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Protein

Protein-lysine N-methyltransferase EFM1

Gene

EFM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates elongation factor 1-alpha (TEF1/TEF2) at 'Lys-30'.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei280 – 2801S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

  • protein-lysine N-methyltransferase activity Source: SGD

GO - Biological processi

  • peptidyl-lysine monomethylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-31057-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-lysine N-methyltransferase EFM11 Publication (EC:2.1.1.-2 Publications)
Alternative name(s):
Elongation factor methyltransferase 11 Publication
Gene namesi
Name:EFM11 Publication
Ordered Locus Names:YHL039WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VIII

Organism-specific databases

CYGDiYHL039w.
EuPathDBiFungiDB:YHL039W.
SGDiS000001031. EFM1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Protein-lysine N-methyltransferase EFM1PRO_0000202879Add
BLAST

Proteomic databases

MaxQBiP38732.
PaxDbiP38732.
PeptideAtlasiP38732.

Interactioni

Protein-protein interaction databases

BioGridi36384. 25 interactions.
DIPiDIP-6582N.
IntActiP38732. 1 interaction.
MINTiMINT-705797.
STRINGi4932.YHL039W.

Structurei

3D structure databases

ProteinModelPortaliP38732.
SMRiP38732. Positions 21-56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 281259SETPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM1 family.PROSITE-ProRule annotationCurated
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG265033.
GeneTreeiENSGT00630000090454.
HOGENOMiHOG000141878.
InParanoidiP38732.
OMAiYNNYGDK.
OrthoDBiEOG7XSTQQ.

Family and domain databases

InterProiIPR017119. Ribosomal_Lys-MeTrfase-1.
IPR001214. SET_dom.
[Graphical view]
PIRSFiPIRSF037136. Ribosomal_Lys-mtfrase-1. 1 hit.
PROSITEiPS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITQTELDNC LQWAQNNGAF IDPKISFRIT EDAGVSAFVN EKFSPKPDQA
60 70 80 90 100
LIRVPETLLI TSQQALSEFS QAANERSLLN SVTQLYLSKL KFGTDAVHLK
110 120 130 140 150
SFYKPYLDVL PLHLPQPYFW STDEVMNLHG TDVYLTMRDT LNKLVKEWRM
160 170 180 190 200
LFQALSIEHS SQDKQFLSLF QENKDSAVVP LEQFCAHING CKLEDSEWNS
210 220 230 240 250
FVAYLWSYCI FNSRAFPRVI LGRAGTDRTN LNEGFLYPIV DLLNHKNDVP
260 270 280 290 300
VRWEMNEQNE LCFMSQTTTF SAQDELFNNY GNISNEKCLL NYGFWDSSNK
310 320 330 340 350
FDFSRLTLKL PSTLVSGLPV DFNKSGNFVT DDGETTILQF SLKISEPLPP
360 370 380 390 400
VLLALFAYLS KLKSEETPTV RSVLEGIDQL TSVVSQRLLF YKNFKIKTSS
410 420 430 440 450
TQKLRPHVIK LIKLYYQDNK KILNATTEKL SVLQKKIYSN NKEFSLSFKT
460 470 480 490 500
IFKNDKIFAN SLLLVFGAIN YEDLITKDCL NDALLLWIVK LINDKSNNQG
510 520 530 540 550
GFIKQTFKEV SDSIVIEKED VMEFLPFYKK YFPNLSERIP EIYSVGDWGI
560 570 580
RQFIVADTAI DRLVWIRKSN KEPIFLMKKA YDLQI
Length:585
Mass (Da):67,452
Last modified:February 1, 1995 - v1
Checksum:i84BC2D3A204D9D29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11583 Genomic DNA. Translation: AAB65051.1.
BK006934 Genomic DNA. Translation: DAA06647.1.
PIRiS48929.
RefSeqiNP_011824.1. NM_001179119.1.

Genome annotation databases

EnsemblFungiiYHL039W; YHL039W; YHL039W.
GeneIDi856346.
KEGGisce:YHL039W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11583 Genomic DNA. Translation: AAB65051.1.
BK006934 Genomic DNA. Translation: DAA06647.1.
PIRiS48929.
RefSeqiNP_011824.1. NM_001179119.1.

3D structure databases

ProteinModelPortaliP38732.
SMRiP38732. Positions 21-56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36384. 25 interactions.
DIPiDIP-6582N.
IntActiP38732. 1 interaction.
MINTiMINT-705797.
STRINGi4932.YHL039W.

Proteomic databases

MaxQBiP38732.
PaxDbiP38732.
PeptideAtlasiP38732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHL039W; YHL039W; YHL039W.
GeneIDi856346.
KEGGisce:YHL039W.

Organism-specific databases

CYGDiYHL039w.
EuPathDBiFungiDB:YHL039W.
SGDiS000001031. EFM1.

Phylogenomic databases

eggNOGiNOG265033.
GeneTreeiENSGT00630000090454.
HOGENOMiHOG000141878.
InParanoidiP38732.
OMAiYNNYGDK.
OrthoDBiEOG7XSTQQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31057-MONOMER.

Miscellaneous databases

NextBioi981778.
PROiP38732.

Family and domain databases

InterProiIPR017119. Ribosomal_Lys-MeTrfase-1.
IPR001214. SET_dom.
[Graphical view]
PIRSFiPIRSF037136. Ribosomal_Lys-mtfrase-1. 1 hit.
PROSITEiPS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae."
    Lipson R.S., Webb K.J., Clarke S.G.
    Arch. Biochem. Biophys. 500:137-143(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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.

Entry informationi

Entry nameiEFM1_YEAST
AccessioniPrimary (citable) accession number: P38732
Secondary accession number(s): D3DKT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 96 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 5170 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

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 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.