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P16521 (EF3A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 3A

Short name=EF-3
Short name=EF-3A
Alternative name(s):
Eukaryotic elongation factor 3
Short name=eEF3
Translation elongation factor 3A
Yeast elongation factor 3
Gene names
Name:YEF3
Synonyms:EFC1, TEF3, YEF3A
Ordered Locus Names:YLR249W
ORF Names:L9672.5
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1044 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis. Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied. Ref.8 Ref.9

Enzyme regulation

Inhibited by the translational inhibitors neomycin and alpha-sarcin, which suppress the ATPase activity. Ref.10

Pathway

Protein biosynthesis; polypeptide chain elongation.

Subunit structure

Monomer. Interacts with elongation factor 1A (eEF1A). Interacts through its N-terminus with 18S rRNA. Ref.12 Ref.14 Ref.16

Subcellular location

Cytoplasm Ref.17.

Miscellaneous

Present with 870578 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.

Contains 2 ABC transporter domains.

Contains 7 HEAT repeats.

Biophysicochemical properties

Kinetic parameters:

KM=0.126 mM for ATP Ref.10

KM=0.125 mM for GTP

Vmax=15.2 µmol/min/mg enzyme with ATP as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 10441043Elongation factor 3A
PRO_0000093458

Regions

Repeat5 – 4238HEAT 1
Repeat86 – 12338HEAT 2
Repeat125 – 16238HEAT 3
Repeat166 – 20338HEAT 4
Repeat205 – 24137HEAT 5
Repeat242 – 27938HEAT 6
Repeat285 – 32339HEAT 7
Domain426 – 641216ABC transporter 1
Domain667 – 993327ABC transporter 2
Nucleotide binding463 – 4708ATP 1 By similarity
Nucleotide binding701 – 7088ATP 2 By similarity
Compositional bias1009 – 103123Lys-rich (basic)

Amino acid modifications

Modified residue21N-acetylserine Ref.11 Ref.22
Modified residue6421Phosphoserine Ref.21
Modified residue9721Phosphothreonine Ref.20 Ref.21
Modified residue9741Phosphoserine Ref.21
Modified residue10391Phosphoserine Ref.19 Ref.20 Ref.21
Modified residue10401Phosphoserine Ref.19 Ref.20 Ref.21

Experimental info

Mutagenesis6501F → S: Reduces ATPase activity and interaction with eEF1A. Required for growth at 37 degrees Celsius and causes a 50% reduction of total protein synthesis at permissive temperatures. Ref.16
Sequence conflict1531I → F in AAA35232. Ref.1
Sequence conflict1531I → F no nucleotide entry Ref.2
Sequence conflict1531I → F in AAA35233. Ref.3
Sequence conflict3321V → L in AAA35232. Ref.1
Sequence conflict3321V → L no nucleotide entry Ref.2
Sequence conflict3321V → L in AAA35233. Ref.3

Secondary structure

......................................................................................................................................................................... 1044
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16521 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: 41E40B8BDD7A4C33

FASTA1,044115,945
        10         20         30         40         50         60 
MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF FGELAKGIKD 

        70         80         90        100        110        120 
KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG NKDKEIQSVA SETLISIVNA 

       130        140        150        160        170        180 
VNPVAIKALL PHLTNAIVET NKWQEKIAIL AAISAMVDAA KDQVALRMPE LIPVLSETMW 

       190        200        210        220        230        240 
DTKKEVKAAA TAAMTKATET VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT 

       250        260        270        280        290        300 
PATLSIMVPL LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT 

       310        320        330        340        350        360 
IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK DETVAPRFKI 

       370        380        390        400        410        420 
VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA KDILDEFRKR AVDNIPVGPN 

       430        440        450        460        470        480 
FDDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRARRYG ICGPNGCGKS TLMRAIANGQ 

       490        500        510        520        530        540 
VDGFPTQEEC RTVYVEHDID GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP 

       550        560        570        580        590        600 
ISALSGGWKM KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS 

       610        620        630        640        650        660 
VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF PEPGYLEGVK 

       670        680        690        700        710        720 
TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP 

       730        740        750        760        770        780 
TSGEVYTHEN CRIAYIKQHA FAHIESHLDK TPSEYIQWRF QTGEDRETMD RANRQINEND 

       790        800        810        820        830        840 
AEAMNKIFKI EGTPRRIAGI HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI 

       850        860        870        880        890        900 
PRGELVESHS KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG 

       910        920        930        940        950        960 
QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT HSAEFTKNLT 

