY 838
Cdd:COG5640 171 RKADVPVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVY 244
|
250
....*....|....*
gi 973216831 839 TRVSQYEDWIYQMVG 853
Cdd:COG5640 245 TRVSAYRDWIKSTAG 259
|
|
| Trypsin |
pfam00089 |
Trypsin; |
618-848 |
4.95e-62 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 211.53 E-value: 4.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 618 IVGGVSAPEGYWPWQVRIYYF-GYYRCGGSLINQQWVLTAATCVYSAwvSELKVYLGRQTQAGPNSQELSKKVKQVLLHP 696
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 697 DYSSS--NNDIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAGWGFTAEFMSlpgNQTLQEVQLPIIGNRQCGCL 774
Cdd:pfam00089 79 NYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973216831 775 YdlnygPGSVNDSMICAGqpNGGKDTCWGDEGGPLICKQGsswVQAGIVRPGEGCGQTDLPGLYTRVSQYEDWI 848
Cdd:pfam00089 156 Y-----GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
888-1130 |
1.39e-61 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 212.20 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 888 CGQAPLRTRIAGGQSAQEGYWPWQASLHYSG---YYMCGGSLINHQWVLSAAGCVYRISdNRQLTVYLGRqNQMNSNPNE 964
Cdd:COG5640 22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGS-TDLSTSGGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 965 VsRRITRVIPHPDFNSTTFTNDIALLRLQTPVNFtnyIQPICLADNSSSFSTGTSCWVTGWGNTD-DYSFYAQILQEAQV 1043
Cdd:COG5640 100 V-VKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1044 PIMGNRQCgclyaeAFGVNSITENMICGGVPDGGNATCLGDSGGPLVCKQGSAWIQAGVVKY-RDGCTPSSlPGVYTRVS 1122
Cdd:COG5640 176 PVVSDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCAAGY-PGVYTRVS 248
|
....*...
gi 973216831 1123 QYQDWINE 1130
Cdd:COG5640 249 AYRDWIKS 256
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1745-1961 |
1.27e-35 |
|
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: 136.25 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1745 GGQYAQEEYWPWMVSLHQN-GNYVCGGTLIASDWVMTAAQCLPSSvDVSEWSVGLGLTVHNISYGFKGSVRVLDVTT--- 1820
Cdd:cd00190 3 GGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVhpn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1821 --SSLSGSNIALLRLDTNVSYTGFILPICLAGASVSFPTGTECWVTSWDKVWENL----VLKEVKMKITP---CENVSST 1891
Cdd:cd00190 82 ynPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplpdVLQEVNVPIVSnaeCKRAYSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1892 DS------ICTEPLNLE----QRDSGSPLVCKQGSVWIQAsvidvnqtAIT--GNRSStavRALSPGVFTRVSRYESFLR 1959
Cdd:cd00190 162 GGtitdnmLCAGGLEGGkdacQGDSGGPLVCNDNGRGVLV--------GIVswGSGCA---RPNYPGVYTRVSSYLDWIQ 230
|
..
gi 973216831 1960 SI 1961
Cdd:cd00190 231 KT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1745-1954 |
3.87e-34 |
|
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: 132.03 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1745 GGQYAQEEYWPWMVSLHQNGNY-VCGGTLIASDWVMTAAQCLPSSvDVSEWSVGLGltVHNISYGfkGSVRVLDVTT--- 1820
Cdd:smart00020 4 GGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLG--SHDLSSG--EEGQVIKVSKvii 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1821 -----SSLSGSNIALLRLDTNVSYTGFILPICLAGASVSFPTGTECWVTSW-----DKVWENLVLKEVKMKITP---CEN 1887
Cdd:smart00020 79 hpnynPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWgrtseGAGSLPDTLQEVNVPIVSnatCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973216831 1888 VSS-----TDS-ICTEPLNLE----QRDSGSPLVCkQGSVWIQAsvidvnqtAITGNRSSTAvRALSPGVFTRVSRY 1954
