ID A0A0A1UWS5_9HYPO Unreviewed; 735 AA.
AC A0A0A1UWS5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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_004504 {ECO:0000313|EMBL:EXV02374.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV02374.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXV02374.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV02374.1,
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:EXV02374.1}.
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DR EMBL; JELW01000005; EXV02374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1UWS5; -.
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; 2.60.270.50; -; 1.
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:SF62; LYSOPHOSPHOLIPASE; 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}.
FT DOMAIN 147..694
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 735 AA; 77975 MW; F2DDD557391096DE CRC64;
MAARELIVIF LNHTNEELSL VPGSVRLDHG EWMTGTPESE PPKEIRAGES GIWRCKSRHV
GSGTVGAVDY CISGYGEKDK ISVSWDVRSV VPSKFEPTVE SDEFAIRVLG GSGWPAVAVF
VLAAVCAGFE HRAVPNAPDG YAPASVSCPS PRPTIRAATG LSANETSWLN LRDNNTIPAL
KSLLTRFNIS GLDTNEYIDN IVKDIDGGNR SAVLPRIGVA VSGGGYRALM NGAGALSAFD
NRTSNSTGKG QLGGLLQATT YLSGLSGGSW LVGSLFVQNF TTVDSIVLST SGFLSTLWQF
DNSILEGPAG LRVGQYYNEL YQTVQDKADA GFNTTITDYW GRALSYQLVN STDGGPAYTF
SSIANDTEFA AANSPMPIII ALERAPGQLQ VPPNATVFEF NPWEMGSYDP EAAAFAPLKY
VGSDFNGGTV SRTAKCFAGV DNAGFVMGTS SSLFNQAFLQ ISRASGVPDV LVRALNRTLG
NIGEENRDIA SWPNPFYKFD GGSNINANAS LLTLVDGGEA LENIPLHPLT LKARQVDVIF
AVDGSADTQT SWPNGTSLVA TYERSTSGEE TNNTAFPVVP DVNTFVNLGL NSRPTFFGCG
NASAGPLIVY VPNTPYTFFS NVSTFDLSYN DSDRNQIIEN GYNVATAGNG TVDGSWATCV
GCAVLARSLE RTGTAMPAAC ADCFSKHCWN GTTNSTTPST FEPQKVIASS GGWTRRPWVP
GLVVWSCGLA AALAV
//