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
//