ID   LAEA_EMEND              Reviewed;         374 AA.
AC   Q6TLK5;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
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:15075281};
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=162425 {ECO:0000312|EMBL:AAQ95166.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   INDUCTION.
RC   STRAIN=TJH3.40;
RX   PubMed=15075281; DOI=10.1128/ec.3.2.527-535.2004;
RA   Bok J.W., Keller N.P.;
RT   "LaeA, a regulator of secondary metabolism in Aspergillus spp.";
RL   Eukaryot. Cell 3:527-535(2004).
CC   -!- FUNCTION: Methyltransferase that performs automethylation at Met-207
CC       (By similarity). No other methyl-accepting substrate has been
CC       identified yet (By similarity). Component of the velvet transcription
CC       factor complex that acts as a global regulator for secondary metabolite
CC       gene expression (PubMed:15075281). Controls the expression of the
CC       sterigmatocystin, penicillin, and lovastatin gene clusters
CC       (PubMed:15075281). Controls light-dependent formation of the velB-vosA
CC       complex, veA protein modification, and is required for light-mediated
CC       inhibition of sexual development (By similarity). Within the velvet
CC       complex, controls light-dependent secondary metabolism (By similarity).
CC       Involved in the defense response against Drosophila melanogaster larval
CC       grazing (By similarity). {ECO:0000250|UniProtKB:C8VQG9,
CC       ECO:0000269|PubMed:15075281}.
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 (By similarity). {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- INDUCTION: Expression is negatively regulated by the transcription
CC       factor AflR, as well as by two signal transduction elements, protein
CC       kinase A and RasA. {ECO:0000269|PubMed:15075281}.
CC   -!- PTM: Self-methylates at Met-207. {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- DISRUPTION PHENOTYPE: Reduces secondary metabolite production,
CC       including sterigmatocystin, a carcinogen biochemically related to the
CC       agricultural contaminant aflatoxin (PubMed:15075281).
CC       {ECO:0000269|PubMed:15075281}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; AY394722; AAQ95166.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6TLK5; -.
DR   SMR; Q6TLK5; -.
DR   OMA; KNCDFYA; -.
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   2: Evidence at transcript level;
KW   Methylation; Methyltransferase; Nucleus; S-adenosyl-L-methionine;
KW   Sporulation; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..374
FT                   /note="Secondary metabolism regulator laeA"
FT                   /id="PRO_0000435742"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         207
FT                   /note="S-methylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:C8VQG9"
SQ   SEQUENCE   374 AA;  42965 MW;  89C49642CF984B32 CRC64;
     MFEMGPVGTR LPAMTSPAHN HYSYHSPTSS DRGRSRQNSD AMDIQSITER EPATRYAVAG
     GPAPWNRNGS PSMSPMYSNN SERNQFHEEN GRTYHGFRRG MYFLPCDEQE QDRLDIFHKL
     FTVARVSESL IYAPHPTNGR FLDLGCGTGI WAIEVANKYP DAFVAGVDLA PIQPPNHPKN
     CEFYAPFDFE APWAMGEDSW DLIHLQMGCG SVMGWPNLYR RIFAHLRPGA WFEQVEIDFE
     PRCDDRSLDG TALRHWYDCL KQATAETMRP IAHSSRDTIK DLQDAGFTEI DHQIVGLPLN
     PWHQDEHERK VARWYNLAVS ESIENLSLAP FSRVYRWPLE RIQQLAADVK SEAFNKEIHA
     YNILHIYQAR KPLR