Cdd:smart00020 159 AYSgggaiTDNmLCAGGLEGGkdacQGDSGGPLVC-NDGRWVLV--------GIVSWGSGCA-RPGKPGVYTRVSSY 225
|
|
| Trypsin |
pfam00089 |
Trypsin; |
1745-1954 |
2.37e-27 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 112.15 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1745 GGQYAQEEYWPWMVSLH-QNGNYVCGGTLIASDWVMTAAQCLPSSVDVSewsVGLGLTVHNISYGFKGSVRVLDVTTSSL 1823
Cdd:pfam00089 3 GGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVHPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1824 SGSN-----IALLRLDTNVSYTGFILPICLAGASVSFPTGTECWVTSWDKVWEN---LVLKEVKMKITPCENVSS----- 1890
Cdd:pfam00089 80 YNPDtldndIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLgpsDTLQEVTVPVVSRETCRSayggt 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973216831 1891 --TDSICTEPLNL--EQRDSGSPLVCKQGSVWIQASVIDVNQtaiTGNRsstavralsPGVFTRVSRY 1954
Cdd:pfam00089 160 vtDTMICAGAGGKdaCQGDSGGPLVCSDGELIGIVSWGYGCA---SGNY---------PGVYTPVSSY 215
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1725-1964 |
4.52e-27 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 112.44 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1725 TAGALATQVCGRPRLNPLLTGGQYAQEEYWPWMVSLHQNG---NYVCGGTLIASDWVMTAAQCLpSSVDVSEWSVGLGLT 1801
Cdd:COG5640 13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1802 VHNISYGFKgsVRVLDVTT-----SSLSGSNIALLRLDTNVSytgFILPICLAGASVSFPTGTECWVTSWDKVWENL--- 1873
Cdd:COG5640 92 DLSTSGGTV--VKVARIVVhpdydPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPgsq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1874 --VLKEVKMKITP---CENVSSTDS---ICTEPLNLE----QRDSGSPLVCKQGSVWIQASVIdvnqtaitgNRSSTAVR 1941
Cdd:COG5640 167 sgTLRKADVPVVSdatCAAYGGFDGgtmLCAGYPEGGkdacQGDSGGPLVVKDGGGWVLVGVV---------SWGGGPCA 237
|
250 260
....*....|....*....|...
gi 973216831 1942 ALSPGVFTRVSRYESFLRSIVGS 1964
Cdd:COG5640 238 AGYPGVYTRVSAYRDWIKSTAGG 260
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
57-270 |
1.22e-11 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 65.85 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 57 NGGHTCGGTLINSQWVLTAAHCFSGSTT---PSQWTVYLGVTDTGSSTNTVSRgvqqIIKHPNYDSSTN-NNDIALMKLS 132
Cdd:COG3591 9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATR----FRVPPGWVASGDaGYDYALLRLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 133 SSVSfnNYIQPVCLAnTSSTFYNGTSCWVTGWGttveGGTtlpstlqevqlPIIGNRQCGCLndvVFGANSvtgnmicaG 212
Cdd:COG3591 85 EPLG--DTTGWLGLA-FNDAPLAGEPVTIIGYP----GDR-----------PKDLSLDCSGR---VTGVQG--------N 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 973216831 213 VLQGGKDSCQGDSGGPLVCKQGSVWVQAGVVSFG-EGCARPSLPGVYTRVSQYQDWING 270
Cdd:COG3591 136 RLSYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGgADRANTGVRLTSAIVAALRAWASA 194
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
358-547 |
2.83e-11 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 64.70 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 358 GQHMCGGSLINQQWVLTAAHCIPDPLNTYP---WTVYLGrltqFSSSPNElSRSVQQIIVHPAY-NSVTEDNDIALMRLS 433
Cdd:COG3591 10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWatnIVFVPG----YNGGPYG-TATATRFRVPPGWvASGDAGYDYALLRLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 434 SPVSFTSYIQPIclaDNSSSFYNGTSCWVTGWGYTAEDGATLpttlqevqlsiignrQCGCLndvvfgVNSVTGNmicag 513
Cdd:COG3591 85 EPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDRPKDLSL---------------DCSGR------VTGVQGN----- 135
|
170 180 190
....*....|....*....|....*....|....
