ID   LAEA_MONPI              Reviewed;         367 AA.
AC   A2SUH3;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 34.
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:19368389};
OS   Monascus pilosus (Red mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Monascus.
OX   NCBI_TaxID=89488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE, AND
RP   FUNCTION.
RC   STRAIN=IFO4520;
RX   PubMed=19368389; DOI=10.1021/jf9004109;
RA   Zhang M.Y., Miyake T.;
RT   "Development and media regulate alternative splicing of a methyltransferase
RT   pre-mRNA in Monascus pilosus.";
RL   J. Agric. Food Chem. 57:4162-4167(2009).
RN   [2]
RP   FUNCTION.
RX   PubMed=23727802; DOI=10.4014/jmb.1303.03026;
RA   Lee S.S., Lee J.H., Lee I.;
RT   "Strain improvement by overexpression of the laeA gene in Monascus pilosus
RT   for the production of monascus-fermented rice.";
RL   J. Microbiol. Biotechnol. 23:959-965(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:23727802). Controls the expression of the monacolin
CC       K gene clusters (PubMed:19368389, PubMed:23727802). Regulates also
CC       pigmentation (PubMed:23727802). {ECO:0000250|UniProtKB:C8VQG9,
CC       ECO:0000269|PubMed:19368389, ECO:0000269|PubMed:23727802}.
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: Alternative splicing of the pre-mRNA occurs in the 5'-
CC       untranslated region (5'-UTR) (PubMed:19368389). The shorter mRNA is
CC       constitutive transcript at all growth stages and different carbon or
CC       nitrogen sources, but the glutamate and NaNO(3) as main nitrogen source
CC       can up-regulate the longer mRNA form (PubMed:19368389). The longer mRNA
CC       is probably not translated (PubMed:19368389).
CC       {ECO:0000269|PubMed:19368389}.
CC   -!- DISRUPTION PHENOTYPE: Decreases synthesis of monacolin K
CC       (PubMed:19368389). {ECO:0000269|PubMed:19368389}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; DQ178028; ABA87010.1; -; Genomic_DNA.
DR   EMBL; DQ178028; ABA87011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2SUH3; -.
DR   SMR; A2SUH3; -.
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   Methyltransferase; Nucleus; S-adenosyl-L-methionine; Sporulation;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..367
FT                   /note="Secondary metabolism regulator laeA"
FT                   /id="PRO_0000435758"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  42085 MW;  1DD7FE6C2CD5509D CRC64;
     MFGQQQQQQP PPPAASAYLN HNSRWTPPNE SAQPRRSSNA MDINAITDRD PAEGHPRSNH
     TSSSIGSPID KSPETYPGHE ENGRIYHGFR RGIYFLPCDD LEQDRLDIFH KVITVARVSD
     ALIYSPHPRN GRFLDLGCGT GIWAIDVAQK YPDAFVVGVD LSPIQPLNSP RNCDFYAPFD
     FESPWALGED SWDLIHMQLG CGSVVSWPSL YRRIFAHLRP GAWFEQVEID FEPRCDDRSL
     EGLALHHWYQ CLKQATEEAM RPLAHNPRET IRHLQEAGFT EIDHQIVGLP LNPWHQDEHE
     KTVARWYNLA ICESIETFSL APFTRFFGWP VDRIKRLVAD VRSEAFNKDI HAYNILHIYQ
     ARKPISN