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Protein

Protein-lysine N-methyltransferase EFM2

Gene

EFM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei222 – 2221S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei290 – 2901S-adenosyl-L-methionineBy similarity
Binding sitei318 – 3181S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei340 – 3401S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

  • protein-lysine N-methyltransferase activity Source: SGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: SGD

GO - Biological processi

  • peptidyl-lysine dimethylation Source: SGD
  • peptidyl-lysine methylation Source: SGD
  • positive regulation of translational termination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29192-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-lysine N-methyltransferase EFM21 Publication (EC:2.1.1.-4 Publications)
Alternative name(s):
Elongation factor methyltransferase 21 Publication
Gene namesi
Name:EFM21 Publication
Ordered Locus Names:YBR271WImported
ORF Names:YBR1739
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR271W.
SGDiS000000475. EFM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Increases sensitivity to antibiotics that target translation and decreases translational fidelity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Protein-lysine N-methyltransferase EFM2PRO_0000202531Add
BLAST

Proteomic databases

MaxQBiP38347.

PTM databases

iPTMnetiP38347.

Interactioni

Protein-protein interaction databases

BioGridi32966. 8 interactions.
DIPiDIP-5051N.
IntActiP38347. 1 interaction.
MINTiMINT-534062.

Structurei

3D structure databases

ProteinModelPortaliP38347.
SMRiP38347. Positions 220-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 2633S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000248259.
InParanoidiP38347.
OMAiENCGRTA.
OrthoDBiEOG76TB3B.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR019410. Methyltransf_16.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF10294. Methyltransf_16. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

P38347-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDPLDLYTP DDIQVEALQF NLAEREPKDP CSPQRDEILT AVDEEESDDD
60 70 80 90 100
DTIIDNLDLP SVKYAPPEVI LCILILLKPD RQVNFNQETG KNKSVLEVCK
110 120 130 140 150
SHGLEPDLLK RLLTWYTEEW PNKRLNSLEK ICNKIPMLRF TVSKELLLGY
160 170 180 190 200
YTSVLKKYNN SCGLNEEIIQ ELLKELSSRI SENCGRTAQP SIVRYFELRN
210 220 230 240 250
LSTSIPLHEP SLTADNLGWK TWGSSLILSQ LVVDHLDYLH TTNVNMLANS
260 270 280 290 300
DIKQIKVLEL GAGTGLVGLS WALKWKELYG TENIEIFVTD LPEIVTNLKK
310 320 330 340 350
NVSLNNLGDF VQAEILDWTN PHDFIDKFGH ENEFDVILIA DPIYSPQHPE
360 370 380 390 400
WVVNMISKFL AASGTCHLEI PLRAKYAKER EVLKLLLKES DLKVVEERHS
410
EGVDDWGAVK YLYRQIVRN
Length:419
Mass (Da):47,977
Last modified:October 1, 1994 - v1
Checksum:iE15B739CB94BE4A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36140 Genomic DNA. Translation: CAA85234.1.
AY692663 Genomic DNA. Translation: AAT92682.1.
BK006936 Genomic DNA. Translation: DAA07387.1.
PIRiS46152.
RefSeqiNP_009830.3. NM_001178619.3.

Genome annotation databases

EnsemblFungiiYBR271W; YBR271W; YBR271W.
GeneIDi852574.
KEGGisce:YBR271W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36140 Genomic DNA. Translation: CAA85234.1.
AY692663 Genomic DNA. Translation: AAT92682.1.
BK006936 Genomic DNA. Translation: DAA07387.1.
PIRiS46152.
RefSeqiNP_009830.3. NM_001178619.3.

3D structure databases

ProteinModelPortaliP38347.
SMRiP38347. Positions 220-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32966. 8 interactions.
DIPiDIP-5051N.
IntActiP38347. 1 interaction.
MINTiMINT-534062.

PTM databases

iPTMnetiP38347.

Proteomic databases

MaxQBiP38347.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR271W; YBR271W; YBR271W.
GeneIDi852574.
KEGGisce:YBR271W.

Organism-specific databases

EuPathDBiFungiDB:YBR271W.
SGDiS000000475. EFM2.

Phylogenomic databases

HOGENOMiHOG000248259.
InParanoidiP38347.
OMAiENCGRTA.
OrthoDBiEOG76TB3B.

Enzyme and pathway databases

BioCyciYEAST:G3O-29192-MONOMER.

Miscellaneous databases

PROiP38347.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR019410. Methyltransf_16.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF10294. Methyltransf_16. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome."
    Wlodarski T., Kutner J., Towpik J., Knizewski L., Rychlewski L., Kudlicki A., Rowicka M., Dziembowski A., Ginalski K.
    PLoS ONE 6:E23168-E23168(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  8. "Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases."
    Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.
    Proteomics 12:960-972(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights into non-histone protein lysine methyltransferase activity."
    Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.
    J. Proteome Res. 13:1744-1756(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Elongation factor methyltransferase 3 - A novel eukaryotic lysine methyltransferase."
    Zhang L., Hamey J.J., Hart-Smith G., Erce M.A., Wilkins M.R.
    Biochem. Biophys. Res. Commun. 451:229-234(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  11. "Translational roles of elongation factor 2 protein lysine methylation."
    Dzialo M.C., Travaglini K.J., Shen S., Roy K., Chanfreau G.F., Loo J.A., Clarke S.G.
    J. Biol. Chem. 289:30511-30524(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiEFM2_YEAST
AccessioniPrimary (citable) accession number: P38347
Secondary accession number(s): D6VQR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 217 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.