ID   A0A437A985_9PEZI        Unreviewed;       839 AA.
AC   A0A437A985;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN   ORFNames=DFL_001989 {ECO:0000313|EMBL:RVD87779.1};
OS   Arthrobotrys flagrans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD87779.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD87779.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD87779.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipid hydrolase. {ECO:0000256|RuleBase:RU362055}.
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000256|ARBA:ARBA00002682}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362055}; Single-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362055}.
CC   -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000256|ARBA:ARBA00006104,
CC       ECO:0000256|RuleBase:RU362055}.
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:RVD87779.1}.
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DR   EMBL; SAEB01000003; RVD87779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437A985; -.
DR   STRING; 97331.A0A437A985; -.
DR   VEuPathDB; FungiDB:DFL_001989; -.
DR   Proteomes; UP000283090; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR   CDD; cd07232; Pat_PLPL; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   PANTHER; PTHR14226:SF66; TRIACYLGLYCEROL LIPASE PTL2; 1.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362055};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU362055};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU362055}; Membrane {ECO:0000256|RuleBase:RU362055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW   Transmembrane {ECO:0000256|RuleBase:RU362055};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
FT   TRANSMEM        79..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362055"
FT   DOMAIN          267..458
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          650..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  94154 MW;  020D8C041D235FE1 CRC64;
     MASNDSVTDA SEPYAAHEYP PEFVVDYSNK KHINQFAQVL NAPPSAPDVF ISAESDWKPI
     RQRVGKRRRK SRKDETREGF SYALFSWPLL LLVFGWILFL GFLYFLTRIY IWLYEHFVTH
     RGKRQRLRLA LRKSRNYDEW KVAAQELDHY LGADEWRETE EFSYYDYITI RRVLTELQDF
     RLRAKKDDDV IEGLAALVRA CVKNDFAGIE NPRLYSQTYY GTKNLLQDYY DELERCLRIL
     VDTDQLTSDE KRKLFKHLSK NLGRTALCLS GGACFAYYHF GVLRAHLDAG VIPNIITGTS
     GGGLVAALVG TRTDEELKIV IRPELADKIT ACHDSMAVWM TRWWKTGARF DSVDWASRAL
     WFTRGSMTFR EAYERTGRTL NISCVPSNPN SPSILLNHIT APDCVIWTAL LASAAVPGIL
     NPVVLMMKTK NDDLIPYSFG HKWKDGSIRT DIPLQALNLH FNVNFPIVSQ VNPHITLFFF
     SSRGTVGRPV SHRKGRGWRG GFLGSATEQY LKLDLNKWLK VIRHLELLPR PLGTDWSTLF
     LQRFYGRVNI LPRTKLIDYY YILSDPSRER LSWMIKSGEH ATFPKLKFIR NRWKIEKLVE
     EGRRKHKGKG AELEAILSSE DIASLLKQKK GGSGSISKRN SRRMSADLSN IVGTAPGLPN
     GIGESRSPTT TGSSGTASPN AQRFSWFKNN LWSGSINDVL ASPRNTEFRR RSVMSLKGLG
     LGSRNGSQET VRAVLEGDGG ANGGLFTPIP AQADSGMSEG EDEGRYFGAA GGEFGGYEDL
     TSAVGTEDSA SGSDGDVFSG SEGRNGFEEY DDEDGLEMGR GVEAGGKPGK MEFFSAGPS
//