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Protein

Elongation factor 1-alpha

Gene

tuf

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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 bindingi14 – 21GTPUniRule annotation8
Nucleotide bindingi89 – 93GTPUniRule annotation5
Nucleotide bindingi144 – 147GTPUniRule 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:PH1484
ORF Names:PHCC033
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 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_00000909901 – 428Elongation factor 1-alphaAdd BLAST428

Interactioni

Protein-protein interaction databases

STRINGi70601.PH1484.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 15Combined sources9
Helixi20 – 31Combined sources12
Helixi36 – 42Combined sources7
Helixi54 – 66Combined sources13
Helixi71 – 74Combined sources4
Beta strandi77 – 79Combined sources3
Beta strandi84 – 89Combined sources6
Beta strandi91 – 93Combined sources3
Helixi96 – 102Combined sources7
Beta strandi103 – 105Combined sources3
Beta strandi108 – 115Combined sources8
Turni116 – 118Combined sources3
Helixi122 – 133Combined sources12
Beta strandi138 – 144Combined sources7
Helixi146 – 149Combined sources4
Helixi153 – 170Combined sources18
Beta strandi177 – 179Combined sources3
Turni182 – 184Combined sources3
Turni186 – 188Combined sources3
Helixi203 – 208Combined sources6
Helixi216 – 218Combined sources3
Beta strandi222 – 231Combined sources10
Turni232 – 234Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi252 – 256Combined sources5
Helixi258 – 262Combined sources5
Beta strandi267 – 275Combined sources9
Beta strandi278 – 283Combined sources6
Beta strandi288 – 293Combined sources6
Helixi298 – 300Combined sources3
Beta strandi306 – 312Combined sources7
Beta strandi322 – 329Combined sources8
Beta strandi343 – 346Combined sources4
Beta strandi349 – 362Combined sources14
Turni364 – 366Combined sources3
Beta strandi369 – 373Combined sources5
Beta strandi382 – 391Combined sources10
Turni398 – 400Combined sources3
Helixi402 – 404Combined sources3
Beta strandi406 – 411Combined sources6
Beta strandi414 – 425Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WY9X-ray2.30A/B1-428[»]
3WYAX-ray2.35A1-428[»]
ProteinModelPortaliO59153.
SMRiO59153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 217tr-type GAdd BLAST213

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 21G1By similarity8
Regioni68 – 72G2By similarity5
Regioni89 – 92G3By similarity4
Regioni144 – 147G4By similarity4
Regioni181 – 183G5By 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.

O59153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKEKPHVNI VFIGHVDHGK STTIGRLLYD TGNIPETIIK KFEEMGEKGK
60 70 80 90 100
SFKFAWVMDR LKEERERGIT IDVAHTKFET PHRYITIIDA PGHRDFVKNM
110 120 130 140 150
ITGASQADAA VLVVAATDGV MPQTKEHAFL ARTLGIKHII VTINKMDMVN
160 170 180 190 200
YDQKVFEKVK AQVEKLLKTL GYKDFPVIPT SAWNGDNVVK KSDKMPWYNG
210 220 230 240 250
PTLIEALDQI PEPEKPIDKP LRIPIQDVYS IKGVGTVPVG RVETGKLKVG
260 270 280 290 300
DVVIFEPAST IFHKPIQGEV KSIEMHHEPL QEALPGDNIG FNVRGVSKND
310 320 330 340 350
IKRGDVAGHT DKPPTVVRTK DTFKAQIIVL NHPTAITVGY SPVLHAHTAQ
360 370 380 390 400
IPVRFEQILA KVDPRTGNIV EENPQFIKTG DSAIVVLRPM KPVVLEPVKE
410 420
IPQLGRFAIR DMGMTIAAGM VISIQKGE
Length:428
Mass (Da):47,525
Last modified:August 1, 1998 - v1
Checksum:i830379915E67E6EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30591.1.
PIRiG71023.
RefSeqiWP_010885563.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30591; BAA30591; BAA30591.
GeneIDi1443801.
KEGGipho:PH1484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30591.1.
PIRiG71023.
RefSeqiWP_010885563.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WY9X-ray2.30A/B1-428[»]
3WYAX-ray2.35A1-428[»]
ProteinModelPortaliO59153.
SMRiO59153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30591; BAA30591; BAA30591.
GeneIDi1443801.
KEGGipho:PH1484.

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_PYRHO
AccessioniPrimary (citable) accession number: O59153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 105 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

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.