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Database: UniProt
Entry: G1X621_ARTOA
LinkDB: G1X621_ARTOA
Original site: G1X621_ARTOA 
ID   G1X621_ARTOA            Unreviewed;       451 AA.
AC   G1X621;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF12697};
GN   ORFNames=AOL_s00054g315 {ECO:0000313|EMBL:EGX51616.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51616.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX51616.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX51616.1}.
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DR   EMBL; ADOT01000084; EGX51616.1; -; Genomic_DNA.
DR   RefSeq; XP_011119933.1; XM_011121631.1.
DR   AlphaFoldDB; G1X621; -.
DR   STRING; 756982.G1X621; -.
DR   GeneID; 22890844; -.
DR   eggNOG; KOG4178; Eukaryota.
DR   HOGENOM; CLU_046024_0_0_1; -.
DR   InParanoid; G1X621; -.
DR   OMA; RTIIVAH; -.
DR   OrthoDB; 2443908at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR   PANTHER; PTHR43329:SF125; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05590)-RELATED; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          91..252
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
SQ   SEQUENCE   451 AA;  49912 MW;  45AFB05022347F0B CRC64;
     MGLVSFVKTA VITVTGLFSL NLFVLGVAST GAFFIPVGKK KKQARLQAQS ELWDLSTQPL
     PGFHHKFFEA PDGVNLHYVE GGDTSPGSPL IIFLHGFPDS WFVWHHQLSA PAIQQKAHLI
     AVDLPGHGGS DGFPRASATA ILTSVANFII AQKEKKTSET CILVSHDWGS IVCCRLAPEI
     GFLFTRCIIL NGLHPPLAIA NMNRATSSAS RMLRTYVRNP TNFALIRSAF QSLKPFLNQM
     KASYYASVFL LPLPLARTLY TMGDFWFLRL LCKLSKSPNE EIFLASAFGP SKSEAEGYPA
     AILARQNANK RASDRIAYYR DNLSVGTWRK PENIQLLIAE SQTNSGFTGL LEQKEGSFKC
     PVTIVYGAKD TAFHRPFCFE GLEEYLVPPK GKTGKSYLIC FPRDGHWTMI PSPAKESVDT
     LIESALDGID GEEMKERVWA VNKDVKFEIE N
//
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