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Entry version 208 (13 Nov 2019)
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

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:G3O-29933-MONOMER
    YEAST:G3O-33657-MONOMER

    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

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    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.<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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    32446, 220 interactors
    34529, 122 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

    <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

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000231589

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P32324

    KEGG Orthology (KO)

    More...
    KOi
    K03234

    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

    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 TF_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_II, 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

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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, 220 interactors
    34529, 122 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

    Phylogenomic databases

    HOGENOMiHOG000231589
    InParanoidiP32324
    KOiK03234
    OMAiGVMTQTE

    Enzyme and pathway databases

    UniPathwayiUPA00345
    BioCyciYEAST:G3O-29933-MONOMER
    YEAST:G3O-33657-MONOMER
    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

    Family and domain databases

    Gene3Di3.30.230.10, 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 TF_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_II, 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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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: November 13, 2019
    This is version 208 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, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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