NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157831615]
View 

Chain A, CHYMASE

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 ...
1-222 7.52e-94

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: 274.15  E-value: 7.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   1 IIGGTESKPHSRPYMAYLEIvtsNGPSKFCGGFLIRRNFVLTAAHC----AGRSITVTLGAHNITEEEDTWQKLEVIKQF 76
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615  77 RHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACS- 155
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157831615 156 --HFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLC----AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQI 222
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 ...
1-222 7.52e-94

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: 274.15  E-value: 7.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   1 IIGGTESKPHSRPYMAYLEIvtsNGPSKFCGGFLIRRNFVLTAAHC----AGRSITVTLGAHNITEEEDTWQKLEVIKQF 76
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615  77 RHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACS- 155
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157831615 156 --HFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLC----AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQI 222
Cdd:cd00190  158 aySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-219 1.04e-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 [Multi-domain]  Cd Length: 229  Bit Score: 253.37  E-value: 1.04e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615     1 IIGGTESKPHSRPYMAYLeivTSNGPSKFCGGFLIRRNFVLTAAHC----AGRSITVTLGAHNITEEEDTwQKLEVIKQF 76
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEG-QVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615    77 RHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRT-GVLKPGSDTLQEVKLRLMDPQACS 155
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157831615   156 HFRDFDHNL---QLCVGNPRKTKSAFKGDSGGPLLC---AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWI 219
Cdd:smart00020 158 RAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-219 1.54e-71

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 217.31  E-value: 1.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615    1 IIGGTESKPHSRPYMAYLEIvtsNGPSKFCGGFLIRRNFVLTAAHCA--GRSITVTLGAHNITEEEDTWQKLEVIKQFRH 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   79 PKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPgSDTLQEVKLRLMDPQACShfR 158
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR--S 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157831615  159 DFDHNL---QLCVGNprKTKSAFKGDSGGPLLCAGV-AQGIVSYGRSDAKP--PAVFTRISHYRPWI 219
Cdd:pfam00089 155 AYGGTVtdtMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-219 2.96e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 96.48  E-value: 2.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   1 IIGGTESKPHSRPYMAYLeiVTSNGPS---KFCGGFLIRRNFVLTAAHCA-GRSI---TVTLGAHNITeEEDTWQKLEVI 73
Cdd:COG5640   33 IIGGSNANAGEYPSLVAL--VDRISDYvsgTFCGGSKLGGRYVLTAAHCAdASSPissDVNRVVVDLN-DSSQAERGHVR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615  74 KQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTL--PFPSQFNFVPPGRMCRVAGWGRTGV-----LKPGSDTLQEVKL 146
Cdd:COG5640  110 TIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSfdASDTFLNSVTTVSPMTNGTFGVTTPsdvprSSPKGTILHEVAV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615 147 RLMDPQACS------HFRDFDHNL-QLCVGNPRktKSAFKGDSGGPLLCAG----VAQGIVSYGRSD-AKP--PAVFTRI 212
Cdd:COG5640  190 LFVPLSTCAqykgcaNASDGATGLtGFCAGRPP--KDACQGDSGGPIFHKGeegrVQRGVVSWGDGGcGGTliPGVYTNV 267

                 ....*..
gi 157831615 213 SHYRPWI 219
Cdd:COG5640  268 SNYQDWI 274
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-222 7.52e-94

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: 274.15  E-value: 7.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   1 IIGGTESKPHSRPYMAYLEIvtsNGPSKFCGGFLIRRNFVLTAAHC----AGRSITVTLGAHNITEEEDTWQKLEVIKQF 76
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615  77 RHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACS- 155
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157831615 156 --HFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLC----AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQI 222
Cdd:cd00190  158 aySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-219 1.04e-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 [Multi-domain]  Cd Length: 229  Bit Score: 253.37  E-value: 1.04e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615     1 IIGGTESKPHSRPYMAYLeivTSNGPSKFCGGFLIRRNFVLTAAHC----AGRSITVTLGAHNITEEEDTwQKLEVIKQF 76
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEG-QVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615    77 RHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRT-GVLKPGSDTLQEVKLRLMDPQACS 155
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157831615   156 HFRDFDHNL---QLCVGNPRKTKSAFKGDSGGPLLC---AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWI 219
Cdd:smart00020 158 RAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-219 1.54e-71

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 217.31  E-value: 1.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615    1 IIGGTESKPHSRPYMAYLEIvtsNGPSKFCGGFLIRRNFVLTAAHCA--GRSITVTLGAHNITEEEDTWQKLEVIKQFRH 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   79 PKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPgSDTLQEVKLRLMDPQACShfR 158
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR--S 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157831615  159 DFDHNL---QLCVGNprKTKSAFKGDSGGPLLCAGV-AQGIVSYGRSDAKP--PAVFTRISHYRPWI 219
Cdd:pfam00089 155 AYGGTVtdtMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-219 2.96e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 96.48  E-value: 2.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615   1 IIGGTESKPHSRPYMAYLeiVTSNGPS---KFCGGFLIRRNFVLTAAHCA-GRSI---TVTLGAHNITeEEDTWQKLEVI 73
Cdd:COG5640   33 IIGGSNANAGEYPSLVAL--VDRISDYvsgTFCGGSKLGGRYVLTAAHCAdASSPissDVNRVVVDLN-DSSQAERGHVR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615  74 KQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTL--PFPSQFNFVPPGRMCRVAGWGRTGV-----LKPGSDTLQEVKL 146
Cdd:COG5640  110 TIYVHEFYSPGNLGNDIAVLELARAASLPRVKITSfdASDTFLNSVTTVSPMTNGTFGVTTPsdvprSSPKGTILHEVAV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831615 147 RLMDPQACS------HFRDFDHNL-QLCVGNPRktKSAFKGDSGGPLLCAG----VAQGIVSYGRSD-AKP--PAVFTRI 212
Cdd:COG5640  190 LFVPLSTCAqykgcaNASDGATGLtGFCAGRPP--KDACQGDSGGPIFHKGeegrVQRGVVSWGDGGcGGTliPGVYTNV 267

                 ....*..
gi 157831615 213 SHYRPWI 219
Cdd:COG5640  268 SNYQDWI 274
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
180-226 4.12e-03

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 36.90  E-value: 4.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157831615 180 GDSGGPLLCAGVAQGIVSYGRSDAKPPAvftRISHYRPwINQILQAN 226
Cdd:cd21112  145 GDSGGPVFSGTQALGITSGGSGNCGSGG---GTSYFQP-VNPVLSAY 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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