EF2_YEAST
ID EF2_YEAST Reviewed; 842 AA.
AC P32324; D6VT19; Q6JEF7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE AltName: Full=Eukaryotic elongation factor 2;
DE Short=eEF2;
DE AltName: Full=Ribosomal translocase;
DE AltName: Full=Translation elongation factor 2;
GN Name=EFT1; OrderedLocusNames=YOR133W; ORFNames=O3317, YOR3317W;
GN and
GN Name=EFT2; OrderedLocusNames=YDR385W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1 AND EFT2).
RX PubMed=1730643; DOI=10.1016/s0021-9258(18)48413-x;
RA Perentesis J.P., Phan L.D., Laporte D.C., Livingston D.M., Bodley J.W.;
RT "Saccharomyces cerevisiae elongation factor 2. Genetic cloning,
RT characterization of expression, and G-domain modeling.";
RL J. Biol. Chem. 267:1190-1197(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1).
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1).
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
RP GENOME REANNOTATION (EFT1 AND EFT2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP PROTEIN SEQUENCE OF 411-422 AND 505-513.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-785.
RX PubMed=15583292; DOI=10.1128/jcm.42.12.5624-5635.2004;
RA Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.;
RT "Phylogeny and evolution of medical species of Candida and related taxa: a
RT multigenic analysis.";
RL J. Clin. Microbiol. 42:5624-5635(2004).
RN [9]
RP PROTEIN SEQUENCE OF 686-700, AND DIPHTHAMIDE AT HIS-699.
RX PubMed=721806; DOI=10.1016/s0021-9258(17)34230-8;
RA Van Ness B.G., Howard J.B., Bodley J.W.;
RT "Isolation and properties of the trypsin-derived ADP-ribosyl peptide from
RT diphtheria toxin-modified yeast elongation factor 2.";
RL J. Biol. Chem. 253:8687-8690(1978).
RN [10]
RP PHOSPHORYLATION.
RX PubMed=1936278; DOI=10.1016/0014-5793(91)81307-t;
RA Donovan M.G., Bodley J.W.;
RT "Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an
RT endogenous kinase.";
RL FEBS Lett. 291:303-306(1991).
RN [11]
RP MUTAGENESIS OF GLY-701.
RX PubMed=8466491; DOI=10.1006/bbrc.1993.1336;
RA Kimata Y., Harashima S., Kohno K.;
RT "Expression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation
RT factor 2 in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 191:1145-1151(1993).
RN [12]
RP MUTAGENESIS OF HIS-699.
RX PubMed=8473309; DOI=10.1016/s0021-9258(18)52926-4;
RA Phan L.D., Perentesis J.P., Bodley J.W.;
RT "Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine
RT precursor of diphthamide yields a functional protein that is resistant to
RT diphtheria toxin.";
RL J. Biol. Chem. 268:8665-8668(1993).
RN [13]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-180; VAL-187; GLN-490; TYR-521;
RP SER-523; ILE-529; PRO-559; ALA-562; PRO-727; VAL-774 AND GLY-790.
RX PubMed=9452424; DOI=10.1074/jbc.273.6.3148;
RA Justice M.C., Hsu M.-J., Tse B., Ku T., Balkovec J., Schmatz D.,
RA Nielsen J.;
RT "Elongation factor 2 as a novel target for selective inhibition of fungal
RT protein synthesis.";
RL J. Biol. Chem. 273:3148-3151(1998).
RN [14]
RP INTERACTION WITH RPL0.
RX PubMed=12410829; DOI=10.1046/j.1365-2958.2002.03179.x;
RA Lalioti V.S., Perez-Fernandez J., Remacha M.A., Ballesta J.P.G.;
RT "Characterization of interaction sites in the Saccharomyces cerevisiae
RT ribosomal stalk components.";
RL Mol. Microbiol. 46:719-729(2002).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP MUTAGENESIS OF HIS-699.
RX PubMed=18627462; DOI=10.1111/j.1365-2958.2008.06350.x;
RA Baer C., Zabel R., Liu S., Stark M.J., Schaffrath R.;
RT "A versatile partner of eukaryotic protein complexes that is involved in
RT multiple biological processes: Kti11/Dph3.";
RL Mol. Microbiol. 69:1221-1233(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; THR-713 AND THR-763, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20]
RP MUTAGENESIS OF PRO-580.
RX PubMed=23001565; DOI=10.1093/hmg/dds392;
RA Hekman K.E., Yu G.Y., Brown C.D., Zhu H., Du X., Gervin K., Undlien D.E.,
RA Peterson A., Stevanin G., Clark H.B., Pulst S.M., Bird T.D., White K.P.,
RA Gomez C.M.;
RT "A conserved eEF2 coding variant in SCA26 leads to loss of translational
RT fidelity and increased susceptibility to proteostatic insult.";
RL Hum. Mol. Genet. 21:5472-5483(2012).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-841, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [23]
RP METHYLATION AT LYS-509.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [24]
RP METHYLATION AT LYS-509 BY EFM3, AND METHYLATION AT LYS-613 BY EFM2.
