ID A0A2C5WZQ1_9PEZI Unreviewed; 837 AA.
AC A0A2C5WZQ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN Name=Pla2g4d {ECO:0000313|EMBL:PHH51273.1};
GN ORFNames=CFIMG_007244RA00001 {ECO:0000313|EMBL:PHH51273.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH51273.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH51273.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH51273.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH51273.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH51273.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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:PHH51273.1}.
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DR EMBL; APWK03000100; PHH51273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5WZQ1; -.
DR STRING; 1035309.A0A2C5WZQ1; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000222788; 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 CDD; cd00147; cPLA2_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF40; LYSOPHOSPHOLIPASE; 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:UP000222788}.
FT DOMAIN 206..828
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 92358 MW; 5C7482FF259AB1EB CRC64;
MPRVSPLVRR ALRTRRLQPL VAHPYAPVSL RLYSGREGAG SASGRRRSQK TLPGSFYREL
FTSSKALGSP QSSRTHRSTP TSTTAVVTSA LLFIWMLYPT DEFDQLKPSA GSSVPTEPAS
EGPGLPLPSL PLDTAWANFA SNFETFSDSM DIEWTLSTDK IVDLILPEWS RLVPAYFRKL
QRELSMAPGS LADEIWTDAH DAIINPEIRY AAKVRVSNEL CEEEREFVSR RRKMAAVALA
RYLDLEETDV NPDDVPTIAM CGSGGGLRAL VAGAGSLLAA EKDGLLDCVM YTAGVSGSCW
LQAIFNSSLS SGKASKVLDH LKARLGVHIA YPPVALDAIS SAPTNKYLLE GLVEKLKGDP
KAQFGLVDIY GILLSSRLLV PKSHLGINQE NFKMSNQQKY IRYGQAPMPI YTAVRHEIPK
LDDDNGNRAS TEHEKAVAKK EAWFQWFEIT PYEFFCEEFS AGIPTWALGR RFNKGLDVPQ
EDGFHLPEIR MPLLMGVFGS AFCATLNHYY REIQPIMRSI SGFAALDQIV TGRSDDLSKV
HPIEPATLPN FAYGMHGQLA KTTPESILNS EYIQLMDAGM SNNLPIYPLL RPGRDVEVII
AFDNSADIKN DNWLAVTDGY ARQRKIRGWP AGIGWPKGVA PEEAGEQIEK AGEQIEKAGD
RSPAEARSAI DMAQEQDMAR KSNMKSSDIA RENGLGYCTV WVGQTSETNT GSNGDVPPPK
AIVDFTESGV SWNTAGIAVI YLPLLANGKV PGVDPRMSDY LSTWNFVYTP EQVDSVAALA
QANYSEGKQQ LRACIRAVYE RKKKVREDKV KAMKSEKLRR QLRKGIVNKL GEGDHFS
//
