LAEA_GIBZE
ID LAEA_GIBZE Reviewed; 316 AA.
AC I1RAW4; A0A0E0RN03;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Secondary metabolism regulator laeA {ECO:0000305};
DE AltName: Full=Methyltransferase laeA {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:C8VQG9};
DE AltName: Full=Velvet complex subunit laeA {ECO:0000305};
GN Name=laeA {ECO:0000303|PubMed:23874628}; ORFNames=FGRRES_15765, FGSG_00657;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP VEA.
RX PubMed=23874628; DOI=10.1371/journal.pone.0068441;
RA Kim H.K., Lee S., Jo S.M., McCormick S.P., Butchko R.A., Proctor R.H.,
RA Yun S.H.;
RT "Functional roles of FgLaeA in controlling secondary metabolism, sexual
RT development, and virulence in Fusarium graminearum.";
RL PLoS ONE 8:E68441-E68441(2013).
CC -!- FUNCTION: Methyltransferase that performs automethylation (By
CC similarity). No other methyl-accepting substrate has been identified
CC yet (By similarity). Component of the velvet transcription factor
CC complex that acts as a global regulator for secondary metabolite gene
CC expression (PubMed:23874628). Controls the expression of the mycotoxins
CC trichothecenes and zearalenon gene clusters (PubMed:23874628).
CC Negatively controls perithecial induction, but positively controls
CC virulence toward the host plant (PubMed:23874628).
CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:23874628}.
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 -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC laeA, ve1 and velB; Ve1 acting as a bridging protein between laeA and
CC velB (By similarity). Interacts directly with veA (PubMed:23874628).
CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:23874628}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23874628}. Cytoplasm
CC {ECO:0000269|PubMed:23874628}.
CC -!- INDUCTION: Constitutively expressed under both trichothecenes mycotoxin
CC production and sexual development conditions (PubMed:23874628).
CC {ECO:0000269|PubMed:23874628}.
CC -!- DISRUPTION PHENOTYPE: Reduces strongly expression of the transcription
CC factors TRI6 and ZEB2 that control the biosynthesis of the mycotoxins
CC trichothecenes and zearalenon, respectively (PubMed:23874628). Exhibits
CC an earlier induction of sexual fruiting body (perithecia) formation and
CC drastically reduces disease symptoms in wheat (PubMed:23874628).
CC {ECO:0000269|PubMed:23874628}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESU05865.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231663; ESU05865.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970332; CEF72628.1; -; Genomic_DNA.
DR RefSeq; XP_011316350.1; XM_011318048.1.
DR AlphaFoldDB; I1RAW4; -.
DR SMR; I1RAW4; -.
DR STRING; 229533.I1RAW4; -.
DR EnsemblFungi; ESU05865; ESU05865; FGSG_00657.
DR GeneID; 23548139; -.
DR KEGG; fgr:FGSG_00657; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01655; -.
DR HOGENOM; CLU_010595_2_0_1; -.
DR InParanoid; I1RAW4; -.
DR PHI-base; PHI:7193; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Sporulation; Transcription;
KW Transcription regulation; Transferase; Virulence.
FT CHAIN 1..316
FT /note="Secondary metabolism regulator laeA"
FT /id="PRO_0000435751"
SQ SEQUENCE 316 AA; 36780 MW; E4F307F957672137 CRC64;
MAVMPPPNSV NGSERRYLED GIWQHGRFYG SWKPGKYLFP IDSEELNRLD IFHKVFLLAR
DNKPFQAPIQ RKAPRMMDIG TGTGIWPINV AEECFTDAQI MAVDLNQILP ALIPPGVLPK
QYDIEEPTWD SLYTDCDFIH MRMLLGSIQT DLWPQVYRNI FEHLAPGIGH LEHIEVDWTP
RCDDDERPAN SAFEKWAELF FDGMDRFNRI ARVVPQETRQ LLEATGFTDV KQEMIRAYVC
PWSSDRQERE IARWFNIGLS HSLESLSLKP LVEKLGWKPE DVRKLCTTAK RETCVLRFHT
YCNIYVWTAR KPGPPQ
