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Protein

Elongation factor 3A

Gene

YEF3

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

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. Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells (PubMed:22888004).3 Publications

Enzyme regulationi

Inhibited by the translational inhibitors neomycin and alpha-sarcin, which suppress the ATPase activity.1 Publication

Kineticsi

  1. KM=0.126 mM for ATP1 Publication
  2. KM=0.125 mM for GTP1 Publication
  1. Vmax=15.2 µmol/min/mg enzyme with ATP as substrate1 Publication

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 bindingi463 – 470ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi701 – 708ATP 2PROSITE-ProRule annotation8

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • rRNA binding Source: UniProtKB-KW
  • translation elongation factor activity Source: SGD

GO - Biological processi

  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • translational elongation Source: SGD
  • translational termination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32354-MONOMER.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:YEF3
Synonyms:EFC1, TEF3, YEF3A
Ordered Locus Names:YLR249W
ORF Names:L9672.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR249W.
SGDiS000004239. YEF3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • cytosolic ribosome Source: SGD
  • polysomal ribosome Source: UniProtKB
  • ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi650F → 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. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000934582 – 1044Elongation factor 3AAdd BLAST1043

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei187N6,N6,N6-trimethyllysine1 Publication1
Modified residuei196N6,N6,N6-trimethyllysine1 Publication1
Cross-linki350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei642PhosphoserineCombined sources1
Modified residuei789N6,N6,N6-trimethyllysine1 Publication1
Modified residuei972PhosphothreonineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei1039PhosphoserineCombined sources1
Modified residuei1040PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16521.
PRIDEiP16521.

PTM databases

iPTMnetiP16521.

Interactioni

Subunit structurei

Monomer. Interacts with elongation factor 1A (eEF1A). Interacts through its N-terminus with 18S rRNA. Associates with ribosomes (PubMed:22888004).4 Publications

Protein-protein interaction databases

BioGridi31517. 133 interactors.
DIPiDIP-2249N.
IntActiP16521. 84 interactors.
MINTiMINT-8285353.

