P32324 (EF2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EFT1
Ordered Locus Names:	YOR133W
ORF Names:	O3317, YOR3317W
AND
Name:	EFT2
Ordered Locus Names:	YDR385W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	842 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.19
Enzyme regulation	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.
Pathway	Protein biosynthesis; polypeptide chain elongation.
Subunit structure	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. Ref.14 Ref.19
Subcellular location	Cytoplasm Ref.15.
Miscellaneous	Present with 160782 molecules/cell in log phase SD medium. There are 2 genes for eEF2 in yeast.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.010 mM for GTP

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding RNA-binding rRNA-binding
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC positive regulation of translational elongation Inferred from mutant phenotype PubMed 19338753. Source: SGD
Cellular_component	ribosome Traceable author statement PubMed 9841679. Source: SGD
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW translation elongation factor activity Traceable author statement PubMed 9841679. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPP0	P05317	2	EBI-6333,EBI-15447
SKP1	P52286	2	EBI-6333,EBI-4090

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 842

842

Elongation factor 2

PRO_0000091024

Regions

Nucleotide binding

26 – 33

8

GTP By similarity

Nucleotide binding

104 – 108

5

GTP By similarity

Nucleotide binding

158 – 161

4

GTP By similarity

Amino acid modifications

Modified residue

79

1

Phosphoserine Ref.17

Modified residue

82

1

Phosphoserine Ref.17

Modified residue

514

1

Phosphoserine Ref.17

Modified residue

569

1

Phosphoserine Ref.17

Modified residue

572

1

Phosphoserine Ref.17

Modified residue

699

1

Diphthamide

Modified residue

763

1

Phosphothreonine Ref.17

Experimental info

Mutagenesis

180

1

R → G: Causes resistance to fusidic acid and reduces sensitivity to sordarin. Ref.13

Mutagenesis

187

1

V → F: Causes resistance to fusidic acid and reduces sensitivity to sordarin. Ref.13

Mutagenesis

490

1

Q → E: Reduces sensitivity to sordarin. Ref.13

Mutagenesis

521

1

Y → D, N or S: Reduces sensitivity to fusidic acid and sordarin. Ref.13

Mutagenesis

523

1

S → F or P: Causes resistance to fusidic acid and sordarin. Ref.13

Mutagenesis

529

1

I → T: Reduces sensitivity to sordarin. Ref.13

Mutagenesis

559

1

P → L or R: Causes resistance to fusidic acid and sordarin. Ref.13

Mutagenesis

562

1

A → P: Reduces sensitivity to fusidic acid and causes resistance to sordarin. Ref.13

