ID   A0A0B2WTD2_METAS        Unreviewed;       665 AA.
AC   A0A0B2WTD2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=MAM_04865 {ECO:0000313|EMBL:KHN97268.1};
OS   Metarhizium album (strain ARSEF 1941).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN97268.1, ECO:0000313|Proteomes:UP000030816};
RN   [1] {ECO:0000313|EMBL:KHN97268.1, ECO:0000313|Proteomes:UP000030816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN97268.1,
RC   ECO:0000313|Proteomes:UP000030816};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(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}.
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:KHN97268.1}.
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DR   EMBL; AZHE01000011; KHN97268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2WTD2; -.
DR   STRING; 1081103.A0A0B2WTD2; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000030816; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           26..665
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005110114"
FT   DOMAIN          74..620
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          59..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  71905 MW;  E8C826AFF488BE29 CRC64;
     MAIGRHLSIL LAAATALAPS QLAAAVVHPQ RLPGPEYLPR QHDPADSADV IRETHLVRRA
     TSQSPKGYTP SPLDCPRSRP RVRDGSSLSP QEREWLPRRR NETVAPIRDL LRRIAIPNFD
     SEAYLKDAAT DPTALPNIGL AVSGGGYRAM LNGAGAVAAW DSRSTGSQTK GNLGGLLQSA
     TYISGLSGGS WLVGSMYSNN FTSVQDAVNA PQIWQFDDSI LKGPQLYSLL QYYSEIIDDV
     KAKAKAGFDT SITDYWGRML SYQLVNATNG GPGFTYSSIA DDPGFSSGKT PLPFIIADGR
     APGQKIIASN STIFEFTPWE FGSFDPSLQG FVPLQYVGSN FTNGSIPDNE SCVVGFDNAG
     FVMGTSSSLF NQIVLYIKDG DSRYVPEDIP KFVVNVLTSL LNSLGDSDND IADWTPNPFK
     GWNTANNPSA RNTRLTLVDG GEDLQNIPYH PHLFHERNVD VVFSIDSSAD TDSSWPDGAS
     AIATYERSLQ SSVANGTGFP AVPGKNTFIN LGLNSRPAFF GCQSSNLTKP SPLIVYIPNY
     PYLYESNIST FQMAIRSDER DAIVQNGWAV ATQLNSTRDP DWAACVGCAM LARSFERTRA
     TVPDKCTQCY TNYCWNGTLN ETKPEPYAPR LYTKGILIKS SGAPGRELGS LMTAVGLAAL
     AVAAF
//