ID   A0A3M9XYH3_9PEZI        Unreviewed;       814 AA.
AC   A0A3M9XYH3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=D7B24_002062 {ECO:0000313|EMBL:RNJ53307.1};
OS   Verticillium nonalfalfae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ53307.1, ECO:0000313|Proteomes:UP000267145};
RN   [1] {ECO:0000313|EMBL:RNJ53307.1, ECO:0000313|Proteomes:UP000267145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ53307.1,
RC   ECO:0000313|Proteomes:UP000267145};
RA   Stajich J.E., Kasson M.T.;
RT   "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL   Submitted (OCT-2018) 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:RNJ53307.1}.
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DR   EMBL; RBVV01000147; RNJ53307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9XYH3; -.
DR   STRING; 1051616.A0A3M9XYH3; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000267145; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   CDD; cd00147; cPLA2_like; 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:SF40; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..805
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          92..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..800
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  91263 MW;  128E0EC1ED2D35AF CRC64;
     MRSIVTYIRS SVGHARWFHS RRKGFDALAT HRLASKQFRT GFFTTTPQDE AKKKTRGIPT
     VPAVIIAGGL FVWALYPSEE FDQISEAQTY RRERQLQRKR DKEKLERDEE QERQDQQAAK
     NASSAAWNTF SSSFEAFSNA ADIEWSSLSD RVVGFILPEW SKQIPGFVRK LQRELSLAPG
     SLADEIWRDA HDPFINPEIR HEATVRISTD LCDDEKEFLA RRKMITRIAL AKYLEIDENE
     IHPDDVPVIA MCGSGGGLRA LVAGSGSLHA ADQDGLFDCV TYTSGVSGSC WLQTLYFSSV
     GGRSFPRILE HLKSRAAIHI AYPPVAFQAL VSAPTSKYLL SGLVEKLRGD PQASFGLVDI
     YGLLLAARFL VPKGELEVCD SDFKLSNQRQ YIKYGQNPMP IYTAVRHEIP GIDDNEPVDS
     VEAAKEKAAR EAWFQWFEIT PYEFFCEEFS AGIPTWALGR KFNNGVDVPP EEGFHLPEVR
     VPFLMGVFGS AFCATLSHYY REVRPLVQSL SGFMNLDEII SGRYNNDLEK VHPIDPGTVA
     NFAYGMHGRL PDTTPPSIYD NEYIQLMDAG MSNNLPLYPL MRPGRGVEVL IAFDASADTK
     TDNWLAVADG YARQRKIKGW PVGIGWPKAG EAPEELTKEL ENAEASDLKD ADRRLNEAQI
     EQKKSPGKNT TDDLGYCTVW VGTSQERSTS PPPPSRALDD STHWHISEPD AGIAVVYLPL
     LGNPEAVPGV SPGESDFLST WNFVYTPEQI DQVVALARAN YAQGQRQIRE TVRAVYLRKK
     KLREAKEKER KSERYRGLVR RGMGTRLGEG DQFS
//