gi 973216831 514 VLQGGKDSCQGDSGGPLVCKQGSSWVQAGVVSFG 547
Cdd:COG3591 136 RLSYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
1198-1388 |
1.63e-08 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 56.61 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1198 GQHICGGSLINHQWVLTAAHCVNGISDGR---QLTVYLGRQSQlGSNTHEVSRMVTmvipHPGYL---NFDKDVALLRLN 1271
Cdd:COG3591 10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGG-PYGTATATRFRV----PPGWVasgDAGYDYALLRLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1272 KPVSFTAYIQPIclaSNISSFQNGTQCWVTGWGniaegvfltGNQALQEVQlsiignrQCTCLYNMIPVPDLITDNMIca 1351
Cdd:COG3591 85 EPLGDTTGWLGL---AFNDAPLAGEPVTIIGYP---------GDRPKDLSL-------DCSGRVTGVQGNRLSYDCDT-- 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 973216831 1352 gdleggkgsCQGDSGGPLVCKQGSSWVQAGVVSFAVG 1388
Cdd:COG3591 144 ---------TGGSSGSPVLDDSDGGGRVVGVHSAGGA 171
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
908-1024 |
3.25e-08 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 53.71 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 908 WPWQASLHYSGYYMCGGSLINHQWVLSAAGCVYRISDNRQ-LTVYLGRQNQMNS--NPNEVSRRItrviphpDFNSTTFT 984
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGAKTLKSieGPYEQIVRV-------DCRHDIPE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 973216831 985 NDIALLRLQTPVNFTNYIQPICLADNSSSFSTGTSCWVTG 1024
Cdd:pfam09342 74 SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
629-742 |
5.92e-08 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 52.94 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 629 WPWQVRIYYFGYYRCGGSLINQQWVLTAATCVY--SAWVSELKVYLG----RQTQAGPNSQelskkVKQVLLHPDYSSSN 702
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRdtNLRHQYISVVLGgaktLKSIEGPYEQ-----IVRVDCRHDIPESE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 973216831 703 ndIALLELRSPVTFTNYIQPICLAANSSSFYTGTSCWVAG 742
Cdd:pfam09342 76 --ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
48-163 |
2.91e-07 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 51.01 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 48 WPWQASLRLNGGHTCGGTLINSQWVLTAAHCFSGSTTPSQwtvYLGVTDTGSSTNTVSRG-VQQIIKHPNYDSSTNNNdI 126
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQ---YISVVLGGAKTLKSIEGpYEQIVRVDCRHDIPESE-I 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 973216831 127 ALMKLSSSVSFNNYIQPVCLANTSSTFYNGTSCWVTG 163
Cdd:pfam09342 77 SLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
1754-1861 |
3.33e-07 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 50.62 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1754 WPWMVSLHQNGNYVCGGTLIASDWVMTAAQCLpSSVDVSEWSVGLGLTVHNISYGFKG---SVRVLDvTTSSLSGSNIAL 1830
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCL-RDTNLRHQYISVVLGGAKTLKSIEGpyeQIVRVD-CRHDIPESEISL 78
|
90 100 110
....*....|....*....|....*....|.
gi 973216831 1831 LRLDTNVSYTGFILPICLAGASVSFPTGTEC 1861
Cdd:pfam09342 79 LHLASPASFSNHVLPTFVPETRNENEKDNEC 109
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
639-823 |
4.91e-07 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 52.37 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 639 GYYRCGGSLINQQWVLTAATCVYS----AWVSELKVYLGRqtQAGPNSQElskKVKQVLLHPDYSSS---NNDIALLELR 711
Cdd:COG3591 10 GGGVCTGTLIGPNLVLTAGHCVYDgaggGWATNIVFVPGY--NGGPYGTA---TATRFRVPPGWVASgdaGYDYALLRLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 712 SPVTFTNYIQPIclaANSSSFYTGTSCWVAGWgftaefmslPGNQtlqevqlPIIGNRQCGCLYdLNYGPGSVndSMICa 791
Cdd:COG3591 85 EPLGDTTGWLGL---AFNDAPLAGEPVTIIGY---------PGDR-------PKDLSLDCSGRV-TGVQGNRL--SYDC- 141
|
170 180 190
....*....|....*....|....*....|..