Structurei

Secondary structure

11044
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Turni23 – 25Combined sources3
Helixi26 – 37Combined sources12
Beta strandi42 – 45Combined sources4
Helixi48 – 58Combined sources11
Helixi61 – 74Combined sources14
Turni77 – 79Combined sources3
Turni82 – 84Combined sources3
Helixi85 – 89Combined sources5
Helixi92 – 98Combined sources7
Helixi104 – 120Combined sources17
Helixi123 – 125Combined sources3
Helixi126 – 139Combined sources14
Helixi143 – 159Combined sources17
Helixi161 – 178Combined sources18
Helixi184 – 197Combined sources14
Helixi198 – 200Combined sources3
Turni204 – 206Combined sources3
Helixi207 – 209Combined sources3
Helixi210 – 218Combined sources9
Helixi222 – 230Combined sources9
Helixi241 – 255Combined sources15
Beta strandi257 – 259Combined sources3
Helixi260 – 274Combined sources15
Helixi280 – 283Combined sources4
Helixi284 – 289Combined sources6
Helixi291 – 297Combined sources7
Turni298 – 300Combined sources3
Helixi304 – 321Combined sources18
Turni325 – 327Combined sources3
Helixi338 – 348Combined sources11
Turni349 – 351Combined sources3
Helixi356 – 358Combined sources3
Helixi359 – 374Combined sources16
Helixi380 – 386Combined sources7
Helixi388 – 391Combined sources4
Turni392 – 394Combined sources3
Helixi397 – 413Combined sources17
Beta strandi426 – 428Combined sources3
Beta strandi430 – 440Combined sources11
Beta strandi443 – 454Combined sources12
Beta strandi458 – 462Combined sources5
Helixi469 – 478Combined sources10
Turni487 – 489Combined sources3
Beta strandi492 – 494Combined sources3
Helixi508 – 513Combined sources6
Turni514 – 516Combined sources3
Helixi520 – 529Combined sources10
Helixi534 – 538Combined sources5
Helixi541 – 543Combined sources3
Helixi546 – 559Combined sources14
Beta strandi563 – 569Combined sources7
Turni570 – 573Combined sources4
Helixi576 – 588Combined sources13
Beta strandi591 – 596Combined sources6
Helixi600 – 606Combined sources7
Beta strandi608 – 614Combined sources7
Beta strandi617 – 623Combined sources7
Helixi625 – 631Combined sources7
Helixi633 – 637Combined sources5
Beta strandi638 – 640Combined sources3
Turni641 – 643Combined sources3
Beta strandi664 – 674Combined sources11
Beta strandi679 – 681Combined sources3
Beta strandi683 – 692Combined sources10
Beta strandi696 – 699Combined sources4
Helixi705 – 714Combined sources10
Beta strandi721 – 727Combined sources7
Beta strandi733 – 736Combined sources4
Helixi738 – 743Combined sources6
Helixi744 – 746Combined sources3
Helixi752 – 759Combined sources8
Turni760 – 762Combined sources3
Turni766 – 772Combined sources7
Helixi783 – 785Combined sources3
Beta strandi788 – 790Combined sources3
Beta strandi793 – 806Combined sources14
Beta strandi809 – 821Combined sources13
Beta strandi828 – 831Combined sources4
Helixi834 – 836Combined sources3
Beta strandi838 – 841Combined sources4
Helixi842 – 844Combined sources3
Helixi846 – 863Combined sources18
Helixi872 – 881Combined sources10
Helixi886 – 891Combined sources6
Helixi894 – 896Combined sources3
Helixi899 – 911Combined sources13
Beta strandi916 – 921Combined sources6
Helixi923 – 925Combined sources3
Helixi929 – 940Combined sources12
Beta strandi943 – 949Combined sources7
Helixi953 – 956Combined sources4
Turni957 – 959Combined sources3
Beta strandi962 – 964Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IW3X-ray2.40A/B2-981[»]
2IWHX-ray3.00A/B2-981[»]
2IX3X-ray2.70A/B2-981[»]
2IX8electron microscopy6.00A2-977[»]
ProteinModelPortaliP16521.
SMRiP16521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16521.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati5 – 42HEAT 1Add BLAST38
Repeati86 – 123HEAT 2Add BLAST38
Repeati125 – 162HEAT 3Add BLAST38
Repeati166 – 203HEAT 4Add BLAST38
Repeati205 – 241HEAT 5Add BLAST37
Repeati242 – 279HEAT 6Add BLAST38
Repeati285 – 323HEAT 7Add BLAST39
Domaini426 – 641ABC transporter 1PROSITE-ProRule annotationAdd BLAST216
Domaini667 – 993ABC transporter 2PROSITE-ProRule annotationAdd BLAST327

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1009 – 1031Lys-rich (basic)Add BLAST23

Domaini

The heat repeats and the C-terminal domain are necessary for impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase activity in amino acid-starved or repleted cells (PubMed:22888004).1 Publication

