ID F4RZ30_MELLP Unreviewed; 683 AA.
AC F4RZ30;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=MELLADRAFT_110225 {ECO:0000313|EMBL:EGG02394.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL883131; EGG02394.1; -; Genomic_DNA.
DR RefSeq; XP_007414379.1; XM_007414317.1.
DR AlphaFoldDB; F4RZ30; -.
DR STRING; 747676.F4RZ30; -.
DR EnsemblFungi; EGG02394; EGG02394; MELLADRAFT_110225.
DR GeneID; 18924008; -.
DR KEGG; mlr:MELLADRAFT_110225; -.
DR VEuPathDB; FungiDB:MELLADRAFT_110225; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_1_0_1; -.
DR InParanoid; F4RZ30; -.
DR OrthoDB; 1826981at2759; -.
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: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:UP000001072}.
FT DOMAIN 101..683
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 108..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 74972 MW; 4CA8D7D93D4B4278 CRC64;
MEPPLMLKVS VLAWFRRRYV RVDTKPADDF WKAYVGFSSA MVWADNWRVS SIGYIQCPAN
FSLRKAGTKS SQQLNPSELH YLQRRRQQIA GPAYVTFLRN VQQSLKAAAA GKKNRPEANT
STQSRRDSNS TTSSNSVLPK YLETILASKD LNILPRTALA TSGGGFRASL YASGVLNAFD
GRNKTSAQVG TGGLLQASDY VVGLSGGAWV VTALAQANFP TLYDLALSGR SPKGKNTASQ
FGSLLLQYDL FSPADNQTVP DGKGIEEKNA KYLADIAARM GEKVKAGFHV TIVDFWSLML
RYHIITGTTE SNFFDQSLPH GIDVTFSGIR NAPTFQRFEQ PFPIITATSL SPRQDETKKQ
PSAFVPLTNT AYEFTPIESG SWDTNLASFI PTEYLGTRLK GGKSETQKCA QGFDQASYLA
AVSSNIFPKV VTSPAYLSKQ SPVFKVMTLI NTTFGSFQPG IPLDTASVPN PFFQEGTNTY
LDKTSADLRL LDGGYDGSMT PYLPMLQPAR KVDIIIGIDA VSLAKDGAVG NEYATGDSLR
AASHRAQLSE GAYSFPRVPS SEAEYEKIRS HPNFFGCNEP EVPLIVWLPN SAPLDGSAGI
TNTSVDQLQY PRKQVESFLG AASEIGYRGF PSEENIKNRV FRDPHWSACL ACAVVDRSRE
RQKIPREGLC NQCFQRYCWN PSK
//