ID   LAEA_COCH5              Reviewed;         307 AA.
AC   M2SNN6; G4XKY9;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
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:22383877}; ORFNames=COCHEDRAFT_1197809;
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C5 / ATCC 48332 / race O;
RX   PubMed=22383877; DOI=10.1371/journal.ppat.1002542;
RA   Wu D., Oide S., Zhang N., Choi M.Y., Turgeon B.G.;
RT   "ChLae1 and ChVel1 regulate T-toxin production, virulence, oxidative stress
RT   response, and development of the maize pathogen Cochliobolus
RT   heterostrophus.";
RL   PLoS Pathog. 8:E1002542-E1002542(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000312|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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 (By similarity). Controls the expression of the T-toxin gene
CC       cluster (PubMed:22383877). Promotes oxidative stress tolerance and acts
CC       as a virulence factors during infection (PubMed:22383877). Negatively
CC       regulate mycelial pigmentation and controls sexual development, as well
CC       as asexual development during vegetative growth (PubMed:22383877).
CC       {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:22383877}.
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 hypersensitivity to oxidative stress,
CC       compromised reproductive development, repression of asexual
CC       sporulation, and reduction of virulence during maize infection
CC       (PubMed:22383877). {ECO:0000269|PubMed:22383877}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEP40318.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JF826792; AEP40318.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; KB445583; EMD86920.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2SNN6; -.
DR   SMR; M2SNN6; -.
DR   STRING; 701091.M2SNN6; -.
DR   EnsemblFungi; EMD86920; EMD86920; COCHEDRAFT_1197809.
DR   eggNOG; ENOG502QQMC; Eukaryota.
DR   HOGENOM; CLU_010595_2_0_1; -.
DR   OMA; KNCDFYA; -.
DR   PHI-base; PHI:2315; -.
DR   Proteomes; UP000016936; 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;
KW   Virulence.
FT   CHAIN           1..307
FT                   /note="Secondary metabolism regulator LAE1"
FT                   /id="PRO_0000435748"
SQ   SEQUENCE   307 AA;  36056 MW;  BD0188BF582D9870 CRC64;
     MTSNGLPVPA QNSNYMENGR WYHGFRRGLY MYPCDEPEKD RMDIYHQFFA VARRGQLHQA
     PVPSEPHLQP RILDVGCGTG IWAIDMADKY LNAEVLGLDL VNIQPEKIPP NLRFRVPRDY
     ESPWTLGEDS WDLIHLRMAC GSVESWPELY QKIYTHLKPG TGWIEHIEID MEPRCDDYTL
     PPDSMLRKWY GWLADATQRA YRPIAYEHRT RQLLQAAGFI DIQETVIRVP YNTWPNDPHQ
     KDIGRWYNLG LTEGLEALTF APLTRVYHWD LNAHVRPIVE GVRRELCNRK IHAYNNIHIW
     TARRPQQ