ID A0A094AYL4_9PEZI Unreviewed; 992 AA.
AC A0A094AYL4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN ORFNames=O988_01649 {ECO:0000313|EMBL:KFY03192.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY03192.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFY03192.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY03192.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable lipid hydrolase. {ECO:0000256|ARBA:ARBA00002682}.
CC -!- SIMILARITY: Belongs to the PLPL family.
CC {ECO:0000256|ARBA:ARBA00006104}.
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:KFY03192.1}.
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DR EMBL; JPJR01000262; KFY03192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094AYL4; -.
DR STRING; 1391699.A0A094AYL4; -.
DR HOGENOM; CLU_009031_2_0_1; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 CDD; cd00879; Sar1; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF66; TRIACYLGLYCEROL LIPASE PTL2; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS51422; SAR1; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..992
FT /note="PNPLA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001892489"
FT TRANSMEM 376..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 567..758
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 295..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..967
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 111955 MW; 60520D1A50F25203 CRC64;
MWMISWFWDV LSSLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVAILQP TLHPTSEELA
IGNVKFTTFD LGGHQQARRL WKDYFPEVSG IVFLVDAKDH ERLSESKAEL DALLSMEELQ
KVPFVILGNK IDHPDAVSED ELRHQLGLYQ TTGKGKVPLE GIRPIEVFMC SVVMRQGYGD
AIRWLSHFLI LPVSIARGSG TETCPVLISA RVAGDLIALR STAETYHKLR FRMADRRKAT
DGPPPDSRAG YDVSLLPDYQ VQFVSEDDLA AFAKALAAPD LEPIGDDASA IISNGVDTPS
LDRMNSNPTS KDRTQSRKGS QTSLFITSKN DWAPVHEKVR RKAGSGKTGR KARRRKGLMR
TTDETREGYL YSLLKWPMLF VVVLWVSGLG ISYLLTRLYI WLYEQFVSLR GTRSMLRKKM
RTTTSYSAWV KLAEEMDTFL GNDKWKEEDE FAYYDHKTIR RVLDSLRRQR RRAEAEEGLE
DGASKYGTRP IEELKTLVQA CVKNNFVGVE SNRLYSQTYF GTKNLVQDFI DEVEKGVQTL
SRTKQLTQEE KRATFKHMYT NVGRTALCLS GGASFAYYHF GVVKALLDAD LLPDVITGTS
GGALVAALTA TRTNEELKAL LVPALAAKID ACSEPFTTWF PRWWKTGSRF DSIDWARRCS
WFSHGSLTFR EAYERTGRIL NVSCIPADPH SPTLLLNYLT SPDCVIWSAV LASAAVPGIL
NPVVLMTKLP NGTLAPYSFG HKWKDGSLRT DVPLRALNLH FNVNFSIVSQ VNPHINLFFF
SSRGTIGEPV THRRGRGWRG GFLGSATEQY LKLDLTKWLK VVRHLELLPR PMGQDWSQVW
LQQFSGTITV WPRGRITDFL RILSDPDPTR LAYMIQTGQQ STFPKLQYLG NRMKVERAVE
RGRAETRQHV RRGSIESIIS EDEIRRLWKG DGAEDGSGGM GTTDEDTDWN ADDGVLYEED
GDELERAMDE YERESETDGL TMAGKRARKT TS
//
