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Conserved domains on  [gi|126131329|gb|ABN79862|]
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coagulation factor VII, partial [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

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 ...
20-256 9.05e-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: 273.38  E-value: 9.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  20 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 98
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  99 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 178
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131329 179 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 256
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 ...
20-256 9.05e-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: 273.38  E-value: 9.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  20 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 98
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  99 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 178
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131329 179 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 256
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
19-253 2.29e-86

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: 257.22  E-value: 2.29e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329    19 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 97
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329    98 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 176
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131329   177 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 253
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
20-254 1.25e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.81  E-value: 1.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329   20 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329   99 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 176
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131329  177 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 254
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-262 2.81e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.09  E-value: 2.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  13 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 89
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  90 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 168
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329 169 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 247
Cdd:COG5640  175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247
                        250
                 ....*....|....*
gi 126131329 248 SQYIEWLQKLMRSEP 262
Cdd:COG5640  248 SAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
20-256 9.05e-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: 273.38  E-value: 9.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  20 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 98
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  99 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 178
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131329 179 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 256
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
19-253 2.29e-86

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: 257.22  E-value: 2.29e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329    19 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 97
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329    98 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 176
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131329   177 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 253
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
20-254 1.25e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.81  E-value: 1.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329   20 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329   99 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 176
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131329  177 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 254
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-262 2.81e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.09  E-value: 2.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  13 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 89
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  90 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 168
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329 169 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 247
Cdd:COG5640  175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247
                        250
                 ....*....|....*
gi 126131329 248 SQYIEWLQKLMRSEP 262
Cdd:COG5640  248 SAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
36-232 1.67e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.22  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329  36 LLLVNGAQLCGGTLINTIWVVSAAHCF---DKIKNWRNLIAVLGehdlsEHDGDEQSRRVAQVIIPSTYVP-GTTNHDIA 111
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG-----YNGGPYGTATATRFRVPPGWVAsGDAGYDYA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329 112 LLRLHQPVVLTDHVVPLCLPERTFSERTLAfvrfslVSGWGQllDRGATAlelmvlnvprlmtqdCLQQSRKVGDSPNIT 191
Cdd:COG3591   80 LLRLDEPLGDTTGWLGLAFNDAPLAGEPVT------IIGYPG--DRPKDL---------------SLDCSGRVTGVQGNR 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126131329 192 EYMFCagysdgskDSCKGDSGGPHATHYRGTWYLTGIVSWG 232
Cdd:COG3591  137 LSYDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
31-132 2.39e-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: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131329   31 CPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVL---GEHDLSEHDGDEQSRRVAQViipsTYVPGTtn 107
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKSIEGPYEQIVRVDCR----HDIPES-- 74
                          90       100
                  ....*....|....*....|....*
gi 126131329  108 hDIALLRLHQPVVLTDHVVPLCLPE 132
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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