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Entry version 219 (29 Sep 2021)
Sequence version 1 (01 Oct 1993)
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Protein

Elongation factor 2

Gene

EFT1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

1 Publication

Miscellaneous

Present with 160782 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eEF2 in yeast.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by fusidic acid and sordarin, which prevent the release of eEF2 from the ribosome after the translocation step. While fusidic acid acts on all eukaryotic eEF2, sordarin specifically binds and inhibits only selected fungal eEF2. Inhibited by diphtheria toxin and Pseudomonas aeruginosa exotoxin A (ETA), which ADP-ribosylate the diphthamide residue.

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.010 mM for GTP

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi26 – 33GTPBy similarity8
Nucleotide bindingi104 – 108GTPBy similarity5
Nucleotide bindingi158 – 161GTPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionElongation factor, RNA-binding, rRNA-binding
Biological processProtein biosynthesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156902, Peptide chain elongation
R-SCE-5358493, Synthesis of diphthamide-EEF2
R-SCE-6798695, Neutrophil degranulation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00345

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Alternative name(s):
Eukaryotic elongation factor 2
Short name:
eEF2
Ribosomal translocase
Translation elongation factor 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EFT1
Ordered Locus Names:YOR133W
ORF Names:O3317, YOR3317W
AND
Name:EFT2
Ordered Locus Names:YDR385W
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome IV, Chromosome XV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000005659, EFT1
S000002793, EFT2

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDR385W
FungiDB:YOR133W

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi180R → G: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 1 Publication1
Mutagenesisi187V → F: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 1 Publication1
Mutagenesisi490Q → E: Reduces sensitivity to sordarin. 1 Publication1
Mutagenesisi521Y → D, N or S: Reduces sensitivity to fusidic acid and sordarin. 1 Publication1
Mutagenesisi523S → F or P: Causes resistance to fusidic acid and sordarin. 1 Publication1
Mutagenesisi529I → T: Reduces sensitivity to sordarin. 1 Publication1
Mutagenesisi559P → L or R: Causes resistance to fusidic acid and sordarin. 1 Publication1
Mutagenesisi562A → P: Reduces sensitivity to fusidic acid and causes resistance to sordarin. 1 Publication1
Mutagenesisi580P → H: Causes impaired ribosomal translocation with an increased rate of -1 programmed ribosomal frameshift read-through during translation. 1 Publication1
Mutagenesisi699H → D, E, L or M: Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin. 1 Publication1
Mutagenesisi701G → R: Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. 1 Publication1
Mutagenesisi727P → S: Causes resistance to sordarin. 1 Publication1
Mutagenesisi774V → F: Causes resistance to sordarin. 1 Publication1
Mutagenesisi790Missing : Causes resistance to fusidic acid and sordarin. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000910241 – 842Elongation factor 2Add BLAST842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei509N6,N6,N6-trimethyllysine; by EFM3; alternate2 Publications1
Modified residuei509N6,N6-dimethyllysine; by EFM3; alternate3 Publications1
Modified residuei509N6-methyllysine; by EFM3; alternate2 Publications1
Modified residuei579PhosphoserineCombined sources1
Modified residuei613N6,N6-dimethyllysine; by EFM2; alternate2 Publications1
Modified residuei613N6-methyllysine; by EFM2; alternate2 Publications1
Modified residuei699Diphthamide1 Publication1
Modified residuei713PhosphothreonineCombined sources1
Modified residuei763PhosphothreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki841Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32324

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P32324

PRoteomics IDEntifications database

More...
PRIDEi
P32324

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P32324

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P32324

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32324

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds to 80S ribosomes.

Interacts directly with the 40S ribosomal subunit protein RPL9A, the 60S ribosomal subunit proteins RPL12A and RPS23A, as well as the 18S rRNA and the 25S rRNA.

Interacts with RPL0.

