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Database: UniProt
Entry: W2RQV5_9EURO
LinkDB: W2RQV5_9EURO
Original site: W2RQV5_9EURO 
ID   W2RQV5_9EURO            Unreviewed;       553 AA.
AC   W2RQV5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=HMPREF1541_07727 {ECO:0000313|EMBL:ETN38103.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN38103.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN38103.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN38103.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) 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|ARBA:ARBA00000960,
CC         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; KB822723; ETN38103.1; -; Genomic_DNA.
DR   RefSeq; XP_008720272.1; XM_008722050.1.
DR   AlphaFoldDB; W2RQV5; -.
DR   STRING; 1220924.W2RQV5; -.
DR   GeneID; 19975066; -.
DR   VEuPathDB; FungiDB:HMPREF1541_07727; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; W2RQV5; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000030752; 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:SF62; 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:UP000030752}.
FT   DOMAIN          1..508
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   553 AA;  59470 MW;  5D21796C2432F76F CRC64;
     MGNLLGRLNI SGFDAQAYLN ENADNTSNLP NIAIAASGGG YRAMLNGAGA VAAFDSRTEN
     STGPGQLGGL LQSATYFSGL SGGSWLVGSI YINNFTSIDA ILGDNTSGLW DLEHSILQGP
     ATVSDYYRQL MDAVGGKTDA GFNDSITDYW GRALSYQLVN ATDGGPAYTW SSIALQPEFV
     DGKMPMPIII ADERAPGQLA IAPNTTVFEF NPWELGTFDP TTYGFAPLEY LGSSFSAGTL
     PQNEECVRGF DNAGFIMGTS SSLFNQGFLL INGTNDTNVL TNAVTAILEQ IGDDNNDISL
     YGPNPFYYYH NETNANAQSP TLYLVDGGED LQNIPLHPLI QPPRSVDIIF AIDSSADTQT
     SWPNGTSMVA TYRRSLDPTG IANGTVFPSV PDQSSFVNLG LNTRPTFFGC DSSNMTGPSP
     LIVYIPNFPY SYLSNVSTFD LQYNTTERNS IIQNGYNVVT MANGTTDMEW PACVGCAILS
     RSLEKTGTDI PRVCQQCFTR YCWNGTINST QPLPYSPEVA LTADAESETA KLTTSLTTLI
     VICAFVMRLH AVF
//
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