ID   A0A1L7X271_9HELO        Unreviewed;       173 AA.
AC   A0A1L7X271;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=PAC_09000 {ECO:0000313|EMBL:CZR59108.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR59108.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR59108.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR59108.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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; FJOG01000013; CZR59108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7X271; -.
DR   STRING; 576137.A0A1L7X271; -.
DR   Proteomes; UP000184330; 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   Pfam; PF01735; PLA2_B; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|RuleBase:RU362103};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU362103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330}.
FT   DOMAIN          10..107
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|Pfam:PF01735"
SQ   SEQUENCE   173 AA;  18882 MW;  65F16AFD1B68631F CRC64;
     MAHIRRVTPS DIFKQISVKL KAGFTISFAD YLGRSLTYEF VQGLVGGIET KFSSYNKIDT
     FDPGFFWLQF LTYDAAIYGI TPLEFSAWSR GSVGAFAPTE RLGTRLLGSF LISTSADAFN
     ALYIESLSNG TEAQSSKHAS NVHGTKRLNQ LTSMAPLTGF GALVQELVFG GLQ
//