EFM3_YEAST
ID EFM3_YEAST Reviewed; 339 AA.
AC P47163; D6VWU7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein-lysine N-methyltransferase EFM3 {ECO:0000305|PubMed:25086354};
DE EC=2.1.1.- {ECO:0000269|PubMed:25086354, ECO:0000269|PubMed:25231979};
DE AltName: Full=Elongation factor methyltransferase 3 {ECO:0000303|PubMed:25086354};
GN Name=EFM3 {ECO:0000303|PubMed:25086354};
GN OrderedLocusNames=YJR129C {ECO:0000312|SGD:S000003890}; ORFNames=J2061;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 118.
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 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25231979; DOI=10.1074/jbc.m114.601658;
RA Davydova E., Ho A.Y., Malecki J., Moen A., Enserink J.M., Jakobsson M.E.,
RA Loenarz C., Falnes P.O.;
RT "Identification and characterization of a novel evolutionarily conserved
RT lysine-specific methyltransferase targeting eukaryotic translation
RT elongation factor 2 (eEF2).";
RL J. Biol. Chem. 289:30499-30510(2014).
RN [9]
RP FUNCTION, AND 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-, di- and trimethylates elongation factor 2
CC (EFT1/EFT2) at 'Lys-509'. {ECO:0000269|PubMed:25086354,
CC ECO:0000269|PubMed:25231979}.
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 1550 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. EEF2KMT family. {ECO:0000305}.
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DR EMBL; Z49629; CAA89660.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08913.2; -; Genomic_DNA.
DR PIR; S57152; S57152.
DR RefSeq; NP_012663.2; NM_001181787.2.
DR AlphaFoldDB; P47163; -.
DR SMR; P47163; -.
DR BioGRID; 33884; 39.
DR STRING; 4932.YJR129C; -.
DR iPTMnet; P47163; -.
DR MaxQB; P47163; -.
DR PaxDb; P47163; -.
DR PRIDE; P47163; -.
DR EnsemblFungi; YJR129C_mRNA; YJR129C; YJR129C.
DR GeneID; 853593; -.
DR KEGG; sce:YJR129C; -.
DR SGD; S000003890; EFM3.
DR VEuPathDB; FungiDB:YJR129C; -.
DR eggNOG; KOG2497; Eukaryota.
DR GeneTree; ENSGT00940000164788; -.
DR HOGENOM; CLU_038942_1_1_1; -.
DR InParanoid; P47163; -.
DR OMA; PIRIYKI; -.
DR BioCyc; YEAST:G3O-31749-MON; -.
DR PRO; PR:P47163; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47163; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:UniProtKB.
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; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..339
FT /note="Protein-lysine N-methyltransferase EFM3"
FT /id="PRO_0000203120"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 174..176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 118
FT /note="K -> T (in Ref. 1; CAA89660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 39024 MW; A13C5ACD44970B99 CRC64;
MNEDLFYDRL HQRCPGKYLL EELETSKSND VLHASRFVCE MELVQKTNAY YCKTIVKMLL
DHEWIFAKAF TIVNDGEDEI EIYDYLYEKY IKLLSTGKPD PMMKDVVRYR FDEDVKIKIE
ETPNLISAAS TTGFRTWEAA LYMGDFLIHK PLQELAPVQG QDDGKKKLNV LEVGAGTGIV
SLVILQKYHE FVNKMYVTDG DSNLVETQLK RNFELNNEVR ENEPDIKLQR LWWGSDRVPE
DIDLVVGADV TYDPTILPDL CECLAECLAL DRCKLCLLSA TIRSESTVQL FSQECNKLGL
KCTIVTSTEY DANNEIRAMK ALQFKPLIAP IRIYKITKQ
