ID A7EGT8_SCLS1 Unreviewed; 648 AA.
AC A7EGT8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 ORFNames=SS1G_04530 {ECO:0000313|EMBL:EDO02054.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO02054.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR EMBL; CH476625; EDO02054.1; -; Genomic_DNA.
DR RefSeq; XP_001594722.1; XM_001594672.1.
DR AlphaFoldDB; A7EGT8; -.
DR STRING; 665079.A7EGT8; -.
DR EnsemblFungi; EDO02054; EDO02054; SS1G_04530.
DR GeneID; 5490529; -.
DR KEGG; ssl:SS1G_04530; -.
DR VEuPathDB; FungiDB:sscle_02g016100; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; A7EGT8; -.
DR OMA; FGHINMS; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR CDD; cd07203; cPLA2_Fungal_PLB; 1.
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:UP000001312};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 20..648
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5010392473"
FT DOMAIN 63..609
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 648 AA; 69630 MW; 05CA6DF0BCCEC9B1 CRC64;
MKGFGAILAS VALTSICDAR QLVLPRDASP ETVAAEVLAA PMVALKRALP DSPTGSYTPG
AVDCPDTRPT IRTANELSAN ETSWLRLRRN NTIQPMITFL ERMNITGFNA AEYINSVSNN
ASTLPNIGIA ISGGGYRAML NGAGFLAAAD DRTTNSTNTG QIGGLLQAST YLAGLSGGGW
LVGSIYTNNF STVEALRDGS DVWNFDNSIF EGPNDDGIQI LSTADYYSTI ESQVKGKANA
PLNFNTSVTD YWGRALSFQL VNATDGGPAY TFSSIALEDN FAKANIPMPF LVADGRAPYT
EIIALNSTVY EFNPFELGSW DPTTYAFAPL RYIGSNFTAG AIPDGQQCVR GFDQVGYVMG
TSSTLFNQFL LQANSTSLPS FVTQAFTAIL DKVGFTNNDI AQYQPNPFYG YNNATNRNAQ
TTQLDLVDGG EDGQNIPLYP LIQPIREVDV IFAVDSSADT DFFWPNGTSL VATWERSQNE
TIANGTAFPS VPGQNTFVNL GLNKRPSFFG CDPSNSTGPT PLIVYIPNAP YIYHSNVSTF
DPSYTNEERN LIIRNGYEVA TMANGTIDPD WPTCVGCAII SRSFHKTNTA VPDVCTACFN
KYCWNGTLNT SAVEYDPAYI ASSGVSLQGS KFMSIVVALT AAACILFA
//
