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Conserved domains on  [gi|455394|dbj|BAA04753|]
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coagulation factor VII, partial [Macaca mulatta]

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 ...
3-159 6.30e-53

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: 167.45  E-value: 6.30e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394     3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPErmfSERTLAFVRFSLVSGWGQLLDRGATALE 82
Cdd:cd00190  65 EGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDV 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 455394    83 LMALNVPRLMTQDCLQQSQKAeasPNITEYMFCAGYSDGSRDSCKGDSGGPHATRYRGTWYLTGIVSWGQGCAAVGH 159
Cdd:cd00190 142 LQEVNVPIVSNAECKRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNY 215
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
3-159 6.30e-53

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: 167.45  E-value: 6.30e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394     3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPErmfSERTLAFVRFSLVSGWGQLLDRGATALE 82
Cdd:cd00190  65 EGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDV 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 455394    83 LMALNVPRLMTQDCLQQSQKAeasPNITEYMFCAGYSDGSRDSCKGDSGGPHATRYRGTWYLTGIVSWGQGCAAVGH 159
Cdd:cd00190 142 LQEVNVPIVSNAECKRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNY 215
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
3-159 4.08e-47

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: 152.45  E-value: 4.08e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394        3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPErmfSERTLAFVRFSLVSGWGQL-LDRGATAL 81
Cdd:smart00020  65 GEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPD 141
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 455394       82 ELMALNVPRLMTQDCLQQSQKAEAspnITEYMFCAGYSDGSRDSCKGDSGGPHATRyRGTWYLTGIVSWGQGCAAVGH 159
Cdd:smart00020 142 TLQEVNVPIVSNATCRRAYSGGGA---ITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGK 215
Trypsin pfam00089
Trypsin;
3-155 1.94e-29

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 107.14  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394       3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPE--RMFSERTLAFvrfslVSGWGQLLDRGaTA 80
Cdd:pfam00089  63 EGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PS 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 455394      81 LELMALNVPRLMTQDCLQQSqkaeaSPNITEYMFCAGYsdGSRDSCKGDSGGPHATRYRgtwYLTGIVSWGQGCA 155
Cdd:pfam00089 137 DTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCA 201
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-156 2.46e-28

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 105.12  E-value: 2.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394     4 GDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVvltDHVVPLCLPERMFSERTLAFVRfslVSGWGQLL-DRGATALE 82
Cdd:COG5640  96 SGGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGT 169
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 455394    83 LMALNVPRLMTQDCLQQSQkaeaspNITEYMFCAGYSDGSRDSCKGDSGGPHATRYRGTWYLTGIVSWGQG-CAA 156
Cdd:COG5640 170 LRKADVPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA 238
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
3-159 6.30e-53

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: 167.45  E-value: 6.30e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394     3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPErmfSERTLAFVRFSLVSGWGQLLDRGATALE 82
Cdd:cd00190  65 EGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDV 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 455394    83 LMALNVPRLMTQDCLQQSQKAeasPNITEYMFCAGYSDGSRDSCKGDSGGPHATRYRGTWYLTGIVSWGQGCAAVGH 159
Cdd:cd00190 142 LQEVNVPIVSNAECKRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNY 215
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
3-159 4.08e-47

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: 152.45  E-value: 4.08e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394        3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPErmfSERTLAFVRFSLVSGWGQL-LDRGATAL 81
Cdd:smart00020  65 GEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPD 141
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 455394       82 ELMALNVPRLMTQDCLQQSQKAEAspnITEYMFCAGYSDGSRDSCKGDSGGPHATRyRGTWYLTGIVSWGQGCAAVGH 159
Cdd:smart00020 142 TLQEVNVPIVSNATCRRAYSGGGA---ITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGK 215
Trypsin pfam00089
Trypsin;
3-155 1.94e-29

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 107.14  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394       3 EGDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVVLTDHVVPLCLPE--RMFSERTLAFvrfslVSGWGQLLDRGaTA 80
Cdd:pfam00089  63 EGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PS 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 455394      81 LELMALNVPRLMTQDCLQQSqkaeaSPNITEYMFCAGYsdGSRDSCKGDSGGPHATRYRgtwYLTGIVSWGQGCA 155
Cdd:pfam00089 137 DTLQEVTVPVVSRETCRSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCA 201
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-156 2.46e-28

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 105.12  E-value: 2.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394     4 GDEQSRRVAQVIIPSTYVLGATNHDIALLRLQQPVvltDHVVPLCLPERMFSERTLAFVRfslVSGWGQLL-DRGATALE 82
Cdd:COG5640  96 SGGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGT 169
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 455394    83 LMALNVPRLMTQDCLQQSQkaeaspNITEYMFCAGYSDGSRDSCKGDSGGPHATRYRGTWYLTGIVSWGQG-CAA 156
Cdd:COG5640 170 LRKADVPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA 238
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
2-151 2.42e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 36.58  E-value: 2.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 455394     2 HEGDEQSRRVAQVIIPSTYVL-GATNHDIALLRLQQPVVLTDHVVPLCLPERMFSERTLAfvrfslVSGWGQllDRGATA 80
Cdd:COG3591  50 NGGPYGTATATRFRVPPGWVAsGDAGYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVT------IIGYPG--DRPKDL 121
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 455394    81 lelmalnvprlmtqdCLQQSQKAEASPNITEYMFCagysdgsrDSCKGDSGGPHATRYRGTWYLTGIVSWG 151
Cdd:COG3591 122 ---------------SLDCSGRVTGVQGNRLSYDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
 
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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