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
32446, 222 interactors
34529, 130 interactors

Database of interacting proteins

More...
DIPi
DIP-4911N

Protein interaction database and analysis system

More...
IntActi
P32324, 156 interactors

Molecular INTeraction database

More...
MINTi
P32324

STRING: functional protein association networks

More...
STRINGi
4932.YOR133W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32324, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1842
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P32324

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32324

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini17 – 346tr-type GPROSITE-ProRule annotationAdd BLAST330

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0469, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154662

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002794_11_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32324

Identification of Orthologs from Complete Genome Data

More...
OMAi
GVMTQTE

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.10, 1 hit
3.40.50.300, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041095, EFG_II
IPR035647, EFG_III/V
IPR000640, EFG_V-like
IPR004161, EFTu-like_2
IPR031157, G_TR_CS
IPR027417, P-loop_NTPase
IPR020568, Ribosomal_S5_D2-typ_fold
IPR014721, Ribosomal_S5_D2-typ_fold_subgr
IPR005225, Small_GTP-bd_dom
IPR000795, T_Tr_GTP-bd_dom
IPR009000, Transl_B-barrel_sf
IPR005517, Transl_elong_EFG/EF2_IV

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00679, EFG_C, 1 hit
PF14492, EFG_III, 1 hit
PF03764, EFG_IV, 1 hit
PF00009, GTP_EFTU, 1 hit
PF03144, GTP_EFTU_D2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00315, ELONGATNFCT

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00838, EFG_C, 1 hit
SM00889, EFG_IV, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50447, SSF50447, 1 hit
SSF52540, SSF52540, 1 hit
SSF54211, SSF54211, 1 hit
SSF54980, SSF54980, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00231, small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00301, G_TR_1, 1 hit
PS51722, G_TR_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P32324-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK
60 70 80 90 100
AGEARFTDTR KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR VTDGALVVVD TIEGVCVQTE TVLRQALGER
160 170 180 190 200
IKPVVVINKV DRALLELQVS KEDLYQTFAR TVESVNVIVS TYADEVLGDV
210 220 230 240 250
QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM MDRLWGDSFF
260 270 280 290 300
NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL
310 320 330 340 350
EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA
360 370 380 390 400
YRAEQLYEGP ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV
410 420 430 440 450
FAGTVKSGQK VRIQGPNYVP GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA
460 470 480 490 500
GNIIGLVGID QFLLKTGTLT TSETAHNMKV MKFSVSPVVQ VAVEVKNAND
510 520 530 540 550
LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI CLQDLEHDHA
560 570 580 590 600
GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA
610 620 630 640 650
IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT
660 670 680 690 700
KAVQYLHEIK DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR
710 720 730 740 750
GGGQIIPTMR RATYAGFLLA DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK
760 770 780 790 800
RGQVVSEEQR PGTPLFTVKA YLPVNESFGF TGELRQATGG QAFPQMVFDH
810 820 830 840
WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD KL
Length:842
Mass (Da):93,289
Last modified:October 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFD2F8073CB9B66AA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M59369 Genomic DNA Translation: AAA21646.1
M59370 Genomic DNA Translation: AAA51398.1
X90518 Genomic DNA Translation: CAA62116.1
X94335 Genomic DNA Translation: CAA64052.1
U32274 Genomic DNA Translation: AAB64827.1
U28373 Genomic DNA Translation: AAB64821.1
Z75041 Genomic DNA Translation: CAA99332.1
AY497635 Genomic DNA Translation: AAT12549.1
BK006948 Genomic DNA Translation: DAA10907.1
BK006938 Genomic DNA Translation: DAA12229.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A41778

NCBI Reference Sequences

More...
RefSeqi
NP_010673.1, NM_001180693.1
NP_014776.1, NM_001183552.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR385W_mRNA; YDR385W; YDR385W
YOR133W_mRNA; YOR133W; YOR133W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851993
854301