Mutagenesis

699

1

H → 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. Ref.12

Mutagenesis

701

1

G → R: Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. Ref.11

Mutagenesis

727

1

P → S: Causes resistance to sordarin. Ref.13

Mutagenesis

774

1

V → F: Causes resistance to sordarin. Ref.13

Mutagenesis

790

1

Missing: Causes resistance to fusidic acid and sordarin. Ref.13

Secondary structure

1

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842

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Helix

6 – 14

9

Helix

16 – 18

3

Beta strand

19 – 25

7

Helix

28 – 30

3

Helix

32 – 43

12

Beta strand

44 – 48

5

Beta strand

74 – 80

7

Helix

83 – 88

6

Beta strand

95 – 103

9

Helix

109 – 111

3

Helix

113 – 120

8

Beta strand

123 – 130

8

Turn

131 – 133

3

Helix

137 – 148

12

Beta strand

152 – 158

7

Helix

160 – 165

6

Helix

171 – 192

22

Helix

195 – 197

3

Helix

204 – 206

3

Beta strand

209 – 213

5

Turn

214 – 217

4

Beta strand

218 – 221

4

Helix

222 – 230

9

Turn

231 – 234

4

Helix

237 – 243

7

Beta strand

245 – 247

3

Beta strand

249 – 251

3

Turn

252 – 255

4

Beta strand

256 – 259

4

Beta strand

261 – 263

3

Turn

264 – 266

3

Helix

272 – 276

5

Helix

278 – 289

12

Helix

295 – 302

8

Helix

309 – 313

5

Helix

316 – 327

12

Helix

330 – 341

12

Helix

345 – 356

12

Beta strand

357 – 359

3

Helix

364 – 370

7

Beta strand

374 – 377

4

Beta strand

379 – 390

12

Beta strand

394 – 406

13

Beta strand

410 – 414

5

Beta strand

420 – 422

3

Beta strand

426 – 430

5

Beta strand

433 – 438

6

Beta strand

441 – 449

9

Beta strand

453 – 458

6

Turn

460 – 462

3

Beta strand

465 – 471

7

Beta strand

489 – 497

9

Helix

498 – 500

3

Helix

501 – 514

14

Beta strand

519 – 522

4

Beta strand

528 – 534

7

Helix

535 – 547

13

Beta strand

554 – 557

4

Beta strand

564 – 569

6

Beta strand

575 – 578

4

Beta strand

580 – 582

3

Beta strand

585 – 592

8

Helix

595 – 602

8

Beta strand

604 – 606

3

Beta strand

608 – 610

3

Helix

612 – 621

10

Helix

627 – 631

5

Beta strand

633 – 638

6

Turn

639 – 641

3

Beta strand

642 – 648

7

Helix

656 – 672

17

Turn

675 – 677

3

Beta strand

683 – 692

10

Helix

697 – 699

3

Helix

702 – 719

18

Beta strand

722 – 735

14

Helix

737 – 739

3

Helix

740 – 748

9

Turn

749 – 751

3

Beta strand

753 – 758

6

Beta strand

766 – 773

8

Helix

774 – 776

3

Helix

780 – 787

8

Turn

788 – 790

3

Beta strand

793 – 803

11

Beta strand

811 – 813

3

Helix

814 – 825

12

Helix

835 – 838

4

Sequences

	Sequence		Length	Mass (Da)
	P32324 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: FD2F8073CB9B66AA	FASTA	842	93,289
	10 20 30 40 50 60 MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR 70 80 90 100 110 120 KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI NLIDSPGHVD FSSEVTAALR 130 140 150 160 170 180 VTDGALVVVD TIEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQVS KEDLYQTFAR 190 200 210 220 230 240 TVESVNVIVS TYADEVLGDV QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM 250 260 270 280 290 300 MDRLWGDSFF NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL 310 320 330 340 350 360 EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA YRAEQLYEGP 370 380 390 400 410 420 ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYVP 430 440 450 460 470 480 GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA GNIIGLVGID QFLLKTGTLT TSETAHNMKV 490 500 510 520 530 540 MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI 550 560 570 580 590 600 CLQDLEHDHA GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA 610 620 630 640 650 660 IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT KAVQYLHEIK 670 680 690 700 710 720 DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR GGGQIIPTMR RATYAGFLLA 730 740 750 760 770 780 DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF 790 800 810 820 830 840 TGELRQATGG QAFPQMVFDH WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling." Perentesis J.P., Phan L.D., Laporte D.C., Livingston D.M., Bodley J.W. J. Biol. Chem. 267:1190-1197(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1 AND EFT2).
[2]	"Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames." Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W. Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1). Strain: ATCC 96604 / S288c / FY1679.
[3]	"DNA sequencing and analysis of 130 kb from yeast chromosome XV." Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W. Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT2). Strain: ATCC 204508 / S288c.
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1). Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION (EFT1 AND EFT2). Strain: ATCC 204508 / S288c.
[7]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 411-422 AND 505-513. Strain: ATCC 204508 / S288c.
[8]	"Phylogeny and evolution of medical species of Candida and related taxa: a multigenic analysis." Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G. J. Clin. Microbiol. 42:5624-5635(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-785.
[9]	"Isolation and properties of the trypsin-derived ADP-ribosyl peptide from diphtheria toxin-modified yeast elongation factor 2." Van Ness B.G., Howard J.B., Bodley J.W. J. Biol. Chem. 253:8687-8690(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 686-700, DIPHTHAMIDE AT HIS-699.
[10]	"Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endogenous kinase." Donovan M.G., Bodley J.W. FEBS Lett. 291:303-306(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"Expression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation factor 2 in Saccharomyces cerevisiae." Kimata Y., Harashima S., Kohno K. Biochem. Biophys. Res. Commun. 191:1145-1151(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLY-701.
[12]	"Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine precursor of diphthamide yields a functional protein that is resistant to diphtheria toxin." Phan L.D., Perentesis J.P., Bodley J.W. J. Biol. Chem. 268:8665-8668(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-699.
[13]	"Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis." Justice M.C., Hsu M.-J., Tse B., Ku T., Balkovec J., Schmatz D., Nielsen J. J. Biol. Chem. 273:3148-3151(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ARG-180; VAL-187; GLN-490; TYR-521; SER-523; ILE-529; PRO-559; ALA-562; PRO-727; VAL-774 AND GLY-790.
[14]	"Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components." Lalioti V.S., Perez-Fernandez J., Remacha M.A., Ballesta J.P.G. Mol. Microbiol. 46:719-729(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RPL0.
[15]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[16]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[17]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-82; SER-514; SER-569; SER-572 AND THR-763, MASS SPECTROMETRY.
[18]	"Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase." Joergensen R., Ortiz P.A., Carr-Schmid A., Nissen P., Kinzy T.G., Andersen G.R. Nat. Struct. Biol. 10:379-385(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SORDARIN.
[19]	"Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation." Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J. EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.7 ANGSTROMS) IN COMPLEX WITH 80S RIBOSOME AND SORDARIN, FUNCTION, INTERACTION WITH RPL9A; RPL12A; RPS23A; 18S RRNA AND 25S RRNA.
[20]	"Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae." Joergensen R., Yates S.P., Teal D.J., Nilsson J., Prentice G.A., Merrill A.R., Andersen G.R. J. Biol. Chem. 279:45919-45925(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ADP-RIBOSYLATED FORM IN COMPLEX WITH GDP AND SORDARIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

