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Conserved domains on  [gi|469474601]
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Chain H, Factor VII heavy chain

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-237 9.23e-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: 272.61  E-value: 9.23e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   1 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 79
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 159
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469474601 160 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 237
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-237 9.23e-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: 272.61  E-value: 9.23e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   1 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 79
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 159
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469474601 160 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 237
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-234 3.03e-85

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: 253.37  E-value: 3.03e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601     1 IVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVIIP 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601    80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQDC 158
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 469474601   159 lqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 234
Cdd:smart00020 157 ---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
1-235 1.36e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.03  E-value: 1.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601    1 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 157
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469474601  158 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 235
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-243 4.11e-57

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.93  E-value: 4.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   1 IVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQSRRVAQVI 77
Cdd:COG5640   31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TVVKVARIV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  78 IPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLNVPRLMTQ 156
Cdd:COG5640  108 VHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601 157 DCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRVSQYIEWL 235
Cdd:COG5640  182 TCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRVSAYRDWI 254

                 ....*...
gi 469474601 236 QKLMRSEP 243
Cdd:COG5640  255 KSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-237 9.23e-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: 272.61  E-value: 9.23e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   1 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 79
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 159
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469474601 160 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 237
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-234 3.03e-85

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: 253.37  E-value: 3.03e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601     1 IVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVIIP 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601    80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQDC 158
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 469474601   159 lqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 234
Cdd:smart00020 157 ---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
1-235 1.36e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.03  E-value: 1.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601    1 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   80 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 157
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 469474601  158 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 235
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-243 4.11e-57

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.93  E-value: 4.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   1 IVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQSRRVAQVI 77
Cdd:COG5640   31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TVVKVARIV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  78 IPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLNVPRLMTQ 156
Cdd:COG5640  108 VHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601 157 DCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRVSQYIEWL 235
Cdd:COG5640  182 TCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRVSAYRDWI 254

                 ....*...
gi 469474601 236 QKLMRSEP 243
Cdd:COG5640  255 KSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
17-213 3.13e-09

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.07  E-value: 3.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  17 LLLVNGAQLCGGTLINTIWVVSAAHCF---DKIKNWRNLIAVLGehdlsEHDGDEQSRRVAQVIIPSTYVP-GTTNHDIA 92
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG-----YNGGPYGTATATRFRVPPGWVAsGDAGYDYA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601  93 LLRLHQPVVLTDHVVPLCLPERTFSERTLAfvrfslVSGWGQllDRGATAlelmvlnvprlmtqdCLQQSRKVGDSPNIT 172
Cdd:COG3591   80 LLRLDEPLGDTTGWLGLAFNDAPLAGEPVT------IIGYPG--DRPKDL---------------SLDCSGRVTGVQGNR 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 469474601 173 EYMFCagysdgskDSCKGDSGGPHATHYRGTWYLTGIVSWG 213
Cdd:COG3591  137 LSYDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
12-113 2.77e-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: 42.53  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469474601   12 CPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVL---GEHDLSEHDGDEQSRRVAQViipsTYVPGTtn 88
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKSIEGPYEQIVRVDCR----HDIPES-- 74
                          90       100
                  ....*....|....*....|....*
gi 469474601   89 hDIALLRLHQPVVLTDHVVPLCLPE 113
Cdd:pfam09342  75 -EISLLHLASPASFSNHVLPTFVPE 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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