29152 |
cd00190 |
Tryp_SPc |
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. |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor... |
true |
false |
true |
232 |
1e-67 |
251.01 |
100.00 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 78
cd00190 1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 79 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 158
cd00190 78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MCV_A 159 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 236
cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
|
|
cl00149 |
119569 |
Tryp_SPc |
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. |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor... |
0 |
47370 |
smart00020 |
Tryp_SPc |
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. |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor... |
false |
false |
false |
231 |
2e-62 |
233.69 |
99.57 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVD--RELTFRVVVGEHNLNQNDGTeQYVGVQKIV 78
smart00020 2 IVGGSEANIGSFPWQVSLQYRGGR---HFCGGSLISPRWVLTAAHCVYgsAPSSIRVRLGSHDLSSGEET-QTVKVSKVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 79 VHPYWNTDdvAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYAI 157
smart00020 78 VHPNYNPS--TYDNDIALLKLSEPVTLSDTVRPICLPSSGYNVPAGTTCTVSGWGRTSeSSGSLPDTLQEVNVPIVSNAT 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MCV_A 158 CSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRlGCNVTRKPTVFTRVSAYISWI 233
smart00020 156 CRRAYSGGPAITDNMLCAGGlEGGKDACQGDSGGPLVCNDPGRWVLVGIVSWGSY-GCARPNKPGVYTRVSSYLDWI 231
|
|
cl00149 |
119569 |
Tryp_SPc |
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. |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor... |
-1 |
109157 |
pfam00089 |
Trypsin |
Trypsin |
Trypsin |
false |
false |
false |
216 |
1e-60 |
228.09 |
100.00 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 1 VVGGTEAQRNSWPSQISLQYRSGsswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 80
pfam00089 1 IVGGDEAQPGSFPWQVSLQVSSG----HFCGGSLISENWVLTAAHCVSNASSVRVVLGAHNIVLREGGEQKFDVKKIIVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 81 PYWNTDDvaagYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICss 160
pfam00089 77 PNYNPDT----NDIALLKLKSPVTLGDTVRPICLPTASSDLPVGTTCTVSGWGNTKTLG-TPDTLQEVTVPVVSRETC-- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MCV_A 161 SSYWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHCLVNgqyAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 233
pfam00089 150 RSAYGGTVTDNMICAGAGG-KDACQGDSGGPLVCSDG---ELVGIVSWGY--GCASGNYPGVYTPVSSYLDWI 216
|
|
cl00149 |
119569 |
Tryp_SPc |
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. |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor... |
-1 |
33391 |
COG3591 |
COG3591 |
V8-like Glu-specific endopeptidase [Amino acid transport and metabolism] |
V8-like Glu-specific endopeptidase [Amino acid transport and metabolism] |
false |
false |
false |
251 |
0.004 |
36.82 |
49.80 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 10 NSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPY---WNTD 86
COG3591 47 TQFPYSAVVQFEAATG-RLCTAATLIGPNTVLTAGHCIYSPDYGEDDIAAAPPGVNSDGGPFYGITKIEIRVYpgeLYKE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
1MCV_A 87 DvAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWG 133
COG3591 126 D-GASYDVGEAALESGINIGDVVNYLKRNTASEAKANDRITVIGYPG 171
|
|
cl00149 |
119569 |
Tryp_SPc |
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. |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor... |
-1 |
35199 |
COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones] |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover,.. |
false |
true |
false |
413 |
3e-18 |
87.00 |
58.60 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 1 VVGGTEAQRNSWPSQISLQYRSGSSWAHT-CGGTLIRQNWVMTAAHCVDRE-----LTFRVVVGEHNLNQNDGteqyVGV 74
COG5640 33 IIGGSNANAGEYPSLVALVDRISDYVSGTfCGGSKLGGRYVLTAAHCADASspissDVNRVVVDLNDSSQAER----GHV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 75 QKIVVHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAG--TILANNSPCYITGWGLTRT-----NGQLAQTLQQ 147
COG5640 109 RTIYVHEFYSPGNL--GNDIAVLELARAASLPRVKITSFDASDTflNSVTTVSPMTNGTFGVTTPsdvprSSPKGTILHE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MCV_A 148 AYLPTVDYAICSSSSYWG----STVKNSMVCAGGDGvRSGCQGDSGGPLHCLVNGQYAVHGVTSFvSRLGCNVTRKPTVF 223
COG5640 187 VAVLFVPLSTCAQYKGCAnasdGATGLTGFCAGRPP-KDACQGDSGGPIFHKGEEGRVQRGVVSW-GDGGCGGTLIPGVY 264
|
250
....*....|
1MCV_A 224 TRVSAYISWI 233
COG5640 265 TNVSNYQDWI 274
|
|
|
|
|
|
|
-1 |