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Database: UniProt
Entry: G1X791_ARTOA
LinkDB: G1X791_ARTOA
Original site: G1X791_ARTOA 
ID   G1X791_ARTOA            Unreviewed;       704 AA.
AC   G1X791;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN   ORFNames=AOL_s00054g735 {ECO:0000313|EMBL:EGX50999.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX50999.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX50999.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX50999.1}.
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DR   EMBL; ADOT01000092; EGX50999.1; -; Genomic_DNA.
DR   RefSeq; XP_011120353.1; XM_011122051.1.
DR   AlphaFoldDB; G1X791; -.
DR   GeneID; 22891310; -.
DR   eggNOG; KOG4231; Eukaryota.
DR   HOGENOM; CLU_391786_0_0_1; -.
DR   InParanoid; G1X791; -.
DR   OrthoDB; 2623704at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07199; Pat17_PNPLA8_PNPLA9_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW   ProRule:PRU01161}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          212..406
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          678..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           216..221
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           250..254
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           393..395
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        680..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        393
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   704 AA;  79633 MW;  7E1CAA2FD364441B CRC64;
     MKRLCKEAIH EFVGRYMSCS YVNENADWEC VNTKNGHVKG HQSEFGDYFA DGEFEEAESP
     NEDSLVTAIE TKIHEIVAKA RNIAGSSPQK WYSFVSVNHK QCMEELRKLG VYPRRKNYRR
     ILSRFLPLWF EGNFFTNSQF CTLCLFGKSE YRLPCQHMIC GTCLKENSSN RIQEPDAMAV
     LEKCVLCDDN GRSHGWPFTV QMLPALANPR ILALDGAGVR GVTQLVLLER LEESIGLGLP
     IGYFFDLVVG SSMGGIVALG LGVEGLPASE CLERFKAISS EGFDNKLGTK TPGLKLISRR
     IRGSIYLQDS YSRAIEEYFD NRKGNITYGL RNHCRVAVTT TVGSDARLIA NYHAGDDEKY
     INSKMTISDA AKCSSMAPLY FEPMLVNGME FWDGGLTANN PVQLALDESN LLWGKPRPDL
     VLSIGTGHSS ALQDEPVGLK NLDEKLKELM ILWLRTMNGQ QDWKNFCNSK RNDPDTLARC
     HRLSVSSVFG REAAFDEADR IISMEMKAQG YNERYKKSYS LYEPVSGECR DDIIEVQANI
     LRASQYYFKV ARILKGGNEK FFIYGSLRCR LNLIHGEPFL YLLKFTNYFT INRLKVFDVD
     EPIRRSQFFD MPVRFEHSSA SGPIRIAVNF NEDTYSVAIS GFPMDIQVLR DYCAETGIEE
     EELDVNFNFE DDDKEQTIVS EDGSSNSDPI ERVMTPSTTA SDFL
//
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