|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
4-233 |
1.98e-98 |
|
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: 306.14 E-value: 1.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 4 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 82
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 83 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 162
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878348173 163 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:smart00020 159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
629-855 |
2.83e-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: 300.73 E-value: 2.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 706
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 786
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878348173 787 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
306-536 |
6.89e-90 |
|
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: 283.78 E-value: 6.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 464
Cdd:cd00190 81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878348173 465 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 536
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Pneumo_att_G super family |
cl25814 |
Pneumovirinae attachment membrane glycoprotein G; |
485-635 |
3.02e-03 |
|
Pneumovirinae attachment membrane glycoprotein G; The actual alignment was detected with superfamily member pfam05539:
Pssm-ID: 114270 [Multi-domain] Cd Length: 408 Bit Score: 40.80 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 485 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 562
Cdd:pfam05539 155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 563 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 635
Cdd:pfam05539 223 GTTTSSNPEPQTEPPPSQRgpsgSPQHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRP 301
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
4-233 |
1.98e-98 |
|
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: 306.14 E-value: 1.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 4 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 82
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 83 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 162
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878348173 163 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:smart00020 159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
5-233 |
7.33e-97 |
|
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: 302.27 E-value: 7.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 5 IVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 163
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 164 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:cd00190 159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
629-855 |
2.83e-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: 300.73 E-value: 2.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 706
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 786
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878348173 787 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
628-855 |
2.98e-95 |
|
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: 298.05 E-value: 2.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 628 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLG-TPFLSGAEGQLERVARIYKH 706
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 785
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 786 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:smart00020 160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
306-536 |
6.89e-90 |
|
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: 283.78 E-value: 6.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 464
Cdd:cd00190 81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878348173 465 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 536
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
305-533 |
2.02e-89 |
|
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: 282.64 E-value: 2.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 305 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLgLGGSPVKIGLRRVVLH 383
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 384 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVL 463
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 464 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:smart00020 160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
5-233 |
3.84e-76 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 246.97 E-value: 3.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 5 IVGGMEASPGEFPWQASL-RENKEHFCGAAIINARWLVSAAHCFNefqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 163
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 164 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
629-855 |
1.98e-71 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 234.26 E-value: 1.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPKQWAAFLGTPFLSGAEG--QLERVARIYKH 706
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 786
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 787 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
622-859 |
3.82e-71 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 234.93 E-value: 3.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 622 APAALTRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGdPKQWAAFLGTPFLSGAEGQLER 699
Cdd:COG5640 24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 700 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLS 778
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 779 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 858
Cdd:COG5640 180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257
|
.
gi 1878348173 859 I 859
Cdd:COG5640 258 A 258
|
|
| Trypsin |
pfam00089 |
Trypsin; |
306-533 |
1.45e-70 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 231.95 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRahLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNatKPELLQKASVGIIDQKTCSVLY 464
Cdd:pfam00089 79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 465 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1-241 |
1.03e-63 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 214.90 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 1 MAGRIVGGMEASPGEFPWQASLRENK---EHFCGAAIINARWLVSAAHCFNEFQDPTKWVaYVGATYLSGSEASTVRaqV 77
Cdd:COG5640 27 AAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTVVK--V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 78 VQIVKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQ 157
Cdd:COG5640 104 ARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 158 ALCASlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWILEAT 237
Cdd:COG5640 181 ATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
|
....
gi 1878348173 238 TKAS 241
Cdd:COG5640 259 GGLG 262
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
295-541 |
7.26e-61 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 207.19 E-value: 7.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 295 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGS 371
Cdd:COG5640 20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 372 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKAS 451
Cdd:COG5640 100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 452 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 531
Cdd:COG5640 175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
|
250
....*....|
gi 1878348173 532 WILEIMSSQP 541
Cdd:COG5640 253 WIKSTAGGLG 262
|
|
| Pneumo_att_G |
pfam05539 |
Pneumovirinae attachment membrane glycoprotein G; |
485-635 |
3.02e-03 |
|
Pneumovirinae attachment membrane glycoprotein G;
Pssm-ID: 114270 [Multi-domain] Cd Length: 408 Bit Score: 40.80 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 485 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 562
Cdd:pfam05539 155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 563 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 635
Cdd:pfam05539 223 GTTTSSNPEPQTEPPPSQRgpsgSPQHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRP 301
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
4-233 |
1.98e-98 |
|
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: 306.14 E-value: 1.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 4 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 82
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 83 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 162
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878348173 163 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:smart00020 159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
5-233 |
7.33e-97 |
|
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: 302.27 E-value: 7.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 5 IVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 163
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 164 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:cd00190 159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
629-855 |
2.83e-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: 300.73 E-value: 2.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 706
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 786
Cdd:cd00190 80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878348173 787 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
628-855 |
2.98e-95 |
|
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: 298.05 E-value: 2.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 628 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLG-TPFLSGAEGQLERVARIYKH 706
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 785
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 786 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:smart00020 160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
306-536 |
6.89e-90 |
|
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: 283.78 E-value: 6.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:cd00190 1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 464
Cdd:cd00190 81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878348173 465 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 536
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
305-533 |
2.02e-89 |
|
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: 282.64 E-value: 2.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 305 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLgLGGSPVKIGLRRVVLH 383
Cdd:smart00020 1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 384 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVL 463
Cdd:smart00020 80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 464 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:smart00020 160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
5-233 |
3.84e-76 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 246.97 E-value: 3.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 5 IVGGMEASPGEFPWQASL-RENKEHFCGAAIINARWLVSAAHCFNefqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 163
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 164 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| Trypsin |
pfam00089 |
Trypsin; |
629-855 |
1.98e-71 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 234.26 E-value: 1.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPKQWAAFLGTPFLSGAEG--QLERVARIYKH 706
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 786
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 787 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
622-859 |
3.82e-71 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 234.93 E-value: 3.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 622 APAALTRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGdPKQWAAFLGTPFLSGAEGQLER 699
Cdd:COG5640 24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 700 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLS 778
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 779 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 858
Cdd:COG5640 180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257
|
.
