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Conserved domains on  [gi|160298223|ref|NP_034501|]
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granzyme C preproprotein [Mus musculus]

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

 Zoom to residue level

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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 ...
21-244 2.58e-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: 266.06  E-value: 2.58e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  21 IIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCKGSS----MTVTLGAHNIKAKEETQQIIPVAKAI 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQV---SLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  97 PHPDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPDGEFPKTLHEVKLTVQKDQVCES 176
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160298223 177 QFQSSYNR-ANEICVGDSKIKGASFEEDSGGPLVCKRA----AAGIVSYGQTDGSA--PQVFTRVLSFVSWIKKT 244
Cdd:cd00190  158 AYSYGGTItDNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-244 2.58e-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: 266.06  E-value: 2.58e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  21 IIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCKGSS----MTVTLGAHNIKAKEETQQIIPVAKAI 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQV---SLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  97 PHPDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPDGEFPKTLHEVKLTVQKDQVCES 176
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160298223 177 QFQSSYNR-ANEICVGDSKIKGASFEEDSGGPLVCKRA----AAGIVSYGQTDGSA--PQVFTRVLSFVSWIKKT 244
Cdd:cd00190  158 AYSYGGTItDNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-241 3.24e-84

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: 250.67  E-value: 3.24e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223    20 EIIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCKG----SSMTVTLGAHNIKAKEEtQQIIPVAKA 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQV---SLQYGGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223    96 IPHPDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPD-GEFPKTLHEVKLTVQKDQVC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160298223   175 ESQF-QSSYNRANEICVGDSKIKGASFEEDSGGPLVCKRA---AAGIVSYGQ--TDGSAPQVFTRVLSFVSWI 241
Cdd:smart00020 157 RRAYsGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSgcARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-241 6.04e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.53  E-value: 6.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223   21 IIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCK--GSSMTVTLGAHNIKAKEETQQIIPVAKAIPH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQV---SLQLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223   99 PDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPDGeFPKTLHEVKLTVQKDQVCESQF 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160298223  179 QSSYNRaNEICVGDSKIkgASFEEDSGGPLVC-KRAAAGIVSYGQ--TDGSAPQVFTRVLSFVSWI 241
Cdd:pfam00089 157 GGTVTD-TMICAGAGGK--DACQGDSGGPLVCsDGELIGIVSWGYgcASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-245 6.86e-52

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 169.44  E-value: 6.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  18 AEEIIGGNEISPHSRPYMAYyEFLKVGGKKMFCGGFLVRDKFVLTAAHC----KGSSMTVTLGAHNIKAkeETQQIIPVA 93
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVA-LQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLST--SGGTVVKVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  94 KAIPHPDYNPDDRSNDIMLLKLVRNAKrtrAVRPLNLPRRNAHVKPGDECYVAGWGKVTPD-GEFPKTLHEVKLTVQKDQ 172
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160298223 173 VCesQFQSSYNRANEICVGDSKIKGASFEEDSGGPLVCKRAA----AGIVSYGQTD--GSAPQVFTRVLSFVSWIKKTM 245
Cdd:COG5640  182 TC--AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGgwvlVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-244 2.58e-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: 266.06  E-value: 2.58e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  21 IIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCKGSS----MTVTLGAHNIKAKEETQQIIPVAKAI 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQV---SLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  97 PHPDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPDGEFPKTLHEVKLTVQKDQVCES 176
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160298223 177 QFQSSYNR-ANEICVGDSKIKGASFEEDSGGPLVCKRA----AAGIVSYGQTDGSA--PQVFTRVLSFVSWIKKT 244
Cdd:cd00190  158 AYSYGGTItDNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-241 3.24e-84

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: 250.67  E-value: 3.24e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223    20 EIIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCKG----SSMTVTLGAHNIKAKEEtQQIIPVAKA 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQV---SLQYGGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223    96 IPHPDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPD-GEFPKTLHEVKLTVQKDQVC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160298223   175 ESQF-QSSYNRANEICVGDSKIKGASFEEDSGGPLVCKRA---AAGIVSYGQ--TDGSAPQVFTRVLSFVSWI 241
Cdd:smart00020 157 RRAYsGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSgcARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-241 6.04e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.53  E-value: 6.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223   21 IIGGNEISPHSRPYMAyyeFLKVGGKKMFCGGFLVRDKFVLTAAHCK--GSSMTVTLGAHNIKAKEETQQIIPVAKAIPH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQV---SLQLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223   99 PDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPDGeFPKTLHEVKLTVQKDQVCESQF 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160298223  179 QSSYNRaNEICVGDSKIkgASFEEDSGGPLVC-KRAAAGIVSYGQ--TDGSAPQVFTRVLSFVSWI 241
Cdd:pfam00089 157 GGTVTD-TMICAGAGGK--DACQGDSGGPLVCsDGELIGIVSWGYgcASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-245 6.86e-52

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 169.44  E-value: 6.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  18 AEEIIGGNEISPHSRPYMAYyEFLKVGGKKMFCGGFLVRDKFVLTAAHC----KGSSMTVTLGAHNIKAkeETQQIIPVA 93
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVA-LQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLST--SGGTVVKVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  94 KAIPHPDYNPDDRSNDIMLLKLVRNAKrtrAVRPLNLPRRNAHVKPGDECYVAGWGKVTPD-GEFPKTLHEVKLTVQKDQ 172
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160298223 173 VCesQFQSSYNRANEICVGDSKIKGASFEEDSGGPLVCKRAA----AGIVSYGQTD--GSAPQVFTRVLSFVSWIKKTM 245
Cdd:COG5640  182 TC--AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGgwvlVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-149 6.91e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 42.36  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223  41 LKVGGKKMFCGGFLVRDKFVLTAAHC--------KGSSMTVTLGAHNikakeETQQIIPVAKAIPHPDYNPD-DRSNDIM 111
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASgDAGYDYA 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 160298223 112 LLKLvrNAKRTRAVRPLNLpRRNAHVKPGDECYVAGWG 149
Cdd:COG3591   80 LLRL--DEPLGDTTGWLGL-AFNDAPLAGEPVTIIGYP 114
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
52-209 8.85e-04

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 38.56  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298223   52 GFLVR-DKFVLTAAHCKGSSMTVTLGAHNIKAKEETQQIIPVAKAiphpdynpdDRSNDIMLLKLvrnAKRTRAVRPLNL 130
Cdd:pfam13365   3 GFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR---------DPDLDLALLRV---SGDGRGLPPLPL 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160298223  131 PRRNAhVKPGDECYVAGWgkvtPDGefpktlhEVKLTVQKDQVCESQFQSSYNRANEICVGDSKIKGASfeedSGGPLV 209
Cdd:pfam13365  71 GDSEP-LVGGERVYAVGY----PLG-------GEKLSLSEGIVSGVDEGRDGGDDGRVIQTDAALSPGS----SGGPVF 133
 
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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