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
//