ID   G0MH27_CAEBE            Unreviewed;       431 AA.
AC   G0MH27;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN   ORFNames=CAEBREN_22017 {ECO:0000313|EMBL:EGT57888.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00010515}.
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DR   EMBL; GL379794; EGT57888.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0MH27; -.
DR   STRING; 135651.G0MH27; -.
DR   ESTHER; caebe-g0mh27; Arylacetamide_deacetylase.
DR   EnsemblMetazoa; CBN22017.1; CBN22017.1; WBGene00160742.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_012494_12_3_1; -.
DR   InParanoid; G0MH27; -.
DR   OMA; PSHMFSK; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR017157; Arylacetamide_deacetylase.
DR   PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1.
DR   PANTHER; PTHR23024:SF24; NEUTRAL CHOLESTEROL ESTER HYDROLASE HOMOLOG-RELATED; 1.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..282
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   DOMAIN          338..402
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   ACT_SITE        369
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
SQ   SEQUENCE   431 AA;  48389 MW;  BE5469CDD10B67D3 CRC64;
     MTLKEGKESF CIKYLVLGIS TIALLTIGYS LYKPLPDGFT VSRWDRAVMH VVEPALRVAY
     YYPSHMFSKA SSMVQWTRSA LNFLSKSLGL GVNTHGEIDI KWHNWNGTPV KVYLPLNNKT
     STDGAVVFIH GGGFALGNVD MYDSLVRRMA YETKTLFISI EYRLSPETAF PGGLLDCEAA
     IEHLFEFGKV QFGINTSKIV IMGDSAGGNL ATVVAQRRAA RNALPKLAGQ VLIYPLLQMA
     DLQTVSYRYF HSRLDGYALV DPESVAYYYM FYAGINMDEK SYLVPSVMSN GHVAADLHSE
     IDEIMSYEKV IESTRTYKNS TIPNRWAVRP SLEAQHLMQP FLTNPDFSPL MRKDVSNLPA
     TMIVTCEFDV LRDEGMIYAH RLETSGVPTT AINYQNGFHA MLNFHSELYE ASKAVIDIEN
     WTLKTINSIQ P
//