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Protein

Elongation factor 1-alpha

Gene

tuf

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 20GTPUniRule annotation8
Nucleotide bindingi90 – 94GTPUniRule annotation5
Nucleotide bindingi152 – 155GTPUniRule annotation4

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-alphaUniRule annotation
Short name:
EF-1-alphaUniRule annotation
Alternative name(s):
Elongation factor TuUniRule annotation
Short name:
EF-TuUniRule annotation
Gene namesi
Name:tufUniRule annotation
Ordered Locus Names:APE_1844
OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Taxonomic identifieri272557 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
Proteomesi
  • UP000002518 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000909741 – 437Elongation factor 1-alphaAdd BLAST437

Proteomic databases

PRIDEiQ9YAV0.

Interactioni

Protein-protein interaction databases

DIPiDIP-59399N.
STRINGi272557.APE_1844.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Helixi19 – 29Combined sources11
Helixi35 – 47Combined sources13
Helixi51 – 53Combined sources3
Helixi56 – 59Combined sources4
Helixi63 – 68Combined sources6
Beta strandi75 – 80Combined sources6
Beta strandi85 – 90Combined sources6
Helixi95 – 97Combined sources3
Helixi98 – 106Combined sources9
Beta strandi109 – 116Combined sources8
Helixi121 – 125Combined sources5
Helixi131 – 141Combined sources11
Beta strandi146 – 152Combined sources7
Turni157 – 161Combined sources5
Helixi163 – 179Combined sources17
Helixi184 – 186Combined sources3
Beta strandi189 – 191Combined sources3
Turni194 – 196Combined sources3
Turni198 – 200Combined sources3
Helixi215 – 220Combined sources6
Beta strandi234 – 236Combined sources3
Beta strandi238 – 243Combined sources6
Turni244 – 246Combined sources3
Beta strandi247 – 253Combined sources7
Beta strandi264 – 268Combined sources5
Turni269 – 271Combined sources3
Beta strandi272 – 281Combined sources10
Beta strandi284 – 289Combined sources6
Beta strandi294 – 300Combined sources7
Helixi304 – 306Combined sources3
Beta strandi312 – 318Combined sources7
Beta strandi322 – 332Combined sources11
Beta strandi346 – 349Combined sources4
Beta strandi352 – 365Combined sources14
Turni367 – 369Combined sources3
Beta strandi372 – 376Combined sources5
Beta strandi385 – 394Combined sources10
Turni401 – 403Combined sources3
Helixi405 – 407Combined sources3
Beta strandi408 – 414Combined sources7
Beta strandi417 – 429Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VMFX-ray2.30A1-437[»]
3WXMX-ray2.30A/C/E/G1-437[»]
4CXGelectron microscopy8.70A1-437[»]
4CXHelectron microscopy8.90A1-437[»]
ProteinModelPortaliQ9YAV0.
SMRiQ9YAV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 229tr-type GAdd BLAST226

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 20G1By similarity8
Regioni69 – 73G2By similarity5
Regioni90 – 93G3By similarity4
Regioni152 – 155G4By similarity4
Regioni193 – 195G5By similarity3

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01561. Archaea.
COG5256. LUCA.
HOGENOMiHOG000229291.
KOiK03231.
OMAiVNYDQKR.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9YAV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKPHMNLV VIGHVDHGKS TLVGHLLYRL GYIEEKKLKE LEEQAKSRGK
60 70 80 90 100
ESFKFAWILD KMKEERERGI TIDLTFMKFE TKKYVFTIID APGHRDFVKN
110 120 130 140 150
MITGASQADA AILVVSARKG EFEAGMSTEG QTREHLLLAR TMGIEQIIVA
160 170 180 190 200
VNKMDAPDVN YDQKRYEFVV SVLKKFMKGL GYQVDKIPFI PVSAWKGDNL
210 220 230 240 250
IERSPNMPWY NGPTLVEALD QLQPPAKPVD KPLRIPVQNV YSIPGAGTVP
260 270 280 290 300
VGRVETGVLR VGDKVVFMPP GVVGEVRSIE MHYQQLQQAE PGDNIGFAVR
310 320 330 340 350
GVSKSDIKRG DVAGHLDKPP TVAEEFEARI FVIWHPSAIT VGYTPVIHVH
360 370 380 390 400
TASVSSRIIE IKAKLDPKTG QVVEQNPQFL KAGDAAIVRF KPVKPLVVEK
410 420 430
FSEIPQLGRF AMRDMNRTVG IGIVTDVKPA KVDIKAK
Length:437
Mass (Da):48,663
Last modified:November 1, 1999 - v1
Checksum:iD6AE87FEB8AD003C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA80848.1.
PIRiC72570.

Genome annotation databases

EnsemblBacteriaiBAA80848; BAA80848; APE_1844.
KEGGiape:APE_1844.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA80848.1.
PIRiC72570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VMFX-ray2.30A1-437[»]
3WXMX-ray2.30A/C/E/G1-437[»]
4CXGelectron microscopy8.70A1-437[»]
4CXHelectron microscopy8.90A1-437[»]
ProteinModelPortaliQ9YAV0.
SMRiQ9YAV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59399N.
STRINGi272557.APE_1844.

Proteomic databases

PRIDEiQ9YAV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA80848; BAA80848; APE_1844.
KEGGiape:APE_1844.

Phylogenomic databases

eggNOGiarCOG01561. Archaea.
COG5256. LUCA.
HOGENOMiHOG000229291.
KOiK03231.
OMAiVNYDQKR.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEF1A_AERPE
AccessioniPrimary (citable) accession number: Q9YAV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.