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR385W
sce:YOR133W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59369 Genomic DNA Translation: AAA21646.1
M59370 Genomic DNA Translation: AAA51398.1
X90518 Genomic DNA Translation: CAA62116.1
X94335 Genomic DNA Translation: CAA64052.1
U32274 Genomic DNA Translation: AAB64827.1
U28373 Genomic DNA Translation: AAB64821.1
Z75041 Genomic DNA Translation: CAA99332.1
AY497635 Genomic DNA Translation: AAT12549.1
BK006948 Genomic DNA Translation: DAA10907.1
BK006938 Genomic DNA Translation: DAA12229.1
PIRiA41778
RefSeqiNP_010673.1, NM_001180693.1
NP_014776.1, NM_001183552.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N0UX-ray2.12A1-842[»]
1N0VX-ray2.85C/D1-842[»]
1U2RX-ray2.60A1-842[»]
1ZM2X-ray3.07A/C/E1-842[»]
1ZM3X-ray3.07A/C/E1-842[»]
1ZM4X-ray2.90A/C/E1-842[»]
1ZM9X-ray2.80A/C/E1-842[»]
2E1RX-ray3.15A1-842[»]
2NPFX-ray2.90A/B1-842[»]
2P8Welectron microscopy11.30T1-842[»]
2P8Xelectron microscopy9.70T1-842[»]
2P8Yelectron microscopy11.70T1-842[»]
2P8Zelectron microscopy8.90T1-842[»]
2ZITX-ray3.00A/C/E1-842[»]
3B78X-ray2.50A/C/E1-842[»]
3B82X-ray2.35A/C/E1-842[»]
3B8HX-ray2.50A/C/E1-842[»]
3DNYelectron microscopy12.60T1-842[»]
4V4Belectron microscopy11.70AT1-842[»]
5JUOelectron microscopy4.00DC1-842[»]
5JUPelectron microscopy3.50DC1-842[»]
5JUSelectron microscopy4.20DC1-842[»]
5JUTelectron microscopy4.00DC1-842[»]
5JUUelectron microscopy4.00DC1-842[»]
6GQ1electron microscopy4.40AZ3-842[»]
6GQBelectron microscopy3.90AZ3-842[»]
6GQVelectron microscopy4.00AX3-839[»]
SMRiP32324
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32446, 222 interactors
34529, 130 interactors
DIPiDIP-4911N
IntActiP32324, 156 interactors
MINTiP32324
STRINGi4932.YOR133W

PTM databases

iPTMnetiP32324

2D gel databases

SWISS-2DPAGEiP32324

Proteomic databases

MaxQBiP32324
PaxDbiP32324
PRIDEiP32324
TopDownProteomicsiP32324

Genome annotation databases

EnsemblFungiiYDR385W_mRNA; YDR385W; YDR385W
YOR133W_mRNA; YOR133W; YOR133W
GeneIDi851993
854301
KEGGisce:YDR385W
sce:YOR133W

Organism-specific databases

SGDiS000005659, EFT1
S000002793, EFT2
VEuPathDBiFungiDB:YDR385W
FungiDB:YOR133W

Phylogenomic databases

eggNOGiKOG0469, Eukaryota
GeneTreeiENSGT00940000154662
HOGENOMiCLU_002794_11_2_1
InParanoidiP32324
OMAiGVMTQTE

Enzyme and pathway databases

UniPathwayiUPA00345
ReactomeiR-SCE-156902, Peptide chain elongation
R-SCE-5358493, Synthesis of diphthamide-EEF2
R-SCE-6798695, Neutrophil degranulation

Miscellaneous databases

EvolutionaryTraceiP32324

Protein Ontology

More...
PROi
PR:P32324
RNActiP32324, protein

Family and domain databases

Gene3Di3.30.230.10, 1 hit
3.40.50.300, 1 hit
InterProiView protein in InterPro
IPR041095, EFG_II
IPR035647, EFG_III/V
IPR000640, EFG_V-like
IPR004161, EFTu-like_2
IPR031157, G_TR_CS
IPR027417, P-loop_NTPase
IPR020568, Ribosomal_S5_D2-typ_fold
IPR014721, Ribosomal_S5_D2-typ_fold_subgr
IPR005225, Small_GTP-bd_dom
IPR000795, T_Tr_GTP-bd_dom
IPR009000, Transl_B-barrel_sf
IPR005517, Transl_elong_EFG/EF2_IV
PfamiView protein in Pfam
PF00679, EFG_C, 1 hit
PF14492, EFG_III, 1 hit
PF03764, EFG_IV, 1 hit
PF00009, GTP_EFTU, 1 hit
PF03144, GTP_EFTU_D2, 1 hit
PRINTSiPR00315, ELONGATNFCT
SMARTiView protein in SMART
SM00838, EFG_C, 1 hit
SM00889, EFG_IV, 1 hit
SUPFAMiSSF50447, SSF50447, 1 hit
SSF52540, SSF52540, 1 hit
SSF54211, SSF54211, 1 hit
SSF54980, SSF54980, 2 hits
TIGRFAMsiTIGR00231, small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS00301, G_TR_1, 1 hit
PS51722, G_TR_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEF2_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32324
Secondary accession number(s): D6VT19, Q6JEF7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 29, 2021
This is version 219 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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