ID G2YRJ9_BOTF4 Unreviewed; 330 AA.
AC G2YRJ9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Similar to epoxide hydrolase {ECO:0000313|EMBL:CCD54247.1};
GN ORFNames=BofuT4_P129470.1 {ECO:0000313|EMBL:CCD54247.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD54247.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; FQ790350; CCD54247.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YRJ9; -.
DR STRING; 999810.G2YRJ9; -.
DR HOGENOM; CLU_020336_7_0_1; -.
DR InParanoid; G2YRJ9; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; PTHR43798:SF30; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14860)-RELATED; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCD54247.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT DOMAIN 29..313
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 330 AA; 38250 MW; 559870C0A0083C70 CRC64;
MDAFEKKTLK TSRGYTYTYY TSEGDRSLPT LFFQHGWPDH AEMWKGIAER LIDTKFPIII
PDLLGYDGTD KPTDPAEYKW DVMTKDLIDI IDTEKVDKVI SIGHDWGSVC AARLYNYHPE
RVVGCMFFNL GYSPPSREPF DLAEWNKTAE QAFGYGPWHY WYLFADPNGG KVLKDNVERL
YSCIHGAGDS LKQYFCFPNV IRQHLTNSAP GPEVRPYAQD TKFRQDFIDR MRRDGFDAPQ
CWYRAFLEQQ HLCDKNLPEG RDKVDVPVLY IGGKDDSVCR VEAMYPAIEQ GWLPKLDQKP
LLDAAHWTPY EKPEEAAGLI KEWLGKNYEK
//
