ID   PLPL_NEOFI              Reviewed;         712 AA.
AC   A1D4C8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein NFIA_019760;
DE            EC=3.1.1.-;
GN   ORFNames=NFIA_019760;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
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DR   EMBL; DS027688; EAW23271.1; -; Genomic_DNA.
DR   RefSeq; XP_001265168.1; XM_001265167.1.
DR   AlphaFoldDB; A1D4C8; -.
DR   STRING; 36630.CADNFIAP00001982; -.
DR   EnsemblFungi; EAW23271; EAW23271; NFIA_019760.
DR   GeneID; 4591597; -.
DR   KEGG; nfi:NFIA_019760; -.
DR   VEuPathDB; FungiDB:NFIA_019760; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   OMA; DMNKWLR; -.
DR   OrthoDB; 425613at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:EnsemblFungi.
DR   GO; GO:1990748; P:cellular detoxification; IEA:EnsemblFungi.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006642; P:triglyceride mobilization; IEA:EnsemblFungi.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..712
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   NFIA_019760"
FT                   /id="PRO_0000295562"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          275..466
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           306..310
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        628..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        453
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   712 AA;  81915 MW;  5B39B399C32F9EA4 CRC64;
     MTSDEKSATR DIYDPNTLPD YDREFIDPDD LRQFEKALNA PEAAPLVALN DWRPVNQRVR
     KSRRTKPRRS KDETREGVLY TVLKWPFLFT VFAWITVLGF AYTLTRLYIF LYEQFVTWRG
     KRERLRKELS MQTNYQDWLK AAQALDTYLG NLKWKETDEY AYYDHLTINK VVAQLKQTRK
     AAETEMQNGR SGLSDPPAVE ELCFLLEACV KNNFAGVENP RLYSETYSGT KDLVQEYIDE
     VHSCIRLVLD SKQISNEDKY QFFKHLDTNF GRTALCLSGG ATFAYYHFGV IRALLDNDVL
     PEIITGTSGG ALVAALVATR TDEELKQLLV PALAHRIRAC HEGFTTWVRR WWRTGARFDT
     LDWARQCSWF CRGSTTFREA YERTGRILNV SCVPSDPHSP TILANYLTSP DCVIWSAVLA
     SAAVPGILNP VVLMTKKRDG TLAPYSFGHK WKDGSLRTDI PIKALNLHFN VNFTIVSQVN
     PHINLFFFNS RGSVGRPVTH RKGRGWRGGF LGSAIEQYIK LDMNKWLRVL RHLELLPRPL
     GQDWSEIWLQ KFSGTITIWP KSIPSDFYHI LSDPSPERLA RMLHVGKQSA FPKIQFIKNR
     LKIENAIMQG LQQCSSGGGR VMSPILSRRR QDRAEEHADR MVERLDQSFP ERQSDYKDES
     HYTEVSDSLS ATSSRPHTPD ARRSSMFEEM RRQSAVFFDD SDMYADEDAV TT