|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1-171 |
1.24e-61 |
|
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: 206.74 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLpwVLQEVEL 80
Cdd:cd00190 70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:cd00190 148 PIVSNAECKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTR 221
|
170
....*....|.
gi 1720424624 161 VAPYESWIREH 171
Cdd:cd00190 222 VSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1-168 |
2.53e-57 |
|
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: 194.82 E-value: 2.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVEL 80
Cdd:smart00020 70 VIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:smart00020 149 PIVSNATCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTR 221
|
....*...
gi 1720424624 161 VAPYESWI 168
Cdd:smart00020 222 VSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
2-168 |
1.25e-42 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 154.14 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 2 RSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlplPWVLQEVELR 81
Cdd:pfam00089 69 FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 82 LLGEAACQCLYSRPgpfnltfqLLPGMLCAGYpaGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:pfam00089 146 VVSRETCRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPV 212
|
....*..
gi 1720424624 162 APYESWI 168
Cdd:pfam00089 213 SSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
2-172 |
1.32e-38 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 144.02 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 2 RSVATILIPDNYSTVELGADLALLRLASPAklgPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVELR 81
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 82 LLGEAACQcLYSRPGPfnltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:COG5640 177 VVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRV 247
|
170
....*....|.
gi 1720424624 162 APYESWIREHV 172
Cdd:COG5640 248 SAYRDWIKSTA 258
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
494-676 |
5.51e-22 |
|
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: 95.42 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSLPQGHQVSRSVVSIrlpRHLGLRPP 572
Cdd:cd00190 12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 573 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW-----KNPQDRVPVVAAVSILTPRLCHCLY--PGIL 638
Cdd:cd00190 86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYsyGGTI 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720424624 639 TPGTFCVLYSEGQEDRCEVTSAPPLLCQTeEGPWVLVG 676
Cdd:cd00190 166 TDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVG 202
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
494-676 |
3.49e-20 |
|
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: 90.04 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSTTVPYIEVYLGRAGVSSlpQGHQVSRSVVSIRlpRHLGLRPP 572
Cdd:smart00020 13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 573 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHCLYPG--I 637
Cdd:smart00020 86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtSEGAGSLPDTlqeVNVPIVSNATCRRAYSGggA 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720424624 638 LTPGTFCVLYSEGQEDRCEVTSAPPLLCQTEEgpWVLVG 676
Cdd:smart00020 166 ITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR--WVLVG 202
|
|
| Trypsin |
pfam00089 |
Trypsin; |
494-665 |
7.78e-17 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 80.18 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSttvpyIEVYLGRAGVSSlPQGHQVSRSVVSIRlpRHLGLRPP 572
Cdd:pfam00089 12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLGAHNIVL-REGGEQKFDVEKII--VHPNYNPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 573 -----LALLELNSRVEPSPSALPICL-HPGGIPS-GASCWVLGWKNP-QDRVPVV---AAVSILTPRLCHCLYPGILTPG 641
Cdd:pfam00089 84 tldndIALLKLESPVTLGDTVRPICLpDASSDLPvGTTCTVSGWGNTkTLGPSDTlqeVTVPVVSRETCRSAYGGTVTDT 163
|
170 180
....*....|....*....|....
gi 1720424624 642 TFCVLYseGQEDRCEVTSAPPLLC 665
Cdd:pfam00089 164 MICAGA--GGKDACQGDSGGPLVC 185
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
212-356 |
7.37e-16 |
|
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: 77.33 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 212 RPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLDSPHDFetWRVLL----PSRPEEE---RVARLVAHENA-SRD 282
Cdd:smart00020 9 NIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSN--IRVRLgshdLSSGEEGqviKVSKVIIHPNYnPST 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720424624 283 FASDLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGELAPGSSA----QLEAQLLNGWWCHCLYGRQG 356
Cdd:smart00020 87 YDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtlqEVNVPIVSNATCRRAYSGGG 164
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
212-419 |
7.89e-16 |
|
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: 77.32 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 212 RPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLDSPHdfETWRVLL--------PSRPEEERVARLVAHENASRD 282
Cdd:cd00190 8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 283 FAS-DLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGELAPGSSAQL-EAQL--LNGWWCHCLYGrqget 358
Cdd:cd00190 86 TYDnDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS----- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720424624 359 vPRPGDPPHLLCpAYQEEEEAGLCwvssrnslqksrpdqdpAGDSSWSLLCREEGTWFLAG 419
Cdd:cd00190 161 -YGGTITDNMLC-AGGLEGGKDAC-----------------QGDSGGPLVCNDNGRGVLVG 202
|
|
| Trypsin |
pfam00089 |
Trypsin; |
208-338 |
6.59e-15 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 74.40 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 208 GKAPRPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFlDSPHDFETW---RVLLPSRPEEER--VARLVAHENA-S 280
Cdd:pfam00089 4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV-SGASDVKVVlgaHNIVLREGGEQKfdVEKIIVHPNYnP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720424624 281 RDFASDLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGElAPGSSAQL 338
Cdd:pfam00089 83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK-TLGPSDTL 139
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
494-703 |
1.06e-12 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 68.91 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSlpQGHQVsRSVVSIRlpRHLGLR 570
Cdd:COG5640 42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLST--SGGTV-VKVARIV--VHPDYD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 571 PP-----LALLELNsrvEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHcLYPGI 637
Cdd:COG5640 114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtSEGPGSQSGTlrkADVPVVSDATCA-AYGGF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720424624 638 LTPGTFCVLYSEGQEDRCEVTSAPPLLcQTEEGPWVLVGMAVRGNRE-------LFAAIGPEATWISQTVGEA 703
Cdd:COG5640 190 DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIKSTAGGL 261
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
1-171 |
1.24e-61 |
|
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: 206.74 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLpwVLQEVEL 80
Cdd:cd00190 70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:cd00190 148 PIVSNAECKRAYSYGGTIT------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTR 221
|
170
....*....|.
