LAEA_HYPJQ
ID LAEA_HYPJQ Reviewed; 332 AA.
AC G0RNN3; I3RU94; R9QQS2;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Secondary metabolism regulator LAE1 {ECO:0000305};
DE AltName: Full=Methyltransferase LAE1 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:C8VQG9};
DE AltName: Full=Velvet complex subunit LAE1 {ECO:0000305};
GN Name=LAE1 {ECO:0000303|PubMed:22554051}; ORFNames=TRIREDRAFT_41617;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=QM6a;
RX PubMed=22554051; DOI=10.1111/j.1365-2958.2012.08083.x;
RA Seiboth B., Karimi R.A., Phatale P.A., Linke R., Hartl L., Sauer D.G.,
RA Smith K.M., Baker S.E., Freitag M., Kubicek C.P.;
RT "The putative protein methyltransferase LAE1 controls cellulase gene
RT expression in Trichoderma reesei.";
RL Mol. Microbiol. 84:1150-1164(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND INTERACTION
RP WITH VEL1/VEA.
RC STRAIN=QM6a;
RX PubMed=23390613; DOI=10.1534/g3.112.005140;
RA Karimi-Aghcheh R., Bok J.W., Phatale P.A., Smith K.M., Baker S.E.,
RA Lichius A., Omann M., Zeilinger S., Seiboth B., Rhee C., Keller N.P.,
RA Freitag M., Kubicek C.P.;
RT "Functional analyses of Trichoderma reesei LAE1 reveal conserved and
RT contrasting roles of this regulator.";
RL G3 (Bethesda) 3:369-378(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 44-310.
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24909838; DOI=10.1186/1471-2164-15-447;
RA Fekete E., Karaffa L., Karimi Aghcheh R., Nemeth Z., Fekete E., Orosz A.,
RA Paholcsek M., Stagel A., Kubicek C.P.;
RT "The transcriptome of lae1 mutants of Trichoderma reesei cultivated at
RT constant growth rates reveals new targets of LAE1 function.";
RL BMC Genomics 15:447-447(2014).
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:23390613, PubMed:24909838). Required for the
CC expression of VEL1 (PubMed:23390613). Regulates expression of the
CC carbohydrate-active enzyme gene clusters, but does not act by directly
CC modulating H3K4 or H3K9 methylation (PubMed:22554051). Required for
CC conidiation (PubMed:22554051). {ECO:0000250|UniProtKB:C8VQG9,
CC ECO:0000269|PubMed:22554051, ECO:0000269|PubMed:24909838}.
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 LAE1, VEL1 and VEL2; VEL1 acting as a bridging protein between LAE1 and
CC VEL2 (By similarity). Interacts with VEL1 (PubMed:23390613).
CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:23390613}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC -!- INDUCTION: Expression is negatively regulated by protein kinase A
CC (PubMed:23390613). {ECO:0000269|PubMed:23390613}.
CC -!- DISRUPTION PHENOTYPE: Leads to a complete loss of expression of all
CC seven cellulases, auxiliary factors for cellulose degradation, beta-
CC glucosidases and xylanases. Affects also the expression of 50% of the
CC GCN5-related N-acetyltransferases (GNATs) present in the genome
CC (PubMed:24909838). {ECO:0000269|PubMed:22554051,
CC ECO:0000269|PubMed:24909838}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFX86442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EGR47184.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JN791097; AFK30952.1; -; Genomic_DNA.
DR EMBL; JX841312; AFX86442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; GL985069; EGR47184.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006966726.1; XM_006966664.1.
DR AlphaFoldDB; G0RNN3; -.
DR STRING; 431241.G0RNN3; -.
DR EnsemblFungi; EGR47184; EGR47184; TRIREDRAFT_41617.
DR GeneID; 18484840; -.
DR KEGG; tre:TRIREDRAFT_41617; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_41617; -.
DR HOGENOM; CLU_010595_2_0_1; -.
DR Proteomes; UP000008984; 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; Reference proteome; S-adenosyl-L-methionine;
KW Sporulation; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..332
FT /note="Secondary metabolism regulator LAE1"
FT /id="PRO_0000435753"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 38405 MW; 61CD58CE622C4B0C CRC64;
MSRNAPNGCV PPSQATAPPS PATSLRLTVG EPVSEPATES GERVLQDGFW EHGRFYGSWK
PGKYLFPIDK EELNRLDVFH KYFLVARDEK VTSTPLRKDG RPKIMDLGTG TGIWAYNVVE
EYAKDAEIMA VDLNQIQPAL IPRGVTTKQF DIEEPSWDPL LRDCELIHMR LLYGSIRDDK
WPHVYRKAFE HLAPGIGYIE QLEIDWMPRW ENEDLPRHSA LQEWAQLFQR AMHRYHRSVT
VSGEATRRRM EAAGFTDFSE TTIRCYVNPW SPDRHQRECA RWFNLAFSLG LEAMSMMPMI
DKLGMTKDDI VDLCSRAKKE MCILRYRAYC TL
