LAEA_ASPFN
ID LAEA_ASPFN Reviewed; 369 AA.
AC B8N406; Q2KNE4;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 57.
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:18667168}; ORFNames=AFLA_033290;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RA Wilkinson J.R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18667168; DOI=10.1016/j.fgb.2008.06.009;
RA Kale S.P., Milde L., Trapp M.K., Frisvad J.C., Keller N.P., Bok J.W.;
RT "Requirement of LaeA for secondary metabolism and sclerotial production in
RT Aspergillus flavus.";
RL Fungal Genet. Biol. 45:1422-1429(2008).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=19411623; DOI=10.1128/ec.00088-09;
RA Amaike S., Keller N.P.;
RT "Distinct roles for VeA and LaeA in development and pathogenesis of
RT Aspergillus flavus.";
RL Eukaryot. Cell 8:1051-1060(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22289775; DOI=10.1016/j.funbio.2011.12.003;
RA Chang P.K., Scharfenstein L.L., Ehrlich K.C., Wei Q., Bhatnagar D.,
RA Ingber B.F.;
RT "Effects of laeA deletion on Aspergillus flavus conidial development and
RT hydrophobicity may contribute to loss of aflatoxin production.";
RL Fungal Biol. 116:298-307(2012).
RN [6]
RP IDENTIFICATION IN THE VELVET COMPLEX, AND INTERACTION WITH VEA.
RX PubMed=23994319; DOI=10.1016/j.fgb.2013.08.009;
RA Chang P.K., Scharfenstein L.L., Li P., Ehrlich K.C.;
RT "Aspergillus flavus VelB acts distinctly from VeA in conidiation and may
RT coordinate with FluG to modulate sclerotial production.";
RL Fungal Genet. Biol. 58:71-79(2013).
RN [7]
RP INDUCTION.
RX PubMed=23676908; DOI=10.4014/jmb.1301.01002;
RA Kim S.S., Kim Y.H., Shin K.S.;
RT "The developmental regulators, FlbB and FlbE, are involved in the virulence
RT of Aspergillus fumigatus.";
RL J. Microbiol. Biotechnol. 23:766-770(2013).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24040154; DOI=10.1371/journal.pone.0074030;
RA Amaike S., Affeldt K.J., Yin W.B., Franke S., Choithani A., Keller N.P.;
RT "The bZIP protein MeaB mediates virulence attributes in Aspergillus
RT flavus.";
RL PLoS ONE 8:E74030-E74030(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. Required for aflR expression and subsequent aflatoxin
CC production (PubMed:18667168, PubMed:19411623, PubMed:22289775,
CC PubMed:24040154). Regulates negatively veA expression (PubMed:18667168,
CC PubMed:19411623). Controls conidiophore and conidial development
CC (PubMed:22289775, PubMed:24040154). Required for hydrophobin production
CC which plays a role in cell surface hydrophobicity and host defense
CC escape (PubMed:22289775). {ECO:0000250|UniProtKB:C8VQG9,
CC ECO:0000269|PubMed:18667168, ECO:0000269|PubMed:19411623,
CC ECO:0000269|PubMed:22289775}.
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:23994319). Interacts directly with veA (PubMed:23994319).
CC {ECO:0000269|PubMed:23994319}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC -!- INDUCTION: Expression is regulated by the developmental regulators flbB
CC and flbE (PubMed:23676908). {ECO:0000269|PubMed:23676908}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased conidial production, loss of
CC sclerotia, and altered in host colonization (PubMed:18667168,
CC PubMed:19411623, PubMed:22289775, PubMed:24040154). Reduces expression
CC of hydrophobins rodA and rodB, resulting in a decrease of colony
CC hydrophobicity (PubMed:22289775). Impairs expression of aflR
CC (PubMed:19411623). Abolishes production of aflatoxin (PubMed:22289775,
CC PubMed:24040154). Leads to down-regulation of nitrate metabolic genes
CC (PubMed:24040154). Unables metabolization of host cell lipid reserves
CC and is inhibited by oleic acid in growth assays (PubMed:19411623).
CC {ECO:0000269|PubMed:18667168, ECO:0000269|PubMed:19411623,
CC ECO:0000269|PubMed:22289775, ECO:0000269|PubMed:24040154}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED56057.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY883016; AAX68412.1; -; Genomic_DNA.
DR EMBL; EQ963473; EED56057.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002374839.1; XM_002374798.1.
DR AlphaFoldDB; B8N406; -.
DR SMR; B8N406; -.
DR STRING; 5059.CADAFLAP00002704; -.
DR EnsemblFungi; EED56057; EED56057; AFLA_033290.
DR eggNOG; ENOG502QQMC; Eukaryota.
DR HOGENOM; CLU_010595_2_0_1; -.
DR PHI-base; PHI:3881; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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; S-adenosyl-L-methionine; Sporulation;
KW Transcription; Transcription regulation; Transferase; Virulence.
FT CHAIN 1..369
FT /note="Secondary metabolism regulator laeA"
FT /id="PRO_0000435744"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 42659 MW; 7BF49FBAACDB43B4 CRC64;
MFGNGQTGQR LPAMASPPHD SYYSQSLASS RSRNNSDAMD IYAITDRDPP AREPSGYSQW
YRNGSPSVNS IHSKSSEKQP FYEENGRMYH AYRKGVYMLP CDEQEQDRLD IFHKLFTVAR
VSDGLMYAPH PRNGRFLDLG CGTGIWAIDV ANKYPDAFVV GVDLAPIQPS NHPKNCEFYA
PFDFESPWAM GEDSWDLIHL QMGCGSVMGW PNLYRRIFAH LRPGAWFEQV EIDFEPRCDD
RPLEGLAIRQ WYQYLKQATQ DAMRPINHNS RDTIRDLQEA GFTDIDHQMV GLPLNPWHQD
EHERKVARWY NLAVSESIES LSMAPFSRIF NWDLDRIRRI SSEVKSEAFN KEIHAYNILH
IYQARKPAN