Sequence similaritiesi

Contains 2 ABC transporter domains.PROSITE-ProRule annotation
Contains 7 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000075671.
HOGENOMiHOG000180957.
InParanoidiP16521.
KOiK03235.
OMAiELMETHS.
OrthoDBiEOG092C22OB.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR003593. 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]
PANTHERiPTHR19211:SF5. PTHR19211:SF5. 2 hits.
PfamiPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF52540. SSF52540. 3 hits.
PROSITEiPS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
PS50077. HEAT_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16521-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF
60 70 80 90 100
FGELAKGIKD KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG
110 120 130 140 150
NKDKEIQSVA SETLISIVNA VNPVAIKALL PHLTNAIVET NKWQEKIAIL
160 170 180 190 200
AAISAMVDAA KDQVALRMPE LIPVLSETMW DTKKEVKAAA TAAMTKATET
210 220 230 240 250
VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT PATLSIMVPL
260 270 280 290 300
LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT
310 320 330 340 350
IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK
360 370 380 390 400
DETVAPRFKI VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA
410 420 430 440 450
KDILDEFRKR AVDNIPVGPN FDDEEDEGED LCNCEFSLAY GAKILLNKTQ
460 470 480 490 500
LRLKRARRYG ICGPNGCGKS TLMRAIANGQ VDGFPTQEEC RTVYVEHDID
510 520 530 540 550
GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP ISALSGGWKM
560 570 580 590 600
KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS
610 620 630 640 650
VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF
660 670 680 690 700
PEPGYLEGVK TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI
710 720 730 740 750
GPNGAGKSTL INVLTGELLP TSGEVYTHEN CRIAYIKQHA FAHIESHLDK
760 770 780 790 800
TPSEYIQWRF QTGEDRETMD RANRQINEND AEAMNKIFKI EGTPRRIAGI
810 820 830 840 850
HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI PRGELVESHS
860 870 880 890 900
KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG
910 920 930 940 950
QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT
960 970 980 990 1000
HSAEFTKNLT EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA
1010 1020 1030 1040
MGNKIAGGKK KKKLSSAELR KKKKERMKKK KELGDAYVSS DEEF
Length:1,044
Mass (Da):115,945
Last modified:October 5, 2010 - v4
Checksum:i41E40B8BDD7A4C33
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti153I → F in AAA35232 (PubMed:2404974).Curated1
Sequence conflicti153I → F no nucleotide entry (PubMed:1976386).Curated1
Sequence conflicti153I → F in AAA35233 (PubMed:2203789).Curated1
Sequence conflicti332V → L in AAA35232 (PubMed:2404974).Curated1
Sequence conflicti332V → L no nucleotide entry (PubMed:1976386).Curated1
Sequence conflicti332V → L in AAA35233 (PubMed:2203789).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS59395. DVBYE3.
RefSeqiNP_013350.1. NM_001182136.1.

Genome annotation databases

EnsemblFungiiYLR249W; YLR249W; YLR249W.
GeneIDi850951.
KEGGisce:YLR249W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS59395. DVBYE3.
RefSeqiNP_013350.1. NM_001182136.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IW3X-ray2.40A/B2-981[»]
2IWHX-ray3.00A/B2-981[»]
2IX3X-ray2.70A/B2-981[»]
2IX8electron microscopy6.00A2-977[»]
ProteinModelPortaliP16521.
SMRiP16521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31517. 133 interactors.
DIPiDIP-2249N.
IntActiP16521. 84 interactors.
MINTiMINT-8285353.

PTM databases

iPTMnetiP16521.

Proteomic databases

MaxQBiP16521.
PRIDEiP16521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR249W; YLR249W; YLR249W.
GeneIDi850951.
KEGGisce:YLR249W.

Organism-specific databases

EuPathDBiFungiDB:YLR249W.
SGDiS000004239. YEF3.

Phylogenomic databases

GeneTreeiENSGT00550000075671.
HOGENOMiHOG000180957.
InParanoidiP16521.
KOiK03235.
OMAiELMETHS.
OrthoDBiEOG092C22OB.

Enzyme and pathway databases

UniPathwayiUPA00345.
BioCyciYEAST:G3O-32354-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP16521.
PROiP16521.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR003593. 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]
PANTHERiPTHR19211:SF5. PTHR19211:SF5. 2 hits.
PfamiPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF52540. SSF52540. 3 hits.
PROSITEiPS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
PS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEF3A_YEAST
AccessioniPrimary (citable) accession number: P16521
Secondary accession number(s): D6VYP7, O93815, Q06558
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 5, 2010
Last modified: November 2, 2016
This is version 187 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 870578 molecules/cell in log phase SD medium.1 Publication

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.