       970        980        990       1000       1010       1020 
EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA MGNKIAGGKK KKKLSSAELR 

      1030       1040 
KKKKERMKKK KELGDAYVSS DEEF 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae."
Qin S., Xie A., Bonato M.C.M., McLaughlin C.S.
J. Biol. Chem. 265:1903-1912(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isolation and characterization of the structural gene encoding elongation factor 3."
Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.
Biochim. Biophys. Acta 1050:230-234(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3."
Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.
J. Biol. Chem. 265:15838-15844(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Detection and analysis of translation elongation factor 3 genes from various yeasts."
Uritani M., Shoumura Y., Yamada S.
Biosci. Biotechnol. Biochem. 63:769-772(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-955.
Strain: ATCC 208279 / BJ926.
[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 959-967.
Strain: ATCC 204508 / S288c.
[8]"Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae."
Dasmahapatra B., Chakraburtty K.
J. Biol. Chem. 256:9999-10004(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]"The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor."
Triana-Alonso F.J., Chakraburtty K., Nierhaus K.H.
J. Biol. Chem. 270:20473-20478(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Comparative analysis of ribosome-associated adenosinetriphosphatase (ATPase) from pig liver and the ATPase of elongation factor 3 from Saccharomyces cerevisiae."
Kovalchuke O., Chakraburtty K.
Eur. J. Biochem. 226:133-140(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[11]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2.
[12]"Competition and cooperation amongst yeast elongation factors."
Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K.
Eur. J. Biochem. 258:986-993(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EEF1A.
[13]"Identification and kinetic analysis of a functional homolog of elongation factor 3, YEF3 in Saccharomyces cerevisiae."
Sarthy A.V., McGonigal T., Capobianco J.O., Schmidt M., Green S.R., Moehle C.M., Goldman R.C.
Yeast 14:239-253(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[14]"The N-terminus of eukaryotic translation elongation factor 3 interacts with 18 S rRNA and 80 S ribosomes."
Gontarek R.R., Li H., Nurse K., Prescott C.D.
J. Biol. Chem. 273:10249-10252(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH 18S RRNA.
[15]"A sampling of the yeast proteome."
Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.
Mol. Cell. Biol. 19:7357-7368(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[16]"Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3."
Anand M., Chakraburtty K., Marton M.J., Hinnebusch A.G., Kinzy T.G.
J. Biol. Chem. 278:6985-6991(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-650, INTERACTION WITH EEF1A.
[17]"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].
[18]"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].
[19]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[20]"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 THR-972; SER-1039 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; THR-972; SER-974; SER-1039 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05197 Genomic DNA. Translation: AAA35232.1.
J05583 Genomic DNA. Translation: AAA35233.1.
U20865 Genomic DNA. Translation: AAB67391.1.
AB018539 Genomic DNA. Translation: BAA33897.1.
BK006945 Genomic DNA. Translation: DAA09563.1.
PIRDVBYE3. S59395.
RefSeqNP_013350.1. NM_001182136.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IW3X-ray2.40A/B2-980[»]
2IWHX-ray3.00A/B2-980[»]
2IX3X-ray2.70A/B2-980[»]
2IX8electron microscopy6.00A2-977[»]
ProteinModelPortalP16521.
SMRP16521. Positions 2-977.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31517. 134 interactions.
DIPDIP-2249N.
IntActP16521. 84 interactions.
MINTMINT-8285353.

Proteomic databases

PaxDbP16521.
PeptideAtlasP16521.
PRIDEP16521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR249W; YLR249W; YLR249W.
GeneID850951.
KEGGsce:YLR249W.

Organism-specific databases

SGDS000004239. YEF3.

Phylogenomic databases

eggNOGCOG0488.
GeneTreeENSGT00550000075671.
HOGENOMHOG000180957.
KOK03235.
OMAFPTQEEC.
OrthoDBEOG7Q2NDN.

Enzyme and pathway databases

BioCycYEAST:G3O-32354-MONOMER.
UniPathwayUPA00345.

Gene expression databases

GenevestigatorP16521.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
3.40.50.300. 4 hits.
InterProIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015688. Elongation_fac_3.
IPR021133. HEAT_type_2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR19211:SF5. PTHR19211:SF5. 1 hit.
PfamPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 6 hits.
SSF52540. SSF52540. 3 hits.
PROSITEPS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
PS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16521.
NextBio967419.

Entry information

Entry nameEF3A_YEAST
AccessionPrimary (citable) accession number: P16521
Secondary accession number(s): D6VYP7, O93815, Q06558
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways