EFM2_YEAST
ID EFM2_YEAST Reviewed; 419 AA.
AC P38347; D6VQR7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein-lysine N-methyltransferase EFM2 {ECO:0000305|PubMed:22522802};
DE EC=2.1.1.- {ECO:0000269|PubMed:21858014, ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354};
DE AltName: Full=Elongation factor methyltransferase 2 {ECO:0000303|PubMed:22522802};
GN Name=EFM2 {ECO:0000303|PubMed:22522802};
GN OrderedLocusNames=YBR271W {ECO:0000312|SGD:S000000475}; ORFNames=YBR1739;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21858014; DOI=10.1371/journal.pone.0023168;
RA Wlodarski T., Kutner J., Towpik J., Knizewski L., Rychlewski L.,
RA Kudlicki A., Rowicka M., Dziembowski A., Ginalski K.;
RT "Comprehensive structural and substrate specificity classification of the
RT Saccharomyces cerevisiae methyltransferome.";
RL PLoS ONE 6:E23168-E23168(2011).
RN [8]
RP FUNCTION.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [9]
RP FUNCTION.
RX PubMed=24517342; DOI=10.1021/pr401251k;
RA Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.;
RT "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights
RT into non-histone protein lysine methyltransferase activity.";
RL J. Proteome Res. 13:1744-1756(2014).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25086354; DOI=10.1016/j.bbrc.2014.07.110;
RA Zhang L., Hamey J.J., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Elongation factor methyltransferase 3 - A novel eukaryotic lysine
RT methyltransferase.";
RL Biochem. Biophys. Res. Commun. 451:229-234(2014).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=25231983; DOI=10.1074/jbc.m114.605527;
RA Dzialo M.C., Travaglini K.J., Shen S., Roy K., Chanfreau G.F., Loo J.A.,
RA Clarke S.G.;
RT "Translational roles of elongation factor 2 protein lysine methylation.";
RL J. Biol. Chem. 289:30511-30524(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that mono- and dimethylates elongation factor 2
CC (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).
CC {ECO:0000269|PubMed:21858014, ECO:0000269|PubMed:22522802,
CC ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Increases sensitivity to antibiotics that target
CC translation and decreases translational fidelity.
CC {ECO:0000269|PubMed:25231983}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. METTL21 family. {ECO:0000305}.
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DR EMBL; Z36140; CAA85234.1; -; Genomic_DNA.
DR EMBL; AY692663; AAT92682.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07387.1; -; Genomic_DNA.
DR PIR; S46152; S46152.
DR RefSeq; NP_009830.3; NM_001178619.3.
DR AlphaFoldDB; P38347; -.
DR SMR; P38347; -.
DR BioGRID; 32966; 26.
DR DIP; DIP-5051N; -.
DR IntAct; P38347; 1.
DR STRING; 4932.YBR271W; -.
DR iPTMnet; P38347; -.
DR MaxQB; P38347; -.
DR PaxDb; P38347; -.
DR PRIDE; P38347; -.
DR EnsemblFungi; YBR271W_mRNA; YBR271W; YBR271W.
DR GeneID; 852574; -.
DR KEGG; sce:YBR271W; -.
DR SGD; S000000475; EFM2.
DR VEuPathDB; FungiDB:YBR271W; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00510000048008; -.
DR HOGENOM; CLU_049351_1_0_1; -.
DR InParanoid; P38347; -.
DR OMA; DDFGEMK; -.
DR BioCyc; YEAST:G3O-29192-MON; -.
DR PRO; PR:P38347; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38347; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..419
FT /note="Protein-lysine N-methyltransferase EFM2"
FT /id="PRO_0000202531"
FT BINDING 222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 261..263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 340
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ SEQUENCE 419 AA; 47977 MW; E15B739CB94BE4A2 CRC64;
MFDPLDLYTP DDIQVEALQF NLAEREPKDP CSPQRDEILT AVDEEESDDD DTIIDNLDLP
SVKYAPPEVI LCILILLKPD RQVNFNQETG KNKSVLEVCK SHGLEPDLLK RLLTWYTEEW
PNKRLNSLEK ICNKIPMLRF TVSKELLLGY YTSVLKKYNN SCGLNEEIIQ ELLKELSSRI
SENCGRTAQP SIVRYFELRN LSTSIPLHEP SLTADNLGWK TWGSSLILSQ LVVDHLDYLH
TTNVNMLANS DIKQIKVLEL GAGTGLVGLS WALKWKELYG TENIEIFVTD LPEIVTNLKK
NVSLNNLGDF VQAEILDWTN PHDFIDKFGH ENEFDVILIA DPIYSPQHPE WVVNMISKFL
AASGTCHLEI PLRAKYAKER EVLKLLLKES DLKVVEERHS EGVDDWGAVK YLYRQIVRN
