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Protein

Elongation factor Tu-A

Gene

tufA

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 4 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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 26GTP8
Nucleotide bindingi82 – 86GTP5
Nucleotide bindingi137 – 140GTP4

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.5.3. 2305.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu-AUniRule annotation
Short name:
EF-Tu-AUniRule annotation
Gene namesi
Name:tufAUniRule annotation
Synonyms:tuf
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000914222 – 406Elongation factor Tu-AAdd BLAST405

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei395PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated on a threonine.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP60338.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-61168N.
IntActiP60338. 1 interactor.
STRINGi262724.TTC1734.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 18Combined sources7
Helixi21 – 23Combined sources3
Helixi25 – 39Combined sources15
Helixi48 – 51Combined sources4
Helixi55 – 60Combined sources6
Beta strandi67 – 72Combined sources6
Beta strandi77 – 82Combined sources6
Helixi87 – 89Combined sources3
Helixi90 – 97Combined sources8
Beta strandi101 – 108Combined sources8
Turni109 – 111Combined sources3
Helixi115 – 126Combined sources12
Beta strandi132 – 137Combined sources6
Helixi139 – 141Combined sources3
Helixi145 – 161Combined sources17
Turni166 – 168Combined sources3
Beta strandi171 – 173Combined sources3
Helixi176 – 185Combined sources10
Turni191 – 193Combined sources3
Helixi195 – 210Combined sources16
Beta strandi218 – 220Combined sources3
Beta strandi223 – 225Combined sources3
Beta strandi228 – 232Combined sources5
Turni233 – 235Combined sources3
Beta strandi236 – 242Combined sources7
Beta strandi245 – 249Combined sources5
Beta strandi253 – 262Combined sources10
Beta strandi264 – 273Combined sources10
Beta strandi279 – 282Combined sources4
Beta strandi286 – 291Combined sources6
Turni296 – 298Combined sources3
Beta strandi304 – 307Combined sources4
Beta strandi314 – 323Combined sources10
Helixi326 – 328Combined sources3
Beta strandi342 – 345Combined sources4
Beta strandi348 – 355Combined sources8
Beta strandi368 – 379Combined sources12
Beta strandi386 – 391Combined sources6
Beta strandi394 – 404Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIPX-ray3.00A/B/E/F2-406[»]
1EXMX-ray1.70A2-406[»]
4H9GX-ray1.93A2-406[»]
4LBVX-ray2.03A3-406[»]
4LBWX-ray1.74A3-406[»]
4LBYX-ray2.69A3-406[»]
4LBZX-ray2.22A3-406[»]
4LC0X-ray2.22A3-406[»]
ProteinModelPortaliP60338.
SMRiP60338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60338.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 215tr-type GAdd BLAST206

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 26G1By similarity8
Regioni61 – 65G2By similarity5
Regioni82 – 85G3By similarity4
Regioni137 – 140G4By similarity4
Regioni175 – 177G5By 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

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.

Family and domain databases

CDDicd03697. EFTU_II. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR033720. EFTU_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.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
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.
TIGRFAMsiTIGR00485. EF-Tu. 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.

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

P60338-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGEFVRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD
60 70 80 90 100
IDKAPEERAR GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM
110 120 130 140 150
DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL
160 170 180 190 200
VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHRNPKTR RGENEWVDKI
210 220 230 240 250
WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV
260 270 280 290 300
GDEVEIVGLA PETRRTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE
310 320 330 340 350
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV
360 370 380 390 400
TGVVQLPPGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV

VTKILE
Length:406
Mass (Da):44,782
Last modified:January 23, 2007 - v2
Checksum:iBA597518358269E4
GO

Sequence databases

PIRiS00229.
S17146.

Cross-referencesi

Sequence databases

PIRiS00229.
S17146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIPX-ray3.00A/B/E/F2-406[»]
1EXMX-ray1.70A2-406[»]
4H9GX-ray1.93A2-406[»]
4LBVX-ray2.03A3-406[»]
4LBWX-ray1.74A3-406[»]
4LBYX-ray2.69A3-406[»]
4LBZX-ray2.22A3-406[»]
4LC0X-ray2.22A3-406[»]
ProteinModelPortaliP60338.
SMRiP60338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61168N.
IntActiP60338. 1 interactor.
STRINGi262724.TTC1734.

Proteomic databases

PRIDEiP60338.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.

Enzyme and pathway databases

BRENDAi3.6.5.3. 2305.

Miscellaneous databases

EvolutionaryTraceiP60338.

Family and domain databases

CDDicd03697. EFTU_II. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR033720. EFTU_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.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
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.
TIGRFAMsiTIGR00485. EF-Tu. 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 nameiEFTU1_THETH
AccessioniPrimary (citable) accession number: P60338
Secondary accession number(s): P07157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1EXM.Curated

Keywords - Technical termi

3D-structure

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.