gi 1720424624 161 VAPYESWIREH 171
Cdd:cd00190 222 VSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
1-168 |
2.53e-57 |
|
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: 194.82 E-value: 2.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 1 MRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVEL 80
Cdd:smart00020 70 VIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 81 RLLGEAACQCLYSRPGPFNltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDgGRWFLAGITSFGFGCGRRNRPGVFTA 160
Cdd:smart00020 149 PIVSNATCRRAYSGGGAIT------DNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTR 221
|
....*...
gi 1720424624 161 VAPYESWI 168
Cdd:smart00020 222 VSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
2-168 |
1.25e-42 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 154.14 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 2 RSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlplPWVLQEVELR 81
Cdd:pfam00089 69 FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 82 LLGEAACQCLYSRPgpfnltfqLLPGMLCAGYpaGRRDTCQGDSGGPLVCEDGgrwFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:pfam00089 146 VVSRETCRSAYGGT--------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPV 212
|
....*..
gi 1720424624 162 APYESWI 168
Cdd:pfam00089 213 SSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
2-172 |
1.32e-38 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 144.02 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 2 RSVATILIPDNYSTVELGADLALLRLASPAklgPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPlPLPWVLQEVELR 81
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 82 LLGEAACQcLYSRPGPfnltfqllPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAV 161
Cdd:COG5640 177 VVSDATCA-AYGGFDG--------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRV 247
|
170
....*....|.
gi 1720424624 162 APYESWIREHV 172
Cdd:COG5640 248 SAYRDWIKSTA 258
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
494-676 |
5.51e-22 |
|
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: 95.42 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSLPQGHQVSRSVVSIrlpRHLGLRPP 572
Cdd:cd00190 12 FPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSN---YTVRLGSHDLSSNEGGGQVIKVKKVI---VHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 573 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW-----KNPQDRVPVVAAVSILTPRLCHCLY--PGIL 638
Cdd:cd00190 86 tydndIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWgrtseGGPLPDVLQEVNVPIVSNAECKRAYsyGGTI 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720424624 639 TPGTFCVLYSEGQEDRCEVTSAPPLLCQTeEGPWVLVG 676
Cdd:cd00190 166 TDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVG 202
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
494-676 |
3.49e-20 |
|
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: 90.04 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDR-VCTGILVAPGWVLAATHCilrLGSTTVPYIEVYLGRAGVSSlpQGHQVSRSVVSIRlpRHLGLRPP 572
Cdd:smart00020 13 FPWQVSLQYGGGRhFCGGSLISPRWVLTAAHC---VRGSDPSNIRVRLGSHDLSS--GEEGQVIKVSKVI--IHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 573 -----LALLELNSRVEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHCLYPG--I 637
Cdd:smart00020 86 tydndIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWgrtSEGAGSLPDTlqeVNVPIVSNATCRRAYSGggA 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720424624 638 LTPGTFCVLYSEGQEDRCEVTSAPPLLCQTEEgpWVLVG 676
Cdd:smart00020 166 ITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR--WVLVG 202
|
|
| Trypsin |
pfam00089 |
Trypsin; |
494-665 |
7.78e-17 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 80.18 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDRV-CTGILVAPGWVLAATHCILRLGSttvpyIEVYLGRAGVSSlPQGHQVSRSVVSIRlpRHLGLRPP 572
Cdd:pfam00089 12 FPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASD-----VKVVLGAHNIVL-REGGEQKFDVEKII--VHPNYNPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 573 -----LALLELNSRVEPSPSALPICL-HPGGIPS-GASCWVLGWKNP-QDRVPVV---AAVSILTPRLCHCLYPGILTPG 641
Cdd:pfam00089 84 tldndIALLKLESPVTLGDTVRPICLpDASSDLPvGTTCTVSGWGNTkTLGPSDTlqeVTVPVVSRETCRSAYGGTVTDT 163
|
170 180
....*....|....*....|....
