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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-Experimental evidence at protein leveli

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

Enzyme 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.

Kineticsi

  1. KM=0.010 mM for GTP

    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
    Nucleotide bindingi26 – 33GTPBy similarity8
    Nucleotide bindingi104 – 108GTPBy similarity5
    Nucleotide bindingi158 – 161GTPBy similarity4

    GO - Molecular functioni

    • GTPase activity Source: SGD
    • GTP binding Source: UniProtKB-KW
    • rRNA binding Source: UniProtKB-KW
    • translation elongation factor activity Source: SGD

    GO - Biological processi

    • maintenance of translational fidelity Source: SGD
    • peptidyl-diphthamide biosynthetic process from peptidyl-histidine Source: Reactome
    • positive regulation of translational elongation Source: SGD
    • translational elongation Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

    Enzyme and pathway databases

    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.
    R-SCE-72165. mRNA Splicing - Minor Pathway.
    UniPathwayiUPA00345.

    Names & Taxonomyi

    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
    Gene namesi
    Name:EFT1
    Ordered Locus Names:YOR133W
    ORF Names:O3317, YOR3317W
    AND
    Name:EFT2
    Ordered Locus Names:YDR385W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componentsi: Chromosome IV, Chromosome XV

    Organism-specific databases

    SGDiS000005659. EFT1.
    S000002793. EFT2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000910241 – 842Elongation factor 2Add BLAST842

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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
    Cross-linki841Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

    Keywords - PTMi

    Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP32324.
    PRIDEiP32324.
    TopDownProteomicsiP32324.

    2D gel databases

    SWISS-2DPAGEP32324.

    PTM databases

    iPTMnetiP32324.

    Interactioni

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RPP0P053172EBI-6333,EBI-15447
    SKP1P522862EBI-6333,EBI-4090

    Protein-protein interaction databases

    BioGridi32446. 135 interactors.
    34529. 85 interactors.
    DIPiDIP-4911N.
    IntActiP32324. 138 interactors.
    MINTiMINT-8285544.

    Structurei

    Secondary structure

    1842
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 4Combined sources3
    Helixi6 – 14Combined sources9
    Helixi16 – 18Combined sources3
    Beta strandi19 – 25Combined sources7
    Helixi28 – 30Combined sources3
    Helixi32 – 43Combined sources12
    Beta strandi44 – 48Combined sources5
    Beta strandi74 – 80Combined sources7
    Helixi83 – 88Combined sources6
    Beta strandi95 – 103Combined sources9
    Helixi109 – 111Combined sources3
    Helixi113 – 120Combined sources8
    Beta strandi123 – 130Combined sources8
    Turni131 – 133Combined sources3
    Helixi137 – 148Combined sources12
    Beta strandi152 – 158Combined sources7
    Helixi160 – 165Combined sources6
    Helixi171 – 192Combined sources22
    Helixi195 – 197Combined sources3
    Helixi204 – 206Combined sources3
    Beta strandi209 – 213Combined sources5
    Turni214 – 217Combined sources4
    Beta strandi218 – 221Combined sources4
    Helixi222 – 230Combined sources9
    Turni231 – 234Combined sources4
    Helixi237 – 243Combined sources7
    Beta strandi245 – 247Combined sources3
    Beta strandi249 – 251Combined sources3
    Turni252 – 255Combined sources4
    Beta strandi256 – 259Combined sources4
    Beta strandi261 – 263Combined sources3
    Turni264 – 266Combined sources3
    Helixi272 – 276Combined sources5
    Helixi278 – 289Combined sources12
    Helixi295 – 302Combined sources8
    Helixi309 – 313Combined sources5
    Helixi316 – 327Combined sources12
    Helixi330 – 341Combined sources12
    Helixi345 – 356Combined sources12
    Beta strandi357 – 359Combined sources3
    Helixi364 – 370Combined sources7
    Beta strandi374 – 377Combined sources4
    Beta strandi379 – 390Combined sources12
    Beta strandi394 – 406Combined sources13
    Beta strandi410 – 414Combined sources5
    Beta strandi420 – 422Combined sources3
    Beta strandi426 – 430Combined sources5
    Beta strandi433 – 438Combined sources6
    Beta strandi441 – 449Combined sources9
    Beta strandi453 – 458Combined sources6
    Turni460 – 462Combined sources3
    Beta strandi465 – 471Combined sources7
    Beta strandi489 – 497Combined sources9
    Helixi498 – 500Combined sources3
    Helixi501 – 514Combined sources14
    Beta strandi519 – 522Combined sources4
    Beta strandi528 – 534Combined sources7
    Helixi535 – 547Combined sources13
    Beta strandi554 – 557Combined sources4
    Beta strandi564 – 569Combined sources6
    Beta strandi575 – 578Combined sources4
    Beta strandi580 – 582Combined sources3
    Beta strandi585 – 592Combined sources8
    Helixi595 – 602Combined sources8
    Beta strandi604 – 606Combined sources3
    Beta strandi608 – 610Combined sources3
    Helixi612 – 621Combined sources10
    Helixi627 – 631Combined sources5
    Beta strandi633 – 638Combined sources6
    Turni639 – 641Combined sources3
    Beta strandi642 – 648Combined sources7
    Helixi656 – 672Combined sources17
    Turni675 – 677Combined sources3
    Beta strandi683 – 692Combined sources10
    Helixi697 – 699Combined sources3
    Helixi702 – 719Combined sources18
    Beta strandi722 – 735Combined sources14
    Helixi737 – 739Combined sources3
    Helixi740 – 748Combined sources9
    Turni749 – 751Combined sources3
    Beta strandi753 – 758Combined sources6
    Beta strandi766 – 773Combined sources8
    Helixi774 – 776Combined sources3
    Helixi780 – 787Combined sources8
    Turni788 – 790Combined sources3
    Beta strandi793 – 803Combined sources11
    Beta strandi811 – 813Combined sources3
    Helixi814 – 825Combined sources12
    Helixi835 – 838Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP32324.
    SMRiP32324.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32324.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini17 – 346tr-type GPROSITE-ProRule annotationAdd BLAST330