gi 1878348173 859 I 859
Cdd:COG5640 258 A 258
|
|
| Trypsin |
pfam00089 |
Trypsin; |
306-533 |
1.45e-70 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 231.95 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRahLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:pfam00089 1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNatKPELLQKASVGIIDQKTCSVLY 464
Cdd:pfam00089 79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 465 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1-241 |
1.03e-63 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 214.90 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 1 MAGRIVGGMEASPGEFPWQASLRENK---EHFCGAAIINARWLVSAAHCFNEFQDPTKWVaYVGATYLSGSEASTVRaqV 77
Cdd:COG5640 27 AAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTVVK--V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 78 VQIVKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQ 157
Cdd:COG5640 104 ARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 158 ALCASlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWILEAT 237
Cdd:COG5640 181 ATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
|
....
gi 1878348173 238 TKAS 241
Cdd:COG5640 259 GGLG 262
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
295-541 |
7.26e-61 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 207.19 E-value: 7.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 295 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGS 371
Cdd:COG5640 20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 372 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKAS 451
Cdd:COG5640 100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 452 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 531
Cdd:COG5640 175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
|
250
....*....|
gi 1878348173 532 WILEIMSSQP 541
Cdd:COG5640 253 WIKSTAGGLG 262
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
326-511 |
3.31e-06 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 48.52 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 326 GSRHFCGATVVGDRWLLSAAHCFNHTK----VEQVRAHLGtasllGLGGSPVKIGLRRVVLHPLY-NPGILDFDLAVLEL 400
Cdd:COG3591 9 GGGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPG-----YNGGPYGTATATRFRVPPGWvASGDAGYDYALLRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 401 ASPLAFnkyiQPVCLPLAIQ-KFPVGRKCMISGWGntqegnATKPELLQkasvgiiDQKTCSVLYnfsltdrmICAGFLE 479
Cdd:COG3591 84 DEPLGD----TTGWLGLAFNdAPLAGEPVTIIGYP------GDRPKDLS-------LDCSGRVTG--------VQGNRLS 138
|
170 180 190
....*....|....*....|....*....|..
gi 1878348173 480 GKVDSCQGDSGGPLACEEaPGVFYLAGIVSWG 511
Cdd:COG3591 139 YDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
|
|
| DUF1986 |
pfam09342 |
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
17-132 |
4.36e-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: 43.69 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 17 PWQASLRENKEHFCGAAIINARWLVSAAHCFNEFQDPTKWVAYV---GATYLSgseastVRAQVVQIVKHPLYNaDTADF 93
Cdd:pfam09342 2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKS------IEGPYEQIVRVDCRH-DIPES 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1878348173 94 DVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISG 132
Cdd:pfam09342 75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
28-233 |
5.15e-05 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 45.05 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 28 HFCGAAIINARWLVSAAHCFNEFQD---PTKWVAYVGATYLSGSEASTVRAQVvqivkHPLYNADT-ADFDVAVLELTSP 103
Cdd:COG3591 12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVASGdAGYDYALLRLDEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 104 LPfgrhiqpvclpaathifppskkcliSGWGYLKEDFLVKPEVLQKATVelldqalcaslYGHSLTDRMVCAGYLDGKV- 182
Cdd:COG3591 87 LG-------------------------DTTGWLGLAFNDAPLAGEPVTI-----------IGYPGDRPKDLSLDCSGRVt 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878348173 183 -----------DSCQGDSGGPLVCEEpSGRFFLAGIVSWGIGCAEARrpGVY---ARVTRLRDWI 233
Cdd:COG3591 131 gvqgnrlsydcDTTGGSSGSPVLDDS-DGGGRVVGVHSAGGADRANT--GVRltsAIVAALRAWA 192
|
|
| Pneumo_att_G |
pfam05539 |
Pneumovirinae attachment membrane glycoprotein G; |
485-635 |
3.02e-03 |
|
Pneumovirinae attachment membrane glycoprotein G;
Pssm-ID: 114270 [Multi-domain] Cd Length: 408 Bit Score: 40.80 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 485 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 562
Cdd:pfam05539 155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 563 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 635
Cdd:pfam05539 223 GTTTSSNPEPQTEPPPSQRgpsgSPQHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRP 301
|
|
|