ID   PLPL_PHANO              Reviewed;         833 AA.
AC   Q0V4Z6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein SNOG_00918;
DE            EC=3.1.1.-;
GN   ORFNames=SNOG_00918;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445325; EAT92413.2; -; Genomic_DNA.
DR   RefSeq; XP_001791585.1; XM_001791533.1.
DR   AlphaFoldDB; Q0V4Z6; -.
DR   SMR; Q0V4Z6; -.
DR   STRING; 13684.SNOT_00918; -.
DR   EnsemblFungi; SNOT_00918; SNOT_00918; SNOG_00918.
DR   GeneID; 5968394; -.
DR   KEGG; pno:SNOG_00918; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_1_1; -.
DR   InParanoid; Q0V4Z6; -.
DR   OrthoDB; 425613at2759; -.
DR   Proteomes; UP000001055; 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..833
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   SNOG_00918"
FT                   /id="PRO_0000295564"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          301..457
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           332..336
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        54..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        444
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   833 AA;  94015 MW;  86BB0CC736706189 CRC64;
     MTDVKKESDG PEPYSSSAFD FTLLPDYNND FINEDDFAEF AKALAAPDHL SPSTEDLTAP
     QPETGKFSAN NDWKPIHQRV RRRKKSKAPP RRGKDETREG FVYVLLKWPL LVVVLGWLLF
     LSIAYVFTRL YIYLYEHMVT WRGTRQKLRR QLQNASSYEE WIKCAQQLDT HLGSDDWKKN
     PSYSYYDSKT IRKVHEQLVK LRQRAESDET GKSTEKHVDG QPRAVEDLRA LLEACIKNNF
     CGFENPRLYS ETYYGTKDAV QSFIEEAEAS LAFLLNSSQL DAENKRALFK HLGSNFGRTA
     LCLSGGATFA YYHFGVAKAL LDAGVLPEII TGTSGGALVA ALLCTRTDEE LKKVLVPALA
     GRITACHEDT WTWMKRWYAT GARFDSVDWA KKCAWMTRGT PDCVVWSAVL ASAAVPGILN
     PVVLMKKNRD GTLSPYSFGH KWKDGSLRTD IPLKALNLHF NVRFSIVSQV NPHINIFFFS
     SRGSVGRPVT HRRGRGWRGG FIGSATEQYL KLDLNKWLKV LRHLELLPRP LGQDWSEIWL
     QRFSGTITIW PKSIPSDFFY ILTDPTPQRL ARMIHVGQQS AFPKLKFIAN RAKLEHLIQQ
     GRRQYRPRGI REDIQAVLSE DDLQGLLKRT KSKSPSEEAI YPLSGSESSS SADFSRPGSP
     ITLPLGFTFT RKNKKGLADL RTDPKALTDT PNSPSLSARL TGWWNTKSPR DSHPSTPKDP
     SRSLSPFTHH DRPNSMFELR PPKEVRDLQA RTHGRPQHRN SDFLEEIRRR SSAFVEGEGS
     DDEGRAGRYR RGDVDAGAQD AEVYGEPAEF GDNEGDGEEV QSAVGLGLEG KGL