ID   LAEA_HYPAT              Reviewed;         349 AA.
AC   T1T504;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
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:23826217};
OS   Hypocrea atroviridis (Trichoderma atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=63577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RC   STRAIN=P1 / ATCC 74058;
RX   PubMed=23826217; DOI=10.1371/journal.pone.0067144;
RA   Karimi Aghcheh R., Druzhinina I.S., Kubicek C.P.;
RT   "The putative protein methyltransferase LAE1 of Trichoderma atroviride is a
RT   key regulator of asexual development and mycoparasitism.";
RL   PLoS ONE 8:E67144-E67144(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:23826217). Controls the expression of the gamma-
CC       pentyl-pyrone gene clusters (PubMed:23826217). Required for the
CC       expression of cellulase (PubMed:23826217). Regulates asexual
CC       sporulation (conidiation) by environmental stimuli such as light and/or
CC       mechanical injury (PubMed:23826217). Required for oxidative stress
CC       tolerance (PubMed:23826217). Also plays a role in defense and
CC       parasitism on other fungi (PubMed:23826217).
CC       {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:23826217}.
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). {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- DISRUPTION PHENOTYPE: Leads to reduced growth rate on plates with D-
CC       glucose or D-galactose, decreases the expression of mycoparasitism-
CC       associated genes, and impairs conidiation (PubMed:23826217).
CC       {ECO:0000269|PubMed:23826217}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; KC174792; AGT59504.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1T504; -.
DR   SMR; T1T504; -.
DR   OMA; KNCDFYA; -.
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; Virulence.
FT   CHAIN           1..349
FT                   /note="Secondary metabolism regulator LAE1"
FT                   /id="PRO_0000435754"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  40063 MW;  93780C930DDB1441 CRC64;
     MSSRNAPSGC VAPSPATAAP PSPTNLRLTV GQSGSESANE PGGEPEERIL QDGFWEYGRF
     YGNWKKGKYN FPIDKEETSR LDILHKYFIV ETEDRVTSVP LDKEGSPKIM DLGTGTGIWA
     FHVVEGYIPN AQIMAVDLNQ IQPALIPRGV TTKQFDLEEP SWEPLLRDCD LIHLRLLYGS
     IRDDLWADTY RKIFEHLAPG GYVEHLEIDW TPQWDGEDHP THSAIREWSQ QFHRAMHRYR
     RSVKVSSEDT KRMMEAAGFT EFKETKIRCY LNPWSTDRHQ REAARWFNLA LGLGLEAMSL
     MPMIDMLHMK QEDVVDLCKR VKAETCVLRY HAYFTLHTWT AKKPASPPQ