RX PubMed=25086354; DOI=10.1016/j.bbrc.2014.07.110;
RA Zhang L., Hamey J.J., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Elongation factor methyltransferase 3 - A novel eukaryotic lysine
RT methyltransferase.";
RL Biochem. Biophys. Res. Commun. 451:229-234(2014).
RN [25]
RP METHYLATION AT LYS-509, AND METHYLATION AT LYS-613 BY EFM2.
RX PubMed=24517342; DOI=10.1021/pr401251k;
RA Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.;
RT "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights
RT into non-histone protein lysine methyltransferase activity.";
RL J. Proteome Res. 13:1744-1756(2014).
RN [26] {ECO:0007744|PDB:1N0U, ECO:0007744|PDB:1N0V}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SORDARIN, AND
RP ACTIVITY REGULATION.
RX PubMed=12692531; DOI=10.1038/nsb923;
RA Joergensen R., Ortiz P.A., Carr-Schmid A., Nissen P., Kinzy T.G.,
RA Andersen G.R.;
RT "Two crystal structures demonstrate large conformational changes in the
RT eukaryotic ribosomal translocase.";
RL Nat. Struct. Biol. 10:379-385(2003).
RN [27] {ECO:0007744|PDB:4V4B}
RP STRUCTURE BY ELECTRON MICROSCOPY (11.7 ANGSTROMS) IN COMPLEX WITH 80S
RP RIBOSOME AND SORDARIN, FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH
RP RPL9A; RPL12A; RPS23A; 18S RRNA AND 25S RRNA.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [28] {ECO:0007744|PDB:1U2R}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ADP-RIBOSYLATED FORM IN COMPLEX
RP WITH GDP AND SORDARIN.
RX PubMed=15316019; DOI=10.1074/jbc.m406218200;
RA Joergensen R., Yates S.P., Teal D.J., Nilsson J., Prentice G.A.,
RA Merrill A.R., Andersen G.R.;
RT "Crystal structure of ADP-ribosylated ribosomal translocase from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:45919-45925(2004).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000269|PubMed:14976550}.
CC -!- ACTIVITY REGULATION: Inhibited by fusidic acid and sordarin, which
CC prevent the release of eEF2 from the ribosome after the translocation
CC step (PubMed:9452424, PubMed:12692531, PubMed:14976550). While fusidic
CC acid acts on all eukaryotic eEF2, sordarin specifically binds and
CC inhibits only selected fungal eEF2 (PubMed:9452424).
CC {ECO:0000269|PubMed:12692531, ECO:0000269|PubMed:14976550,
CC ECO:0000269|PubMed:9452424}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.010 mM for GTP;
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Binds to 80S ribosomes (PubMed:12692531, PubMed:14976550,
CC PubMed:15316019). Interacts with the 40S ribosomal subunit protein
CC RPL9A; the interaction is direct (PubMed:14976550). Interacts with the
CC 60S ribosomal subunit proteins RPL12A; the interaction is direct
CC (PubMed:14976550). Interacts with RPS23A; the interaction is direct
CC (PubMed:14976550). Interacts with 18S rRNA; the interaction is direct
CC (PubMed:14976550). Interacts with 25S rRNA; the interaction is direct
CC (PubMed:14976550). Interacts with RPL0 (PubMed:12410829).
CC {ECO:0000269|PubMed:12410829, ECO:0000269|PubMed:12692531,
CC ECO:0000269|PubMed:14976550, ECO:0000269|PubMed:15316019}.
CC -!- INTERACTION:
CC P32324; P32324: EFT2; NbExp=4; IntAct=EBI-6333, EBI-6333;
CC P32324; P05317: RPP0; NbExp=3; IntAct=EBI-6333, EBI-15447;
CC P32324; P52286: SKP1; NbExp=2; IntAct=EBI-6333, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Diphthamide can be ADP-ribosylated by diphtheria toxin and by
CC Pseudomonas exotoxin A, thus abolishing its function.
CC {ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:18627462}.
CC -!- MISCELLANEOUS: Present with 160782 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eEF2 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; M59369; AAA21646.1; -; Genomic_DNA.
DR EMBL; M59370; AAA51398.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62116.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64052.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64827.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64821.1; -; Genomic_DNA.
DR EMBL; Z75041; CAA99332.1; -; Genomic_DNA.
DR EMBL; AY497635; AAT12549.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10907.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12229.1; -; Genomic_DNA.
