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Conserved domains on  [gi|1831521059|ref|NP_001367204|]
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Carboxylic ester hydrolase [Caenorhabditis elegans]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
1-169 2.86e-07

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00135:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 513  Bit Score: 51.15  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831521059   1 MLCGVTDNEFTIF--KYPDGYYISATFL-DFENPVDTVNVYRNKFTN-----------------------ITPTFVNSDS 54
Cdd:pfam00135 308 LLIGVTKDEGLLFaaYILDNVDILKALEeKLLRSLLIDLLYLLLVDLpeeisaalreeyldwgdrddpetSRRALVELLT 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831521059  55 SAVF-VSAATYSEALTNAGGNVYLFE------SRQKPFSM---HVTDMQYFIGIHREKNHTT---DMDILDSFySKLLVN 121
Cdd:pfam00135 388 DYLFnCPVIRFADLHASRGTPVYMYSfdyrgsSLRYPKWVgvdHGDELPYVFGTPFVGALLFteeDEKLSRKM-MTYWTN 466
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831521059 122 FTKFGSP-----SPNWEKYDPSKMNFmaMEIDTeqgiEPKMENGFHEELVNFW 169
Cdd:pfam00135 467 FAKTGNPngpegLPKWPPYTDENGQY--LSIDL----EPRVKQGLKAERCAFW 513
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
1-169 2.86e-07

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 51.15  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831521059   1 MLCGVTDNEFTIF--KYPDGYYISATFL-DFENPVDTVNVYRNKFTN-----------------------ITPTFVNSDS 54
Cdd:pfam00135 308 LLIGVTKDEGLLFaaYILDNVDILKALEeKLLRSLLIDLLYLLLVDLpeeisaalreeyldwgdrddpetSRRALVELLT 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831521059  55 SAVF-VSAATYSEALTNAGGNVYLFE------SRQKPFSM---HVTDMQYFIGIHREKNHTT---DMDILDSFySKLLVN 121
Cdd:pfam00135 388 DYLFnCPVIRFADLHASRGTPVYMYSfdyrgsSLRYPKWVgvdHGDELPYVFGTPFVGALLFteeDEKLSRKM-MTYWTN 466
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831521059 122 FTKFGSP-----SPNWEKYDPSKMNFmaMEIDTeqgiEPKMENGFHEELVNFW 169
Cdd:pfam00135 467 FAKTGNPngpegLPKWPPYTDENGQY--LSIDL----EPRVKQGLKAERCAFW 513
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
1-169 2.86e-07

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 51.15  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831521059   1 MLCGVTDNEFTIF--KYPDGYYISATFL-DFENPVDTVNVYRNKFTN-----------------------ITPTFVNSDS 54
Cdd:pfam00135 308 LLIGVTKDEGLLFaaYILDNVDILKALEeKLLRSLLIDLLYLLLVDLpeeisaalreeyldwgdrddpetSRRALVELLT 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831521059  55 SAVF-VSAATYSEALTNAGGNVYLFE------SRQKPFSM---HVTDMQYFIGIHREKNHTT---DMDILDSFySKLLVN 121
Cdd:pfam00135 388 DYLFnCPVIRFADLHASRGTPVYMYSfdyrgsSLRYPKWVgvdHGDELPYVFGTPFVGALLFteeDEKLSRKM-MTYWTN 466
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831521059 122 FTKFGSP-----SPNWEKYDPSKMNFmaMEIDTeqgiEPKMENGFHEELVNFW 169
Cdd:pfam00135 467 FAKTGNPngpegLPKWPPYTDENGQY--LSIDL----EPRVKQGLKAERCAFW 513
 
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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