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Database: UniProt
Entry: A0A0A1VA76_9HYPO
LinkDB: A0A0A1VA76_9HYPO
Original site: A0A0A1VA76_9HYPO 
ID   A0A0A1VA76_9HYPO        Unreviewed;       660 AA.
AC   A0A0A1VA76;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=X797_001523 {ECO:0000313|EMBL:EXV06801.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV06801.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXV06801.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV06801.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXV06801.1}.
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DR   EMBL; JELW01000001; EXV06801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1VA76; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000030151; 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..24
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           25..660
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005108715"
FT   DOMAIN          67..613
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          51..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  70931 MW;  3C86E77FFAA352B7 CRC64;
     MAIGSQLSLL LAAATALAPA QVAAAVVQDL PRQHDASGSA DVVVRQASLV QRATDQSPKG
     YAPSPVDCPT SRPKVRDGGG LSSQEREWLP KRRNETVAPI RELLKRIAIP GFDSDAYLKN
     AASDPTALPN IGLAVSGGGY RAMLNGAGAV AAWDSRSTGS QTKGNLGGLL QSATYISGLS
     GGSWLVGSMY TNNFTSVQDA VNAPQIWQFD DSILKGPEQY SLLQYYSEIL DDVDAKDKAG
     FDRSITDYWG RMLAYQLINA TNGGPGFTYS SIAKDPDFSS GKNPLPLIVA DGRAPGQKII
     ASNSTIYEFT PWEFGSFDPS LQGFVPLQYV GSNFTNGSIP SNQKCIVGFD NAGFIMGTSS
     SLFNQIIMYI KDGNSRYVPE DIPKFVVDAL TTFLNALGDE SNDIADWTPN PFKGWNTAKN
     PSANETRLTL VDGGEDLQNV PYHPHLFRER RVDVVFSIDS SADTDSSWPD GASAIATYER
     SLQSSVANGT GFPAVPGKDT FVNLGLNSRP AFFGCDSSNL TAPSPLIVYI PNYPYIYESN
     ISTFQMAIKS DERDAIVQNG WAVATQLNST RDPDWAVCVG CAMLARSFER TRTAVPDKCR
     QCFTNYCWNG TLNETKPAPY VPSLYGKPIL SKSSGAAGQE LSAMMTTVGL VVMAVTAFNL
//
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