ID   LAEA_MAGO7              Reviewed;         327 AA.
AC   G4MXJ9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Secondary metabolism regulator LAE1 {ECO:0000303|PubMed:28820236};
DE   AltName: Full=Methyltransferase LAE1 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:C8VQG9};
GN   Name=LAE1 {ECO:0000303|PubMed:28820236}; ORFNames=MGG_01233;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RA   Ma L.-J., Dean R.A., Gowda M., Nunes C., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Magnaporthe oryzae 70-15.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28820236; DOI=10.1021/acschembio.7b00353;
RA   Yun C.S., Motoyama T., Osada H.;
RT   "Regulatory mechanism of mycotoxin tenuazonic acid production in
RT   Pyricularia oryzae.";
RL   ACS Chem. Biol. 12:2270-2274(2017).
CC   -!- FUNCTION: Secondary metabolism regulator that controls the expression
CC       of the tenuazonic acid biosynthesis cluster (PubMed:28820236).
CC       Methyltransferase that performs automethylation (By similarity). No
CC       other methyl-accepting substrate has been identified yet (By
CC       similarity). {ECO:0000250|UniProtKB:C8VQG9,
CC       ECO:0000269|PubMed:28820236}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionyl-[protein] + S-adenosyl-L-methionine = S-adenosyl-
CC         L-homocysteine + S-methyl-L-methionyl-[protein];
CC         Xref=Rhea:RHEA:60560, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:15592,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:142742; Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60561;
CC         Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- INDUCTION: Expression is induced by the presence of dimethylsulphoxide
CC       (DMSO) or by the deletion of OSM1, a HOG1-related mitogen-activated
CC       protein kinase. {ECO:0000269|PubMed:28820236}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the ability to produce TeA under the
CC       DMSO-added, TeA-inducing culture conditions.
CC       {ECO:0000269|PubMed:28820236}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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; CM001232; EHA54329.1; -; Genomic_DNA.
DR   EMBL; CM001232; EHA54330.1; -; Genomic_DNA.
DR   RefSeq; XP_003714136.1; XM_003714088.1.
DR   RefSeq; XP_003714137.1; XM_003714089.1.
DR   AlphaFoldDB; G4MXJ9; -.
DR   STRING; 318829.MGG_01233T0; -.
DR   EnsemblFungi; MGG_01233T0; MGG_01233T0; MGG_01233.
DR   EnsemblFungi; MGG_01233T1; MGG_01233T1; MGG_01233.
DR   GeneID; 2679435; -.
DR   KEGG; mgr:MGG_01233; -.
DR   VEuPathDB; FungiDB:MGG_01233; -.
DR   eggNOG; ENOG502QQMC; Eukaryota.
DR   HOGENOM; CLU_010595_2_0_1; -.
DR   InParanoid; G4MXJ9; -.
DR   OMA; RPGTGQI; -.
DR   OrthoDB; 1047281at2759; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Virulence.
FT   CHAIN           1..327
FT                   /note="Secondary metabolism regulator LAE1"
FT                   /id="PRO_0000452835"
SQ   SEQUENCE   327 AA;  37660 MW;  F497B6A990F382F2 CRC64;
     MDKVLHATSL PILPGAIMSK NDAPEVEQLF KENGRLYQVW PRDRYLLPAD QTEQDRLDIF
     SQLFKIILKE KLHTDASRVE ENSHVLDLGC GTGLWVILMA HELHPKPSLF IGADVQMTQP
     DLIPATVRFT PADIEAPWTD EMVQHAPYDL INCRLMKGAI RSWPALYEKI AAHLKPETGV
     FEQFEIDWQF RCDDGPIPPA LKQWSDEVMQ AMDQHGMSIR CNREETRSML LNHGFDDVQE
     QAIVLPISNW AEDERGREIG RWFNLALNHS TLPMSLAPLF RVMKKTPQYI DELNKAASRE
     VCSQAHTDGV YCMLYIWTAR TRPSRRR