gi 973216831 792 gqpnggkDTCWGDEGGPLICKQGSSWVQAGIV 823
Cdd:COG3591 142 -------DTTGGSSGSPVLDDSDGGGRVVGVH 166
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
1484-1675 |
1.37e-06 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 50.83 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1484 GYHFCGGSLINNQWVLTAAHCTY------WISSmmVQVYLGKEsqegsNPHQVSRGVERIILHPNFDYMTL-NNDIALLK 1556
Cdd:COG3591 10 GGGVCTGTLIGPNLVLTAGHCVYdgagggWATN--IVFVPGYN-----GGPYGTATATRFRVPPGWVASGDaGYDYALLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1557 LSSPVtfTDYIQPICLAANSSSFhTGTSCWVTGWgniadgvslPNNKTLQEVQlpiigksQCGCIsnltfgVNFITDNMI 1636
Cdd:COG3591 83 LDEPL--GDTTGWLGLAFNDAPL-AGEPVTIIGY---------PGDRPKDLSL-------DCSGR------VTGVQGNRL 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 973216831 1637 CAGVldnrkSPCNGDSGGPLVCKQGSAWVQAGIVSFGYG 1675
Cdd:COG3591 138 SYDC-----DTTGGSSGSPVLDDSDGGGRVVGVHSAGGA 171
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
348-464 |
3.10e-06 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 47.93 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 348 WPWQASLHYYGQHMCGGSLINQQWVLTAAHCIPD-PLNTYPWTVYLGRLTQFSS--SPNElsrsvqQIIVHPAYNSVTED 424
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKTLKSieGPYE------QIVRVDCRHDIPES 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 973216831 425 NdIALMRLSSPVSFTSYIQPICLADNSSSFYNGTSCWVTG 464
Cdd:pfam09342 75 E-ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
916-1103 |
3.30e-06 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 49.67 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 916 YSGYYMCGGSLINHQWVLSAAGCVYRISDNR---QLTVYLGRQNQMNSnpnevSRRITRVIPHPDF-NSTTFTNDIALLR 991
Cdd:COG3591 8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGPYG-----TATATRFRVPPGWvASGDAGYDYALLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 992 LQTPVnfTNYIQPICLADNSSSFsTGTSCWVTGWGNTDDYSFYaqilqeaqvpimgnRQCGCLyaeafgVNSITENMICg 1071
Cdd:COG3591 83 LDEPL--GDTTGWLGLAFNDAPL-AGEPVTIIGYPGDRPKDLS--------------LDCSGR------VTGVQGNRLS- 138
|
170 180 190
....*....|....*....|....*....|..
gi 973216831 1072 gvpdGGNATCLGDSGGPLVCKQGSAWIQAGVV 1103
Cdd:COG3591 139 ----YDCDTTGGSSGSPVLDDSDGGGRVVGVH 166
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
1188-1302 |
3.62e-06 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 47.93 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1188 WPWQASLHHYGQHICGGSLINHQWVLTAAHCVNGISDGRQ-LTVYLGRQSQLGS--NTHEVSRMVTMVIPHPgylnfDKD 1264
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGAKTLKSieGPYEQIVRVDCRHDIP-----ESE 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 973216831 1265 VALLRLNKPVSFTAYIQPICLASNISSFQNGTQCWVTG 1302
Cdd:pfam09342 76 ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
1474-1589 |
1.59e-05 |
|
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.
Pssm-ID: 286432 Cd Length: 116 Bit Score: 46.00 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1474 WPWQASLQYYGYHFCGGSLINNQWVLTAAHCTYWIS--SMMVQVYLG--KESQEGSNPHQVSRGVEriilhpNFDYMTLN 1549
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNlrHQYISVVLGgaKTLKSIEGPYEQIVRVD------CRHDIPES 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 973216831 1550 NdIALLKLSSPVTFTDYIQPICLAANSSSFHTGTSCWVTG 1589
Cdd:pfam09342 75 E-ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
1763-1947 |
4.14e-03 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 40.43 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1763 NGNYVCGGTLIASDWVMTAAQCLPSSVD---VSEWSVGLGLtvHNISYGFKGSVRVL---DVTTSSLSGSNIALLRLDTN 1836
Cdd:COG3591 9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGY--NGGPYGTATATRFRvppGWVASGDAGYDYALLRLDEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973216831 1837 VSYTGFILPIclaGASVSFPTGTECWVTS--WDKVwENLVLKEvkmkitPCENVSSTDSICTEPLNLEQRDSGSPLVCKQ 1914
Cdd:COG3591 87 LGDTTGWLGL---AFNDAPLAGEPVTIIGypGDRP-KDLSLDC------SGRVTGVQGNRLSYDCDTTGGSSGSPVLDDS 156
|
170 180 190
....*....|....*....|....*....|...
gi 973216831 1915 GSVWIQASVIdvnqTAITGNRSSTAVRALSPGV 1947
Cdd:COG3591 157 DGGGRVVGVH----SAGGADRANTGVRLTSAIV 185
|
|
| |
