LAEA_ASPNA
ID LAEA_ASPNA Reviewed; 375 AA.
AC G3XRG4;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
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:26566947}; ORFNames=ASPNIDRAFT_170198;
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC 328 / USDA 3528.7;
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26566947; DOI=10.1534/g3.115.024067;
RA Niu J., Arentshorst M., Nair P.D., Dai Z., Baker S.E., Frisvad J.C.,
RA Nielsen K.F., Punt P.J., Ram A.F.;
RT "Identification of a classical mutant in the industrial host Aspergillus
RT niger by systems genetics: laeA is required for citric acid production and
RT regulates the formation of some secondary metabolites.";
RL G3 (Bethesda) 6:193-204(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:26566947). Controls the expression of the citric
CC acid, demethylkotanin, orlandin, asperrubrol, tensidol B, atromentin
CC and JBIR8 gene clusters (PubMed:26566947). Represses also the
CC expression of genes related to the production of BMS-192548 and
CC aspernigrin A (PubMed:26566947). {ECO:0000250|UniProtKB:C8VQG9,
CC ECO:0000269|PubMed:26566947}.
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 -!- DISRUPTION PHENOTYPE: Results in a complete absence of citrate
CC production (PubMed:26566947). {ECO:0000269|PubMed:26566947}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; ACJE01000004; EHA27020.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XRG4; -.
DR SMR; G3XRG4; -.
DR STRING; 380704.G3XRG4; -.
DR EnsemblFungi; EHA27020; EHA27020; ASPNIDRAFT_170198.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_170198; -.
DR HOGENOM; CLU_010595_2_0_1; -.
DR Proteomes; UP000009038; 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 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Sporulation; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..375
FT /note="Secondary metabolism regulator laeA"
FT /id="PRO_0000435746"
FT REGION 15..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 43361 MW; 96B95D2B530B1811 CRC64;
MFEISRLLHQ PITMASPNRN NYSYQGIESY DSGRSRQNSD AMDIHVITAQ EPPREPPDNN
DPYDGHGGPA GTSHYSKPPN RWLFYEENGR TYHGYRRGVY PLPCDEQEQD RLDIFHKLFT
VARMSESLIY APHPPNGRFL DLGCGTGIWA IDVAHKYPNA FVAGVDLAPI QPPNHPDNCE
FYAPFDFEAP WTLGENSWDL IHLQMGCGSV LGWQNLYKRI LRHLQPGAWF EQVEIDFEPR
CDDRSLNGLA LREWYQYLKQ ATQDTMRPIA HSSRDTIRHL EEAGFTQIDH QMVGLPLNPW
HRDEHEQKVA RWYNLAISES IETLSLAPFS RIFHWDLDRI RQITAEVKSQ AFNKEIHAYN
ILHIYQARKP GGPSL
