ID   LAEA_FUSO4              Reviewed;         316 AA.
AC   A0A0J9UBD6; A0A0D2XAQ9; A0A0J9U886; A0A0J9U8U0; A0A0J9WGP4;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   03-AUG-2022, entry version 21.
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:23106229}; ORFNames=FOXG_00975;
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
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   [2]
RP   IDENTIFICATION.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RG   EnsemblFungi;
RL   Submitted (MAR-2015) to UniProtKB.
RN   [3]
RP   IDENTIFICATION IN THE VELVET COMPLEX, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23106229; DOI=10.1111/mmi.12082;
RA   Lopez-Berges M.S., Hera C., Sulyok M., Schaefer K., Capilla J., Guarro J.,
RA   Di Pietro A.;
RT   "The velvet complex governs mycotoxin production and virulence of Fusarium
RT   oxysporum on plant and mammalian hosts.";
RL   Mol. Microbiol. 87:49-65(2013).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24240057; DOI=10.1016/j.fgb.2013.11.002;
RA   Lopez-Berges M.S., Schaefer K., Hera C., Di Pietro A.;
RT   "Combinatorial function of velvet and AreA in transcriptional regulation of
RT   nitrate utilization and secondary metabolism.";
RL   Fungal Genet. Biol. 62:78-84(2014).
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:23106229). Controls the biosynthetic gene cluster
CC       for beauvericin, a depsipeptide mycotoxin that functions as a virulence
CC       determinant (PubMed:23106229). The velvet complex regulates also
CC       chromatin structure and transcription of siderophore biosynthetic genes
CC       and is required for infection of tomato plants (PubMed:23106229). The
CC       velvet complex also governs expression of nitrate metabolism genes
CC       (PubMed:24240057). {ECO:0000250|UniProtKB:C8VQG9,
CC       ECO:0000269|PubMed:23106229, ECO:0000269|PubMed:24240057}.
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, veA and velB; VeA acting as a bridging protein between laeA and
CC       velB (PubMed:23106229). {ECO:0000269|PubMed:23106229}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- DISRUPTION PHENOTYPE: Impairs production of beauvericin and attenuates
CC       virulence during infection of tomato plants (PubMed:23106229). Impairs
CC       also growth on the non-preferred nitrogen sources nitrate and nitrite
CC       (PubMed:24240057). {ECO:0000269|PubMed:23106229,
CC       ECO:0000269|PubMed:24240057}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=KNA95386.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=KNA95387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=KNA95388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=KNA95389.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS231696; KNA95390.1; -; Genomic_DNA.
DR   EMBL; DS231696; KNA95386.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DS231696; KNA95387.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DS231696; KNA95389.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DS231696; KNA95388.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_018233432.1; XM_018377671.1.
DR   RefSeq; XP_018233433.1; XM_018377672.1.
DR   RefSeq; XP_018233434.1; XM_018377673.1.
DR   RefSeq; XP_018233435.1; XM_018377674.1.
DR   RefSeq; XP_018233436.1; XM_018377675.1.
DR   AlphaFoldDB; A0A0J9UBD6; -.
DR   SMR; A0A0J9UBD6; -.
DR   EnsemblFungi; KNA95386; KNA95386; FOXG_00975.
DR   EnsemblFungi; KNA95387; KNA95387; FOXG_00975.
DR   EnsemblFungi; KNA95388; KNA95388; FOXG_00975.
DR   EnsemblFungi; KNA95389; KNA95389; FOXG_00975.
DR   EnsemblFungi; KNA95390; KNA95390; FOXG_00975.
DR   GeneID; 28943257; -.
DR   KEGG; fox:FOXG_00975; -.
DR   VEuPathDB; FungiDB:FOXG_00975; -.
DR   Proteomes; UP000009097; Unplaced.
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   Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW   Sporulation; Transcription; Transcription regulation; Transferase;
KW   Virulence.
FT   CHAIN           1..316
FT                   /note="Secondary metabolism regulator laeA"
FT                   /id="PRO_0000435752"
SQ   SEQUENCE   316 AA;  36726 MW;  B31FF99C55701147 CRC64;
     MVVMPPQNSV NESEGRYLQD GFWQHGRFYG SWKPGKYLFP IDSEELNRLD IFHKVFLLAR
     DNKPFLAPIR RPSPRIMDIG TGTGIWAINV AEECLSDAQI MAVDLNQIQP ALIPPGFMPK
     QYDIEEPSWG PLLTDCDLIH MRMLLGSIQT DLWPQVYHNV FEHLTPGIGF FEHIEVDWIP
     RCDDDERPAN SAFVKWAELF LDGMDRFNRS VRVTPQEHRQ MLEAAGFTDI RQEVIKAYVC
     PWSADRNERE IARWFNIGLS HSLEAMSLKP LIEKLGFEAE EVRELCERAK RETCVLRYHT
     YCNIHVWTAR KPGPQQ