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00860000133841.
    ENSGT00860000133864.
    HOGENOMiHOG000231589.
    InParanoidiP32324.
    KOiK03234.
    OMAiVYPDQGT.
    OrthoDBiEOG092C0D4V.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR009022. EFG_III-V.
    IPR000640. EFG_V.
    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.
    IPR005517. Transl_elong_EFG/EF2_IV.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    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
    Checksum:iFD2F8073CB9B66AA
    GO

    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.

    Genome annotation databases

    EnsemblFungiiYDR385W; YDR385W; YDR385W.
    YOR133W; YOR133W; YOR133W.
    GeneIDi851993.
    854301.
    KEGGisce:YDR385W.
    sce:YOR133W.

    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:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP32324.
    SMRiP32324.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32446. 135 interactors.
    34529. 85 interactors.
    DIPiDIP-4911N.
    IntActiP32324. 138 interactors.
    MINTiMINT-8285544.

    PTM databases

    iPTMnetiP32324.

    2D gel databases

    SWISS-2DPAGEP32324.

    Proteomic databases

    MaxQBiP32324.
    PRIDEiP32324.
    TopDownProteomicsiP32324.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDR385W; YDR385W; YDR385W.
    YOR133W; YOR133W; YOR133W.
    GeneIDi851993.
    854301.
    KEGGisce:YDR385W.
    sce:YOR133W.

    Organism-specific databases

    SGDiS000005659. EFT1.
    S000002793. EFT2.

    Phylogenomic databases

    GeneTreeiENSGT00860000133841.
    ENSGT00860000133864.
    HOGENOMiHOG000231589.
    InParanoidiP32324.
    KOiK03234.
    OMAiVYPDQGT.
    OrthoDBiEOG092C0D4V.

    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.
    R-SCE-72165. mRNA Splicing - Minor Pathway.

    Miscellaneous databases

    EvolutionaryTraceiP32324.
    PROiP32324.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR009022. EFG_III-V.
    IPR000640. EFG_V.
    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.
    IPR005517. Transl_elong_EFG/EF2_IV.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiEF2_YEAST
    AccessioniPrimary (citable) accession number: P32324
    Secondary accession number(s): D6VT19, Q6JEF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: November 30, 2016
    This is version 178 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 160782 molecules/cell in log phase SD medium.1 Publication
    There are 2 genes for eEF2 in yeast.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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