ID   A0A1X6MJ87_9APHY        Unreviewed;       626 AA.
AC   A0A1X6MJ87;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=POSPLADRAFT_1050753 {ECO:0000313|EMBL:OSX56222.1};
OS   Postia placenta MAD-698-R-SB12.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX56222.1, ECO:0000313|Proteomes:UP000194127};
RN   [1] {ECO:0000313|EMBL:OSX56222.1, ECO:0000313|Proteomes:UP000194127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX56222.1,
RC   ECO:0000313|Proteomes:UP000194127};
RG   DOE Joint Genome Institute;
RA   Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA   Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA   Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA   Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT   "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL   Submitted (APR-2017) 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; KZ110614; OSX56222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6MJ87; -.
DR   STRING; 670580.A0A1X6MJ87; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000194127; 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:UP000194127};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           22..626
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5010755661"
FT   DOMAIN          35..626
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   626 AA;  66850 MW;  8D5BCA18D68102FD CRC64;
     MKHLALLLSA VLCCIPLPVA SQLAASVAYA PVLTPCPSGV SLLREVGTVD QSLSDGEHAY
     VAGRRSEVLP GAWGSYLAAV LKSMTGVTNL PEYVTDILGG TYGERGYPHF GIVTSGGGYR
     AAIFGAGVLN TLDGRNTTSV EAGTGGLLQA ATYLAGLSGG SWLVTSLAQA NFPTLPDLIF
     GPSASGKDSF GGWLTQFDLL APSDDPLVDG VYLLDVVAEI MGKHSAGFPV TISDVWARTL
     SRHFVNGTDA SNFWDDTLKH GAGLTLSSIA DLNTFANYAQ PFPIIIADSL SPNGNESNVL
     NETDIDVPLT NPIYEINVFE FGSFDPTLSA FTPTEYLGSP NDSLCATNVD QLCFIEAMSS
     NAYNVYNTSV SSQRTGAPVG DANLAYKAAA AVMELVVEAF SQLIPESKVE LDVAIVPNPF
     HGVAPSTYID SNETLLQLVD GGEDGETVPF MPLLVKARNV EVIFAIDVHR RQAADTEDNW
     TAGLSIIATQ DRVAFFTDTY SFPPVPPLES TFLEYNLTKR PTFFGCESTV ESGEPLVIYL
     ANGGPPLGQP PLTNTSTAQF TYSADEIDKM LSQTFDIATQ GIPEGLEKDP LWPACLACAV
     VDRSRRRERI ERSGVCESCM ERYCWS
//