gi 1720424624 642 TFCVLYseGQEDRCEVTSAPPLLC 665
Cdd:pfam00089 164 MICAGA--GGKDACQGDSGGPLVC 185
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
212-356 |
7.37e-16 |
|
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: 77.33 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 212 RPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLDSPHDFetWRVLL----PSRPEEE---RVARLVAHENA-SRD 282
Cdd:smart00020 9 NIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSN--IRVRLgshdLSSGEEGqviKVSKVIIHPNYnPST 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720424624 283 FASDLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGELAPGSSA----QLEAQLLNGWWCHCLYGRQG 356
Cdd:smart00020 87 YDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtlqEVNVPIVSNATCRRAYSGGG 164
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
212-419 |
7.89e-16 |
|
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: 77.32 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 212 RPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFLDSPHdfETWRVLL--------PSRPEEERVARLVAHENASRD 282
Cdd:cd00190 8 KIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVYSSAP--SNYTVRLgshdlssnEGGGQVIKVKKVIVHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 283 FAS-DLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGELAPGSSAQL-EAQL--LNGWWCHCLYGrqget 358
Cdd:cd00190 86 TYDnDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLqEVNVpiVSNAECKRAYS----- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720424624 359 vPRPGDPPHLLCpAYQEEEEAGLCwvssrnslqksrpdqdpAGDSSWSLLCREEGTWFLAG 419
Cdd:cd00190 161 -YGGTITDNMLC-AGGLEGGKDAC-----------------QGDSGGPLVCNDNGRGVLVG 202
|
|
| Trypsin |
pfam00089 |
Trypsin; |
208-338 |
6.59e-15 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 74.40 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 208 GKAPRPGTWPWEAQVTVPGSTP-CYGALVSDRWVLAPASCFlDSPHDFETW---RVLLPSRPEEER--VARLVAHENA-S 280
Cdd:pfam00089 4 GDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV-SGASDVKVVlgaHNIVLREGGEQKfdVEKIIVHPNYnP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720424624 281 RDFASDLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGElAPGSSAQL 338
Cdd:pfam00089 83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK-TLGPSDTL 139
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
494-703 |
1.06e-12 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 68.91 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDR---VCTGILVAPGWVLAATHCILRLGSTTvpyIEVYLGRAGVSSlpQGHQVsRSVVSIRlpRHLGLR 570
Cdd:COG5640 42 YPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLST--SGGTV-VKVARIV--VHPDYD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 571 PP-----LALLELNsrvEPSPSALPICLHPGG--IPSGASCWVLGW---KNPQDRVPVV---AAVSILTPRLCHcLYPGI 637
Cdd:COG5640 114 PAtpgndIALLKLA---TPVPGVAPAPLATSAdaAAPGTPATVAGWgrtSEGPGSQSGTlrkADVPVVSDATCA-AYGGF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720424624 638 LTPGTFCVLYSEGQEDRCEVTSAPPLLcQTEEGPWVLVGMAVRGNRE-------LFAAIGPEATWISQTVGEA 703
Cdd:COG5640 190 DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPcaagypgVYTRVSAYRDWIKSTAGGL 261
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
494-543 |
8.38e-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: 45.62 E-value: 8.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720424624 494 WPWLTEVHVTGDRVCTGILVAPGWVLAATHCiLRLGSTTVPYIEVYLGRA 543
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSC-LRDTNLRHQYISVVLGGA 49
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
216-320 |
3.51e-03 |
|
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: 37.91 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 216 WPWEAQVTVPGSTPCYGALVSDRWVLAPASCFLDSPHDFETWRVLLPS-------RPEEERVARLVAHENASRdfaSDLA 288
Cdd:pfam09342 1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGaktlksiEGPYEQIVRVDCRHDIPE---SEIS 77
|
90 100 110
....*....|....*....|....*....|..
gi 1720424624 289 LLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHC 320
Cdd:pfam09342 78 LLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
504-615 |
3.73e-03 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 39.27 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424624 504 GDRVCTGILVAPGWVLAATHCILRLGSTTVPY-IEVYLGRAGvssLPQGHQVSRSVVSIRLPRHLGLRPP-LALLELNSR 581
Cdd:COG3591 10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnIVFVPGYNG---GPYGTATATRFRVPPGWVASGDAGYdYALLRLDEP 86
|
90 100 110
....*....|....*....|....*....|....
gi 1720424624 582 VEPSPSALPIcLHPGGIPSGASCWVLGWknPQDR 615
Cdd:COG3591 87 LGDTTGWLGL-AFNDAPLAGEPVTIIGY--PGDR 117
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
119-154 |
5.39e-03 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 38.89 E-value: 5.39e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1720424624 119 DTCQGDSGGPLVCEDGGRWFLAGITSFGfGCGRRNR 154
Cdd:COG3591 142 DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT 176
|
|
|