ID A0A1C7MJ80_GRIFR Unreviewed; 617 AA.
AC A0A1C7MJ80;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=plb2 {ECO:0000313|EMBL:OBZ76687.1};
GN ORFNames=A0H81_03934 {ECO:0000313|EMBL:OBZ76687.1};
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ76687.1, ECO:0000313|Proteomes:UP000092993};
RN [1] {ECO:0000313|EMBL:OBZ76687.1, ECO:0000313|Proteomes:UP000092993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9006-11 {ECO:0000313|EMBL:OBZ76687.1,
RC ECO:0000313|Proteomes:UP000092993};
RA Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT "Whole genome sequencing of Grifola frondosa 9006-11.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|RuleBase:RU362103};
CC -!- SIMILARITY: Belongs to the lysophospholipase family.
CC {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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:OBZ76687.1}.
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DR EMBL; LUGG01000003; OBZ76687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7MJ80; -.
DR STRING; 5627.A0A1C7MJ80; -.
DR OMA; FASCLAC; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000092993; Unassembled WGS sequence.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU00555};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 19..617
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5008810967"
FT DOMAIN 52..617
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 617 AA; 65976 MW; E13B08DA985C9E65 CRC64;
MNILLVTILL GYSSFAASQT AAEVAYTPIL APCPSGTELI RLTGAQNQSL SSSEAAYIST
RHRTVIPKAW VSYLENVQQS TNQSLPVYVH DIFCGNYGYD VAPKLGISVS GGGYRAAVFG
AGVLNALDGR NISSIRAGTG GLLQATSYIS GLSGGSWLVG SLAQADFPTI PGLIFGNPNA
STHEFGGWIA EVDLLAPTAD NETNIAYLEE IIQEPSGKYA AGFQVSRADD LSRLYARHFV
NGTNVNNFFN NSLLHGAGIT FSAIADVPSF NAYEQPFPIL VADSFSPNGN MSTMLDWTGV
AVPLTNPIYE FNVFEMGSFD PMLSAFTPTK YLGSSNDSTC VTNFDQVSFI VSTSSMEGAV
AYVQQTELSE RAIDTTEQRI RATTDSPAEL PPNPNVNTSL ALFPNPFYGA AANSFIDTNE
TVLQLVDGSL DGENIPIQPF LVKARGVDVI LAVDAGDQAH EGEIDDNFAD GSALIATQLR
VSQPLLRSHY SFPPVPTSHT MFLSQNLTKR PTFFGCNTDP SAPLVIYLAN GAAPLGQSPV
TNISAGQTSI STEQMNAMLA QTFDIATQGI AVETQSHGET VWQKDPEWPA CLACAVADRA
RRRINEERSG VRAQHRS
//
