ID   A0A261B5I1_9PELO        Unreviewed;       431 AA.
AC   A0A261B5I1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
DE   Flags: Fragment;
GN   ORFNames=FL83_17336 {ECO:0000313|EMBL:OZG05000.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG05000.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG05000.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG05000.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00010515}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZG05000.1}.
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DR   EMBL; NIPN01000175; OZG05000.1; -; Genomic_DNA.
DR   STRING; 1503980.A0A261B5I1; -.
DR   Proteomes; UP000216463; 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:UP000216463};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..281
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   DOMAIN          343..404
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG05000.1"
SQ   SEQUENCE   431 AA;  48783 MW;  3CFBC75265920806 CRC64;
     MRLKAEKKPI HVRNIVISIV ILSVFLLLTG YSLHKPLPDG FTVTQWDRTV MHVVEPALRV
     AYYYPSQMFS KASNMVYWTR GILNILSKTL GLRVYTQGQI DIEWQNWNGT PVKIYRPINN
     QTSADGAVIF IHGGGFALGN VEMYDSLVER MAFEMNTLFI SIEYRLSPET AFPGGILDCE
     AAIDHFFRVG GTQFGVNTSK VVIMGDSAGG NLATVVAQRR AARKALPALA GQVLIYPLLQ
     MADMQTVSYR YFXTRLNGYA LVDPESVAYY YMFYAGINMD EKAYLIPSVV SNGHVAKHLH
     KDVEEIMSYR TVIETTRNYN NHSISGRWHI ERNYEAQDLM KPFLTNPDFS PLMRKDLSNL
     PPTMVITCEF DVLRDEGLIY AKRLEASGVP TTSIHYENGF HAMLNFHSEL HEASKSVGDI
     EQWTLNIINN V
//