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Database: UniProt
Entry: F4RZ30_MELLP
LinkDB: F4RZ30_MELLP
Original site: F4RZ30_MELLP 
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}.
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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
//
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