ID LAEA_GIBF5 Reviewed; 316 AA. AC S0DQI7; E0WDF6; DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot. DT 16-MAR-2016, sequence version 2. DT 08-NOV-2023, entry version 32. 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:20572938}; ORFNames=FFUJ_00592; OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae OS and foot rot disease fungus) (Fusarium fujikuroi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium fujikuroi species complex. OX NCBI_TaxID=1279085; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION, RP INTERACTION WITH VEL1/VEA, AND DISRUPTION PHENOTYPE. RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831; RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x; RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U., RA Tudzynski B.; RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium RT fujikuroi, affect differentiation, secondary metabolism and virulence."; RL Mol. Microbiol. 77:972-994(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831; RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475; RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M., RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D., RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T., RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W., RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U., RA Tudzynski B.; RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and RT novel metabolites."; RL PLoS Pathog. 9:E1003475-E1003475(2013). RN [3] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=24389666; DOI=10.1007/s00253-013-5453-1; RA Niehaus E.M., von Bargen K.W., Espino J.J., Pfannmueller A., Humpf H.U., RA Tudzynski B.; RT "Characterization of the fusaric acid gene cluster in Fusarium fujikuroi."; RL Appl. Microbiol. Biotechnol. 98:1749-1762(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:20572938). Controls the expression of the CC gibberellins gene clusters, but does not affect bikaverin production CC (PubMed:20572938). Controls the expression of the fusaric acid gene CC cluster (PubMed:24389666). Acts as a virulence factors during CC infection, most likely through activation of gibberellins biosynthesis CC (PubMed:20572938). {ECO:0000250|UniProtKB:C8VQG9, CC ECO:0000269|PubMed:20572938, ECO:0000269|PubMed:24389666}. 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:20572938). CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:20572938}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20572938}. CC -!- INDUCTION: Expression is regulated by the VEL1 (PubMed:20572938). CC {ECO:0000269|PubMed:20572938}. CC -!- DISRUPTION PHENOTYPE: Reduces gibberellins production and subsequent CC virulence during infection (PubMed:20572938). Reduces both the fusaric CC acid gene cluster expression and production of fusaric acid CC (PubMed:24389666). {ECO:0000269|PubMed:20572938, CC ECO:0000269|PubMed:24389666}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA CC methyltransferase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CCT62818.1; 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; FN548141; CBE54370.1; -; Genomic_DNA. DR EMBL; HF679023; CCT62818.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; S0DQI7; -. DR SMR; S0DQI7; -. DR STRING; 1279085.S0DQI7; -. DR EnsemblFungi; CCT62818; CCT62818; FFUJ_00592. DR HOGENOM; CLU_010595_2_0_1; -. DR OrthoDB; 2241530at2759; -. DR Proteomes; UP000016800; Chromosome 1. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro. 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 CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR Pfam; PF13489; Methyltransf_23; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 1: Evidence at protein level; KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine; KW Sporulation; Transcription; Transcription regulation; Transferase; KW Virulence. FT CHAIN 1..316 FT /note="Secondary metabolism regulator LAE1" FT /id="PRO_0000435749" SQ SEQUENCE 316 AA; 36624 MW; 4657FCFE4FFDB2DA CRC64; MVVMPPQNSV NESEGRYLQD GFWQHGRFYG SWKPGKYLFP IDSEELNRLD IFHKVFLLAR DNKPFLAPIR RTSPRIMDIG TGTGIWAINV AEECLSDAQI MAVDLNQIQP ALIPPGFMPK QYDIEEPSWG PLLADCDLIH MRMLLGSIQT DLWPQVYHNA FEHLTPGIGF LEHIEVDWIP RCDDDERPAN SAFVKWAELF LDGMDRFNRS VRVIPQEHRQ MLEATGFTDV KQEVIKAYVC PWSADRNERE IARWFNIGLS HSLEAMSLKP LIEKLGFEAE DVRELCERAK RETCVLRYHT YCNIHVWTAR KPGPQQ //