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Database: UniProt
Entry: A0A1V6QST8_9EURO
LinkDB: A0A1V6QST8_9EURO
Original site: A0A1V6QST8_9EURO 
ID   A0A1V6QST8_9EURO        Unreviewed;       902 AA.
AC   A0A1V6QST8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN   ORFNames=PENSOL_c043G11337 {ECO:0000313|EMBL:OQD92283.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92283.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
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:OQD92283.1}.
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DR   EMBL; MDYO01000043; OQD92283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QST8; -.
DR   STRING; 60172.A0A1V6QST8; -.
DR   OrthoDB; 1943592at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
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   InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF35; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT   DOMAIN          147..261
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   REGION          507..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..902
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ   SEQUENCE   902 AA;  99385 MW;  AEFB65DD144DFDFD CRC64;
     MPLHTVALGV ALTPTVLHTL ISHYLHRKSL HNKPTVHVTY DEGIQIVRQF LFYASKHPVE
     DLQAFTRQWA PSPHWVRTET ITIPDTFLSS AADAVTKQLG PKGVIRVGGE KWWQWRGPSE
     ELKGEWIEMR NHYNQTEGAG GHCNRVMLYI HGGAYFFGSV DTHRYMMQRH ARKLKGRVFA
     PEYRLSPQFP FPCGLHDCMA AYLWLLNSYE PKEIILAGDS AGGGLALSML VIMRDQGIPL
     PAGAILISPW VDLTHSFPSI VEDNPGDYVP AYGFRHKPSP AWPPPNADDI LEMKRLSRQP
     IVNAEDVKKA IPQPNSTAEE TAIRGYTVHE NGPPLAEHAY PGLQQAPNPA SLHAEPDNIH
     VVLDGKTVEL KDQIQLYTTN QLMSHPLVSP VLQPSLGGLP PLQILSGGGE TLRDEQFYIA
     HKAANPTAYP PSDAYLDEND PTRETLNKYE PTYVQLQVWD NLCHVAPTLS FTRPAKYMFR
     SISQFGSWAL ARAQNGEVEI VDDSALSAVS SNSSEDEDVP GPRTALNSPP DAPGPSSVGK
     AGDPLPAFHQ YMIRQRIDKR GHVFPLDPSS SYPVLEIPPA EVGAINPLLI RMWLDAKKEW
     DIRFAKEKLR IQSRRLKELA HGFQDFDGEC PPPSSLAARR AAPGVLPKRH AKKNYGMMMW
     SGWGSRHDER RMEMEKRAEE SGRRSTRVST DAGQAGAWSS TPATHPQPQK VSDKDLTDTK
     SQSNGYTAVS PDKRERPRNG DSSIGRTSTD PETFSRPLSQ KSAGPILILP EVNNNKFTDE
     NASTRALFHA AGSLPMKSDL SLAHSRYRPS SAAGSAAGRS EMLSDTASTV GGDKDSVAYM
     NMAPDTASTR AVRSARGVIA PIMAGENGRR STDTLSVFSA AGRDSMSHRP EVLDREGSKT
     AE
//
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