ID   LAEA_BOTFB              Reviewed;         327 AA.
AC   A0A0B5L7R4;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 17.
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:25625818};
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   IDENTIFICATION IN THE VELVET COMPLEX.
RC   STRAIN=B05.10;
RX   PubMed=25625818; DOI=10.1094/mpmi-12-14-0411-r;
RA   Schumacher J., Simon A., Cohrs K.C., Traeger S., Porquier A., Dalmais B.,
RA   Viaud M., Tudzynski B.;
RT   "The VELVET complex in the gray mold fungus Botrytis cinerea: impact of
RT   BcLAE1 on differentiation, secondary metabolism, and virulence.";
RL   Mol. Plant Microbe Interact. 28:659-674(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:25625818). Controls the expression of the oxalic
CC       acid gene cluster (PubMed:25625818). Controls also the expression of
CC       proteases and carbohydrate-active enzymes (PubMed:25625818). Regulates
CC       sclerotia formation and plays a role in virulence (PubMed:25625818).
CC       {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:25625818}.
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 (PubMed:25625818). {ECO:0000269|PubMed:25625818}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the ability to produce oxalic acid, to
CC       colonize the host tissue, and to form sclerotia (PubMed:25625818).
CC       {ECO:0000269|PubMed:25625818}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; KP099423; AJG44853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5L7R4; -.
DR   VEuPathDB; FungiDB:Bcin05g01210; -.
DR   OrthoDB; 1047281at2759; -.
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..327
FT                   /note="Secondary metabolism regulator LAE1"
FT                   /id="PRO_0000435756"
SQ   SEQUENCE   327 AA;  37600 MW;  C3A85ED871908176 CRC64;
     MVVAMAMANN GSLSPAPPAA FQEPPPDYTE NGRLYHGLHK GKYMFPCDED EKDRMDIFHK
     FFEVAMGGVL HSRNTTFTNN YDGPRILDLG TGTGIWAIDM ADKYGSDMGT GEVLGLDLAR
     IQPPTIPENL QFLQRDIESP WWGLEVESWD MVHIRMLSGS INSWPALYQK VRRYLKPQVG
     RFEQVEIDFT PRSDFGDIPA DSALATWARN LFEATRRNFR PLAYNTEIRA MLQKEEFLDI
     QEEVIRIPLN PWPDDPQEKD VARWYNLALT QGLEAMTLGP MHRIYGWTKD DVTRLITEVR
     RDICNRKIRA YNNLHVWTAR APVKPPS