DR PIR; A41778; A41778.
DR RefSeq; NP_010673.1; NM_001180693.1.
DR RefSeq; NP_014776.1; NM_001183552.1.
DR PDB; 1N0U; X-ray; 2.12 A; A=1-842.
DR PDB; 1N0V; X-ray; 2.85 A; C/D=1-842.
DR PDB; 1U2R; X-ray; 2.60 A; A=1-842.
DR PDB; 1ZM2; X-ray; 3.07 A; A/C/E=1-842.
DR PDB; 1ZM3; X-ray; 3.07 A; A/C/E=1-842.
DR PDB; 1ZM4; X-ray; 2.90 A; A/C/E=1-842.
DR PDB; 1ZM9; X-ray; 2.80 A; A/C/E=1-842.
DR PDB; 2E1R; X-ray; 3.15 A; A=1-842.
DR PDB; 2NPF; X-ray; 2.90 A; A/B=1-842.
DR PDB; 2P8W; EM; 11.30 A; T=1-842.
DR PDB; 2P8X; EM; 9.70 A; T=1-842.
DR PDB; 2P8Y; EM; 11.70 A; T=1-842.
DR PDB; 2P8Z; EM; 8.90 A; T=1-842.
DR PDB; 2ZIT; X-ray; 3.00 A; A/C/E=1-842.
DR PDB; 3B78; X-ray; 2.50 A; A/C/E=1-842.
DR PDB; 3B82; X-ray; 2.35 A; A/C/E=1-842.
DR PDB; 3B8H; X-ray; 2.50 A; A/C/E=1-842.
DR PDB; 3DNY; EM; 12.60 A; T=1-842.
DR PDB; 4V4B; EM; 11.70 A; AT=1-842.
DR PDB; 5JUO; EM; 4.00 A; DC=1-842.
DR PDB; 5JUP; EM; 3.50 A; DC=1-842.
DR PDB; 5JUS; EM; 4.20 A; DC=1-842.
DR PDB; 5JUT; EM; 4.00 A; DC=1-842.
DR PDB; 5JUU; EM; 4.00 A; DC=1-842.
DR PDB; 6GQ1; EM; 4.40 A; AZ=3-842.
DR PDB; 6GQB; EM; 3.90 A; AZ=3-842.
DR PDB; 6GQV; EM; 4.00 A; AX=3-839.
DR PDBsum; 1N0U; -.
DR PDBsum; 1N0V; -.
DR PDBsum; 1U2R; -.
DR PDBsum; 1ZM2; -.
DR PDBsum; 1ZM3; -.
DR PDBsum; 1ZM4; -.
DR PDBsum; 1ZM9; -.
DR PDBsum; 2E1R; -.
DR PDBsum; 2NPF; -.
DR PDBsum; 2P8W; -.
DR PDBsum; 2P8X; -.
DR PDBsum; 2P8Y; -.
DR PDBsum; 2P8Z; -.
DR PDBsum; 2ZIT; -.
DR PDBsum; 3B78; -.
DR PDBsum; 3B82; -.
DR PDBsum; 3B8H; -.
DR PDBsum; 3DNY; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR AlphaFoldDB; P32324; -.
DR SMR; P32324; -.
DR BioGRID; 32446; 222.
DR BioGRID; 34529; 152.
DR DIP; DIP-4911N; -.
DR IntAct; P32324; 231.
DR MINT; P32324; -.
DR STRING; 4932.YDR385W; -.
DR iPTMnet; P32324; -.
DR SWISS-2DPAGE; P32324; -.
DR MaxQB; P32324; -.
DR PaxDb; P32324; -.
DR PRIDE; P32324; -.
DR TopDownProteomics; P32324; -.
DR EnsemblFungi; YDR385W_mRNA; YDR385W; YDR385W.
DR EnsemblFungi; YOR133W_mRNA; YOR133W; YOR133W.
DR GeneID; 851993; -.
DR GeneID; 854301; -.
DR KEGG; sce:YDR385W; -.
DR KEGG; sce:YOR133W; -.
DR SGD; S000005659; EFT1.
DR SGD; S000002793; EFT2.
DR VEuPathDB; FungiDB:YDR385W; -.
DR VEuPathDB; FungiDB:YOR133W; -.
DR eggNOG; KOG0469; Eukaryota.
DR GeneTree; ENSGT00940000154662; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; P32324; -.
DR OMA; GVMTQTE; -.
DR BioCyc; YEAST:G3O-29933-MON; -.
DR BioCyc; YEAST:G3O-33657-MON; -.
DR Reactome; R-SCE-156902; Peptide chain elongation.
DR Reactome; R-SCE-5358493; Synthesis of diphthamide-EEF2.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00345; -.
DR EvolutionaryTrace; P32324; -.
