ID A0A1V6RF11_9EURO Unreviewed; 354 AA.
AC A0A1V6RF11;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN ORFNames=PENVUL_c053G05812 {ECO:0000313|EMBL:OQE00372.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE00372.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE00372.1}.
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DR EMBL; MDYP01000053; OQE00372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RF11; -.
DR STRING; 29845.A0A1V6RF11; -.
DR OrthoDB; 1366960at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF28; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G13270)-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..329
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
SQ SEQUENCE 354 AA; 39518 MW; 5EED99B03877F6CD CRC64;
MSSNHDIPKL GFWEKADIPL MRLSVFANLL YAAITGVFRG KASPRRYDHY IMASVIRGMV
DRTTDRQIQY ISSPTSVAYA TVMKKRGLQP ETVALPHGAE GHWLGNKNAK NVIIYYHGGG
FAIPATASYF EFWLDMLKVL NETGHDLAVF FPRYTLTPHA TYPTQLRQAV EALRYIINET
GRSPANVVIG GDSAGGNLAT ATLLHLSHPH AEIEPLVLSA PLAGVFAYAP WVNFSSEWPS
MKDNRWKDVI TASALTRWSV VYRSGKPADN WNEPFNAPAE WWSGAKTEKI LFLVGSDEIL
LSPVQEFAKK IKSTFEGITC VVGQDESHDA PFYTMVNEEA QTRSELRQWL AARL
//
