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Database: UniProt
Entry: W9Z4R3_FUSOX
LinkDB: W9Z4R3_FUSOX
Original site: W9Z4R3_FUSOX 
ID   W9Z4R3_FUSOX            Unreviewed;       655 AA.
AC   W9Z4R3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=FOMG_17045 {ECO:0000313|EMBL:EXK26370.1};
OS   Fusarium oxysporum f. sp. melonis 26406.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK26370.1};
RN   [1] {ECO:0000313|EMBL:EXK26370.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK26370.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum melonis.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXK26370.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK26370.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT   26406.";
RL   Submitted (MAY-2012) 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}.
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DR   EMBL; JH659362; EXK26370.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9Z4R3; -.
DR   VEuPathDB; FungiDB:FOMG_17045; -.
DR   HOGENOM; CLU_014602_3_0_1; -.
DR   Proteomes; UP000030703; 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}; Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           21..655
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005152031"
FT   DOMAIN          53..606
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   655 AA;  71174 MW;  337458BF9E57F30D CRC64;
     MAKILSLVVL ALSFSSPAIA APDATAIAHV VNTVGIRALP DSPSGNYAPR VVDCPSKRPT
     IRLADELSDS ETAWVRRRRD NTIDPLKDLL SRAKIPGFDA EAYIDRVKKN SSALPIIAIA
     ASGGGYRALM NGAGFLSAAD SRNNESGPIS GLLQSSTYLA GLSGGGWLVG SIFANNFSTI
     PELQRGTSDS AVWRFDRSIL KGPKSSGIGL LNTADYWKDI SHAVDEKDKG WNTTLTDWWG
     RALSYQLIND SDGGPAYTFS SIAETSSFKD ADTPFPILVA DGRAPGDRVI SLNATVFEFN
     PFEFGTWDPT IYGFAPIRYL ASNFTNGTIS SQGECVRGFD QLGFVMGTSS SLFNQFLLHN
     ITKIGAENDI PSFIINTIGT ILKGLDVGNE DIAQYTPNPF FGWNPTNKSI NAKDYQLTLV
     DGGEDLQNLP LHPLIQPTRG VDIIFAIDSS ADTVNNWPNG TALRATYDRA DSRIGNGTLF
     PHIPSAETFI NKRLNQRPTL FGCDANNFTL LDGQFPPPLI FYIPNAPYTA HSNVSTFDMT
     YSIRERDNII QNALNGATQG NSTIDKEWSV CVVCAIMSRS WWKANEDIPD ACNTCFDRYC
     WDGKSNDTAV RDYEPEYIIG ESQSQKEEDN AAGARFGPSS YATIATGAVL LSIVL
//
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