ID A0A165C744_9APHY Unreviewed; 605 AA.
AC A0A165C744;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=LAESUDRAFT_730299 {ECO:0000313|EMBL:KZT02314.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT02314.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT02314.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT02314.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV427653; KZT02314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165C744; -.
DR STRING; 1314785.A0A165C744; -.
DR InParanoid; A0A165C744; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000076871; 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:UP000076871};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 21..605
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5007748304"
FT DOMAIN 34..605
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 605 AA; 63960 MW; A87420D9299816EF CRC64;
MFAVLLALSG LCWLPLYASA QSQASKAYAP VVAPCPSGIS VLREAGTTNQ SLSEGESAYV
SGKRKTVLPA AWKSYLAAVN GSTSDVVSLP SYVSAILNGS FGGSAYPNLS IATSGGGYRA
ATFGAGVLNA LDARNATSVR AGTGGLLQAS TYLAGLSGGS WMVTSLAQAD FPTLYDLVLG
PETTTSSGFN GWLANFSLFD PSDSIVQDTV YIIDLADETD GKAGKGFNVS ITDVWARALS
RHFANGTTAA TFLEKNVTHG AGLTFSSIST LPAFTSHTLP FPIVVTDSIS PYQNDSNILN
ETEVLVPLTN PIYEINAYEM GSFDPVLGAF ILTKYLGTTN STLCVTEYDQ VSFIEGLSSS
LFNEAVVLEN AEISDFIEIL SEYLPDGGDI FYGLLPNPFH GLSPNTYIAS NQTVLQLVDG
GEDGEEIPFT PLLVKAREVD VIVAIDAAAD TSYNWADGSS LIATQDRVSY FPGTYAFPPV
PTSASTFLSK NLTRYPTFFG CNSSVNSSEP LVIYLANGGP PLGQTPATNT STLQLSYGAE
ELEAMLSQTF DIATQGRATE SSAGWEKDPE WPACLACAVV DRSRQREGVT RSGVCASCLD
RYCWS
//