ID A1DCP5_NEOFI Unreviewed; 320 AA.
AC A1DCP5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Phospholipase/carboxylesterase, putative {ECO:0000313|EMBL:EAW19605.1};
GN ORFNames=NFIA_026790 {ECO:0000313|EMBL:EAW19605.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19605.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000256|ARBA:ARBA00006499}.
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DR EMBL; DS027695; EAW19605.1; -; Genomic_DNA.
DR RefSeq; XP_001261502.1; XM_001261501.1.
DR AlphaFoldDB; A1DCP5; -.
DR EnsemblFungi; EAW19605; EAW19605; NFIA_026790.
DR GeneID; 4588005; -.
DR KEGG; nfi:NFIA_026790; -.
DR VEuPathDB; FungiDB:NFIA_026790; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_2_1_1; -.
DR OMA; IPINQWF; -.
DR OrthoDB; 910288at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR10655:SF72; -; 1.
DR PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 18..177
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
FT REGION 183..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 35138 MW; D4C2F7716E6CBD88 CRC64;
MPSSKPYPSP LVIAPLRDDQ HTHTIILLHG RGSNSERFGH VFIESTGIAK RLPTTKFIFP
TARKRRSTVL KRIPINQWFD NYSLKNPNTR TELQIDGLQE SSEFLRKLIV EEAKLLSNDP
AVGDGYSRVV IGGLSQGCAA SVFCLLGGFP SASEDGDSRR LGGYIGMSGW LPFEGEISGF
LSIDEDNQGE PKSGAEDDDD DDPFAHDTDV DVPAHSQAVN HVREILGTPP IQTDADDSEN
ALCVSYLKTP VFLGHGAADP KVSVDLGRRM ASILSDGFGM DVTWKAYEEF GHWYKVPDEI
DDVVLFLKEK AGFSVVENVE
//