A41778.

RefSeq

NP_010673.1. NM_001180693.1.
NP_014776.1. NM_001183552.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N0U	X-ray	2.12	A	1-842	[»]
1N0V	X-ray	2.85	C/D	1-842	[»]
1S1H	electron microscopy	11.70	T	1-842	[»]
1U2R	X-ray	2.60	A	1-842	[»]
1ZM2	X-ray	3.07	A/C/E	1-842	[»]
1ZM3	X-ray	3.07	A/C/E	1-842	[»]
1ZM4	X-ray	2.90	A/C/E	1-842	[»]
1ZM9	X-ray	2.80	A/C/E	1-842	[»]
2E1R	X-ray	3.15	A	1-842	[»]
2NPF	X-ray	2.90	A/B	1-842	[»]
2P8W	electron microscopy	11.30	T	1-842	[»]
2P8X	electron microscopy	9.70	T	1-842	[»]
2P8Y	electron microscopy	11.70	T	1-842	[»]
2P8Z	electron microscopy	8.90	T	1-842	[»]
2ZIT	X-ray	3.00	A/C/E	1-842	[»]
3B78	X-ray	2.50	A/C/E	1-842	[»]
3B82	X-ray	2.35	A/C/E	1-842	[»]
3B8H	X-ray	2.50	A/C/E	1-842	[»]
3DNY	electron microscopy	12.60	T	1-842	[»]

ProteinModelPortal

P32324.

SMR

P32324. Positions 2-842.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4911N.

IntAct

P32324. 133 interactions.

MINT

MINT-516631.

STRING

4932.YDR385W.

2D gel databases

SWISS-2DPAGE

P32324.

Proteomic databases

PaxDb

P32324.

PRIDE

P32324.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR385W; YDR385W; YDR385W.
YOR133W; YOR133W; YOR133W.

GeneID

851993.
854301.

KEGG

sce:YDR385W.
sce:YOR133W.

Organism-specific databases

CYGD

YDR385w.
YOR133w.

SGD

S000005659. EFT1.
S000002793. EFT2.

Phylogenomic databases

eggNOG

COG0480.

GeneTree

ENSGT00620000088029.
ENSGT00620000088065.

HOGENOM

HOG000231589.

KO

K03234.

OMA

NRHNRFY.

OrthoDB

EOG4PZNFQ.

Enzyme and pathway databases

UniPathway

UPA00345.

Gene expression databases

Genevestigator

P32324.

GermOnline

YDR385W. Saccharomyces cerevisiae.
YOR133W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.
3.30.70.240. 1 hit.

InterPro

IPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Pfam

PF00679. EFG_C. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SMART

SM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]

SUPFAM

SSF54980. EFG_III_V. 2 hits.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3376.

EvolutionaryTrace

P32324.

NextBio

970163.

Entry information

Entry name

EF2_YEAST

Accession

Primary (citable) accession number: P32324
Secondary accession number(s): D6VT19, Q6JEF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program