ID R7SGU0_DICSQ Unreviewed; 564 AA.
AC R7SGU0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
DE Flags: Fragment;
GN ORFNames=DICSQDRAFT_74300 {ECO:0000313|EMBL:EJF55371.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF55371.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF55371.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF55371.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH719736; EJF55371.1; -; Genomic_DNA.
DR RefSeq; XP_007371890.1; XM_007371828.1.
DR AlphaFoldDB; R7SGU0; -.
DR GeneID; 18844011; -.
DR KEGG; dsq:DICSQDRAFT_74300; -.
DR HOGENOM; CLU_014602_1_0_1; -.
DR OMA; FARYCWN; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000053319; 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:UP000053319};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 24..564
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005145755"
FT DOMAIN 37..564
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT NON_TER 564
FT /evidence="ECO:0000313|EMBL:EJF55371.1"
SQ SEQUENCE 564 AA; 59111 MW; E234DE7169033CD9 CRC64;
MRAILTPLTF YLIACSLGLG AAAESVAAVA YTPSVQACPP RTSLVRQTGS SAQSLSAGEA
AYVSGRQQVA LNAWKGYLAN VQAYLNTSQS NASLPQYVDD ILSGLFGVGP QPRLGIATSG
GGYRSAIFGA GILNALDGRN QTSVEAGTGG VLQAATYLSG LSGGSWLVSS LAQADFPMLP
ELIFGSSPSQ TNDGNAKFGG WLADMDLLTP GGANIIRDAE YLVDIVDEVS GKFSAGFPVT
VTDVWARALS GHFANGTTAA NFFDDNLPHG AGITFSSIVY VSSFVNHEQP FPIVVADSLV
SRTNGSAVTE DGDLVPLTNP IYEFNPFEMG TYDPQLGAFT PMRFLGSPPT NRSTCVTGFD
QLAYIAGTSS NVFNGPNVTS AVLSIIDKIV NFLEETFTQT DVRLDSAAVP NAFFGVSPAT
FPDSDQTVLT LVDGGEDGET DPLQPLLVLA RGVDTIIAID APADTSDNFA AGLDLISTQA
RVQLFPGTYF FPPVPNTTDV YLSQNLTRRP TFFGCNSSAA SDEPFVIYIA NGGPPLGQAP
VTNTPTFQLE YSNGELGAML DQTF
//
