ID   A0A0F7ZSX1_9HYPO        Unreviewed;       176 AA.
AC   A0A0F7ZSX1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=HIM_08476 {ECO:0000313|EMBL:KJZ72103.1};
OS   Hirsutella minnesotensis 3608.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX   NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ72103.1, ECO:0000313|Proteomes:UP000054481};
RN   [1] {ECO:0000313|EMBL:KJZ72103.1, ECO:0000313|Proteomes:UP000054481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3608 {ECO:0000313|EMBL:KJZ72103.1,
RC   ECO:0000313|Proteomes:UP000054481};
RX   PubMed=25359922; DOI=10.1093/gbe/evu241;
RA   Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA   Bushley K.E., Xiang M., Liu X.;
RT   "Comparative genomics and transcriptomics analyses reveal divergent
RT   lifestyle features of nematode endoparasitic fungus Hirsutella
RT   minnesotensis.";
RL   Genome Biol. Evol. 6:3077-3093(2014).
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; KQ030552; KJZ72103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7ZSX1; -.
DR   OrthoDB; 2332239at2759; -.
DR   Proteomes; UP000054481; 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   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:UP000054481}.
FT   DOMAIN          48..176
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   176 AA;  19102 MW;  AC5B53FE864DF126 CRC64;
     MTRLLSSSSS MDADLIFEAT KLRNSMLAEV VQLASEPGPQ KYAPRAVTCP RLRPRIRIGS
     TLSSQEKAWV QRRQRETARH LRDLFSRISI PDFNSNNYIK QSESSRALPV IGIACSGGGY
     RAMLNGAGVL ASWDSRSEGS RQRSGLGGLL QSATYISGLS GGGWLVGSEF KRPAVA
//