ID A0A094EUY2_9PEZI Unreviewed; 958 AA.
AC A0A094EUY2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN ORFNames=V499_04580 {ECO:0000313|EMBL:KFY75455.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY75455.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY75455.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY75455.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY75455.1}.
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DR EMBL; JPKB01000699; KFY75455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EUY2; -.
DR HOGENOM; CLU_009031_2_0_1; -.
DR Proteomes; UP000029295; 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 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..958
FT /note="PNPLA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001901608"
FT TRANSMEM 343..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 534..725
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 270..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 108377 MW; A8C213EE804950D1 CRC64;
MWMISWFWDV LSSLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVAILQP TLHPTSEELA
IGNVKFTTFD LGGHQQARRL WKDYFPEVSG IVFLVDAKDH ERLSESKAEL DALLSMEELQ
KVPFVILGNK IDHPDAVSED ELRHQLGLYQ TTGKGKVPLE GIRPIEVFMC SVVMRQGYGD
AIRWLSQPAL YLHSTAENNY KLPFGMADRR KATDGPPPDS RAGYDVSLLP DSQVQFVSED
DLAAFAKALA APDLEPIGDD ASAIISNGVD TPRLDRMNSN PGSIDRTQSR KDSQTSLFIT
SKNDWAPVHE RVRRKGKKAR RRKGLMRTTD ETREGYLYSL LKWPMLFIVV LWILGLGASY
LLTRLYIWLY ERFIALRGTR NMLRKKMRAT TSYADWVKLA QEMDTFLGND KWKEDDEFAY
YDHKTIRRVL DSLRRQRRRA EAEEGLEGGS SKYATRPIEE LKTLVQACVK NNFVGVESNR
LYSQTYFGTK NLVQEFVDEV EKGVQTLSRT KQLTQEEKRV IFKHMYTNVG RTALCLSGGA
SFAYYHFGVV KALLDADLLP DVITGTSGGA LVAALTATRT NDELKALLVP ALAAKIDACS
EPFTTWFPRW WKTGSRFDSI DWARRCSWFS HGSLTFREAY ERTGRILNVS CIPADPHSPT
LLLNYLTSPD CVIWSAVLAS AAVPGILNPV VLMTKLPNGT LAPYSFGHKW KDGSLRTDVP
LRALNLHFNV NFSVVSQVNP HINLFFFSSR GTIGEPVTHR RGRGWRGGFL GSATEQYLKL
DLTKWLKVVR HLELLPRPMG QDWSQVWLQQ FSGTITVWPR GRITDFLRIL SDPDPTRLAY
MLQTGQQSTF PKLQYLGNRM KVERAVERGR AATRQHVRRG SIESIISEDE MRKLWKGDGE
DGSGGIGTTD EDTDWNADDG ALYEEGGDEL EQAVDGYERE REIEGLTMAG KRAREKTI
//
