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Conserved domains on  [gi|815890846|ref|NP_001295012|]
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chymase isoform 2 [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.-
Gene Ontology:  GO:0008236|GO:0008233|GO:0006508|GO:0004252
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 ...
 1-132 6.61e-50

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: 158.98  E-value: 6.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846   1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACS---HFRDFDHNLQLC 77
Cdd:cd00190   92 ALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKraySYGGTITDNMLC 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890846  78 VGNPRKTKSAFKGDSGGPLLC----AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQI 132
Cdd:cd00190  172 AGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-132 6.61e-50

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: 158.98  E-value: 6.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846   1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACS---HFRDFDHNLQLC 77
Cdd:cd00190   92 ALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKraySYGGTITDNMLC 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890846  78 VGNPRKTKSAFKGDSGGPLLC----AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQI 132
Cdd:cd00190  172 AGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-129 7.86e-44

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: 143.20  E-value: 7.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846     1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRT-GVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNL---QL 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAItdnML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 815890846    77 CVGNPRKTKSAFKGDSGGPLLC---AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWI 129
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-129 4.68e-34

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 117.93  E-value: 4.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846    1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPgSDTLQEVKLRLMDPQACShfRDFDHNL---QLC 77
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR--SAYGGTVtdtMIC 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 815890846   78 VGNprKTKSAFKGDSGGPLLCAGV-AQGIVSYGRSDAKP--PAVFTRISHYRPWI 129
Cdd:pfam00089 167 AGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2-136 9.56e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 107.81  E-value: 9.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846   2 LLKLKEKASltlAVGTLPFPSQFNFVPPGRMCRVAGWGRTGV-LKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGN 80
Cdd:COG5640  123 LLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGY 199

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815890846  81 PRKTKSAFKGDSGGPLL----CAGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQILQAN 136
Cdd:COG5640  200 PEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-132 6.61e-50

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: 158.98  E-value: 6.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846   1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACS---HFRDFDHNLQLC 77
Cdd:cd00190   92 ALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKraySYGGTITDNMLC 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815890846  78 VGNPRKTKSAFKGDSGGPLLC----AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQI 132
Cdd:cd00190  172 AGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-129 7.86e-44

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: 143.20  E-value: 7.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846     1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRT-GVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNL---QL 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAItdnML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 815890846    77 CVGNPRKTKSAFKGDSGGPLLC---AGVAQGIVSYGRSDAKP--PAVFTRISHYRPWI 129
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-129 4.68e-34

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 117.93  E-value: 4.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846    1 MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPgSDTLQEVKLRLMDPQACShfRDFDHNL---QLC 77
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR--SAYGGTVtdtMIC 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 815890846   78 VGNprKTKSAFKGDSGGPLLCAGV-AQGIVSYGRSDAKP--PAVFTRISHYRPWI 129
Cdd:pfam00089 167 AGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2-136 9.56e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 107.81  E-value: 9.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890846   2 LLKLKEKASltlAVGTLPFPSQFNFVPPGRMCRVAGWGRTGV-LKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGN 80
Cdd:COG5640  123 LLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGY 199

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815890846  81 PRKTKSAFKGDSGGPLL----CAGVAQGIVSYGRSDAKP--PAVFTRISHYRPWINQILQAN 136
Cdd:COG5640  200 PEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKSTAGGL 261
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 90-136 1.25e-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: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 815890846  90 GDSGGPLLCAGVAQGIVSYGRSDAKPPAvftRISHYRPwINQILQAN 136
Cdd:cd21112  145 GDSGGPVFSGTQALGITSGGSGNCGSGG---GTSYFQP-VNPVLSAY 187
 
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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