ID F4R357_MELLP Unreviewed; 682 AA.
AC F4R357;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=MELLADRAFT_86725 {ECO:0000313|EMBL:EGG12571.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883090; EGG12571.1; -; Genomic_DNA.
DR RefSeq; XP_007403509.1; XM_007403447.1.
DR AlphaFoldDB; F4R357; -.
DR STRING; 747676.F4R357; -.
DR EnsemblFungi; EGG12571; EGG12571; MELLADRAFT_86725.
DR GeneID; 18934279; -.
DR KEGG; mlr:MELLADRAFT_86725; -.
DR VEuPathDB; FungiDB:MELLADRAFT_86725; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_013227_1_0_1; -.
DR InParanoid; F4R357; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000001072; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072}.
FT DOMAIN 84..682
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 508..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 75300 MW; AAC6CB7F9248CF59 CRC64;
MAGLLVGAIG ISRSRYATKS NCEEKKDSSY GSTIQDWLSI DSMKTQFTSL SSRLSQISSE
LSGDPNSLFQ EIVEESINDQ KLNPELSWRA SVRIGSDIGF CEKGFMRERK HFMRRALASL
IDVDEREIDE RDIPVVGIAA SGGGYRAMTS TTGCLLGARQ SGILDVVSYI SGISGSCWAL
AGWYSVAGGN LLDLSNHIKS RITTPFLDLE NFQLFTDAPT NKYLLAGPVA KLASKGGTTS
LVDVYGTLVS SRLYVPNDLS RLDPHHLKLS NQRHLLDGSL PLPIYCAIYH QVPDQIQRTN
DSDNAGSSSE KVARDQSFIS PSYHWYEMTP YEVGSQDVGA FIPTWALGRA FENGRDVKAR
PEISLSILSG IFASAFTATL AHYYQEVKPG LVMLPFFKAF DAYVSTFESD LSVLHPFPPA
ELPNFLRGLN GQLKPGISAA VTERETLGFM DAGADLNIPY VPLYRRGCDV IISLDASADS
QDVWFSKAET YAQRCGLDTW PIVKYPGSSE SAPATEHADH DAEIPLDKSE VAVKKSRVQA
FSQLENEDQK SSDGDEANPF PAETKGAPDS ANPEPPLGRC NIWVGDSSNK EISARMDEPN
EEMIRSRDGP ALIYIPLAPG NGLDDPAKVW STWRFDYKEE ETEQLLKLSE MNFRSGEQQM
KAVLKAIWKR KRDKRLRMNS ES
//
