ID   LAEA_ASPFS              Reviewed;         373 AA.
AC   A0A0H4LJX8;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   03-AUG-2022, entry version 16.
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:26466873};
OS   Aspergillus fumisynnematus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=286432;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=F746;
RX   PubMed=26466873; DOI=10.1016/j.funbio.2015.06.006;
RA   Hong E.J., Kim N.K., Lee D., Kim W.G., Lee I.;
RT   "Overexpression of the laeA gene leads to increased production of
RT   cyclopiazonic acid in Aspergillus fumisynnematus.";
RL   Fungal Biol. 119:973-983(2015).
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:26466873). Controls the expression of the
CC       cyclopiazonic acid (CPA) gene clusters (PubMed:26466873). Regulates
CC       also pigmentation and conidial head morphology (PubMed:26466873).
CC       {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:26466873}.
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   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; KP769770; AKP07636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H4LJX8; -.
DR   SMR; A0A0H4LJX8; -.
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   3: Inferred from homology;
KW   Methyltransferase; Nucleus; S-adenosyl-L-methionine; Sporulation;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..373
FT                   /note="Secondary metabolism regulator laeA"
FT                   /id="PRO_0000435757"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  42548 MW;  EA9DFC5B162C54D2 CRC64;
     MFLNGQGGQR PPTVASPPLN VRGSISSDFN ALGRSRNNSD AMDIYTITDR GPAAERDPAA
     GRWHANGSPS INSTSSKNPD RYPCYQENGR TYHGYRKGIY MLPCDEQEQD RLDIFHKLFT
     VARVSDGLIY APHPTNGRFL DLGCGTGIWA IDVANKYPEA FVVGVDLAPI QPPNHPRNCD
     FYAPFDFESL WALGEDSWDL IHMQMGSGSV ASWPNLYRRI YSHLRPGAWF EQVEIDFEPR
     CDDRSLEGLA IRQWYQLLKQ ATEETMRPVA HNSRETIRNL QEAGFTEIDH QMVGLPLNPW
     HQDEHERRVA RWYNLAISES IETMSLAPFS RVFGWPIERI KQIAADVKSE AFNKEIHTYN
     ILHIYQARKP LAN