DR PRO; PR:P32324; -.
DR Proteomes; UP000002311; Chromosome IV.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32324; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:SGD.
DR GO; GO:0045901; P:positive regulation of translational elongation; IMP:SGD.
DR GO; GO:0006414; P:translational elongation; IMP:SGD.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Elongation factor;
KW GTP-binding; Isopeptide bond; Methylation; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW rRNA-binding; Ubl conjugation.
FT CHAIN 1..842
FT /note="Elongation factor 2"
FT /id="PRO_0000091024"
FT DOMAIN 17..346
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 509
FT /note="N6,N6,N6-trimethyllysine; by EFM3; alternate"
FT /evidence="ECO:0000269|PubMed:24517342,
FT ECO:0000269|PubMed:25086354"
FT MOD_RES 509
FT /note="N6,N6-dimethyllysine; by EFM3; alternate"
FT /evidence="ECO:0000269|PubMed:22522802,
FT ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354"
FT MOD_RES 509
FT /note="N6-methyllysine; by EFM3; alternate"
FT /evidence="ECO:0000269|PubMed:24517342,
FT ECO:0000269|PubMed:25086354"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 613
FT /note="N6,N6-dimethyllysine; by EFM2; alternate"
FT /evidence="ECO:0000269|PubMed:24517342,
FT ECO:0000269|PubMed:25086354"
FT MOD_RES 613
FT /note="N6-methyllysine; by EFM2; alternate"
FT /evidence="ECO:0000269|PubMed:24517342,
FT ECO:0000269|PubMed:25086354"
FT MOD_RES 699
FT /note="Diphthamide"
FT /evidence="ECO:0000269|PubMed:721806"
FT MOD_RES 713
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 763
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 841
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 180
FT /note="R->G: Causes resistance to fusidic acid and reduces
FT sensitivity to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 187
FT /note="V->F: Causes resistance to fusidic acid and reduces
FT sensitivity to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 490
FT /note="Q->E: Reduces sensitivity to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 521
FT /note="Y->D,N,S: Reduces sensitivity to fusidic acid and
FT sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 523
FT /note="S->F,P: Causes resistance to fusidic acid and
FT sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 529
FT /note="I->T: Reduces sensitivity to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 559
FT /note="P->L,R: Causes resistance to fusidic acid and
FT sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 562
FT /note="A->P: Reduces sensitivity to fusidic acid and causes
FT resistance to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 580
FT /note="P->H: Causes impaired ribosomal translocation with
FT an increased rate of -1 programmed ribosomal frameshift
FT read-through during translation."
FT /evidence="ECO:0000269|PubMed:23001565"
FT MUTAGEN 699
FT /note="H->D,E,L,M,I: Prevents post-translational
FT modification of this residue to diphthamide. Results in a
FT functional protein that is resistant to diphtheria toxin
FT and sordarin."
FT /evidence="ECO:0000269|PubMed:18627462,
FT ECO:0000269|PubMed:8473309"
FT MUTAGEN 701
FT /note="G->R: Prevents ADP-ribosylation of the diphthamide
FT by diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:8466491"
FT MUTAGEN 727
FT /note="P->S: Causes resistance to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 774
FT /note="V->F: Causes resistance to sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT MUTAGEN 790
FT /note="Missing: Causes resistance to fusidic acid and
FT sordarin."
FT /evidence="ECO:0000269|PubMed:9452424"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2E1R"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2E1R"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1ZM9"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 171..192
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1N0V"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1N0V"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:3B82"
FT STRAND 379..390
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 394..406
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 501..514
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 535..547
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 564..569
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:1ZM9"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:1N0V"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:1N0V"
FT HELIX 612..621
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 627..631
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 642..648
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 656..672
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 683..692
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 702..719
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 722..735
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 740..748
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 766..773
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 780..787
FT /evidence="ECO:0007829|PDB:1N0U"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 793..803
FT /evidence="ECO:0007829|PDB:1N0U"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:2ZIT"
FT HELIX 814..825
FT /evidence="ECO:0007829|PDB:1N0U"
FT HELIX 835..838
FT /evidence="ECO:0007829|PDB:1N0U"
SQ SEQUENCE 842 AA; 93289 MW; FD2F8073CB9B66AA CRC64;
MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TIEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQVS KEDLYQTFAR
TVESVNVIVS TYADEVLGDV QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM
MDRLWGDSFF NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL
EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA YRAEQLYEGP
ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYVP
GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA GNIIGLVGID QFLLKTGTLT TSETAHNMKV
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI
CLQDLEHDHA GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA
IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT KAVQYLHEIK
DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR GGGQIIPTMR RATYAGFLLA
DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
TGELRQATGG QAFPQMVFDH WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD
KL
