NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1295944609|ref|NP_034910|]
View 

chymase preproprotein [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
22-243 7.20e-67

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: 206.74  E-value: 7.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  22 IIGGTECIPHSRPYMAYLEIVTSENYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSKEDTWQKLEVEKQF 97
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  98 LHPKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQACKH 177
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1295944609 178 FTSFR---HNSQLCVGNPKKMQNVYKGDSGGPLLC----AGIAQGIASYVHRNAKP--PAVFTRISHYRPWINKI 243
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 ...
22-243 7.20e-67

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: 206.74  E-value: 7.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  22 IIGGTECIPHSRPYMAYLEIVTSENYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSKEDTWQKLEVEKQF 97
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  98 LHPKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQACKH 177
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1295944609 178 FTSFR---HNSQLCVGNPKKMQNVYKGDSGGPLLC----AGIAQGIASYVHRNAKP--PAVFTRISHYRPWINKI 243
Cdd:cd00190   158 AYSYGgtiTDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
21-240 7.40e-61

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: 190.97  E-value: 7.40e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609   21 EIIGGTECIPHSRPYMAYLEIVTSENYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSKEDTwQKLEVEKQ 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF---CGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609   97 FLHPKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTLQEVKMRLQEPQAC 175
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1295944609  176 KHFTSFRH---NSQLCVGNPKKMQNVYKGDSGGPLLC---AGIAQGIASYVHRNAKP--PAVFTRISHYRPWI 240
Cdd:smart00020 157 RRAYSGGGaitDNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
22-240 1.77e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 169.55  E-value: 1.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  22 IIGGTECIPHSRPYMAYLEIVTSEnylSACSGFLIRRNFVLTAAHCA--GRSITVLLGAHNKTSKEDTWQKLEVEKQFLH 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609 100 PKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPaSDTLQEVKMRLQEPQACKHFT 179
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1295944609 180 SFRHN-SQLCVGNPKKMQNvyKGDSGGPLLCA-GIAQGIAS--YVHRNAKPPAVFTRISHYRPWI 240
Cdd:pfam00089 157 GGTVTdTMICAGAGGKDAC--QGDSGGPLVCSdGELIGIVSwgYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
16-247 1.88e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 144.79  E-value: 1.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  16 STKAGEIIGGTECIPHSRPYMAYLEIVTSENYLSaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSkeDTWQKL 91
Cdd:COG5640    25 ADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQF-CGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLST--SGGTVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  92 EVEKQFLHPKYDENLVVHDI--------MLlklkekakltlGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTL 162
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIallklatpVP-----------GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqSGTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609 163 QEVKMRLQEPQACKHFTSFRHNSQLCVGNPKKMQNVYKGDSGGPLL--CAGIAQ--GIASYVHRNAKP--PAVFTRISHY 236
Cdd:COG5640   171 RKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWGGGPCAAgyPGVYTRVSAY 250
                         250
                  ....*....|.
gi 1295944609 237 RPWINKILREN 247
Cdd:COG5640   251 RDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
22-243 7.20e-67

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: 206.74  E-value: 7.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  22 IIGGTECIPHSRPYMAYLEIVTSENYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSKEDTWQKLEVEKQF 97
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  98 LHPKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQACKH 177
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1295944609 178 FTSFR---HNSQLCVGNPKKMQNVYKGDSGGPLLC----AGIAQGIASYVHRNAKP--PAVFTRISHYRPWINKI 243
Cdd:cd00190   158 AYSYGgtiTDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
21-240 7.40e-61

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: 190.97  E-value: 7.40e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609   21 EIIGGTECIPHSRPYMAYLEIVTSENYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSKEDTwQKLEVEKQ 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF---CGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609   97 FLHPKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTLQEVKMRLQEPQAC 175
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1295944609  176 KHFTSFRH---NSQLCVGNPKKMQNVYKGDSGGPLLC---AGIAQGIASYVHRNAKP--PAVFTRISHYRPWI 240
Cdd:smart00020 157 RRAYSGGGaitDNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
22-240 1.77e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 169.55  E-value: 1.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  22 IIGGTECIPHSRPYMAYLEIVTSEnylSACSGFLIRRNFVLTAAHCA--GRSITVLLGAHNKTSKEDTWQKLEVEKQFLH 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609 100 PKYDENLVVHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPaSDTLQEVKMRLQEPQACKHFT 179
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1295944609 180 SFRHN-SQLCVGNPKKMQNvyKGDSGGPLLCA-GIAQGIAS--YVHRNAKPPAVFTRISHYRPWI 240
Cdd:pfam00089 157 GGTVTdTMICAGAGGKDAC--QGDSGGPLVCSdGELIGIVSwgYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
16-247 1.88e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 144.79  E-value: 1.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  16 STKAGEIIGGTECIPHSRPYMAYLEIVTSENYLSaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTSkeDTWQKL 91
Cdd:COG5640    25 ADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQF-CGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLST--SGGTVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609  92 EVEKQFLHPKYDENLVVHDI--------MLlklkekakltlGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTL 162
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIallklatpVP-----------GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqSGTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1295944609 163 QEVKMRLQEPQACKHFTSFRHNSQLCVGNPKKMQNVYKGDSGGPLL--CAGIAQ--GIASYVHRNAKP--PAVFTRISHY 236
Cdd:COG5640   171 RKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWGGGPCAAgyPGVYTRVSAY 250
                         250
                  ....*....|.
gi 1295944609 237 RPWINKILREN 247
Cdd:COG5640   251 RDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
42-105 4.57e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.13  E-value: 4.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1295944609  42 VTSENYLSACSGFLIRRNFVLTAAHC--------AGRSITVLLGAHNktskeDTWQKLEVEKQFLHPKYDEN 105
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVAS 71
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH