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Protein

Elongation factor Tu

Gene

tuf

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: Annotation score: 3 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. 6334.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor TuUniRule annotation
Short name:
EF-TuUniRule annotation
Gene namesi
Name:tufUniRule annotation
Synonyms:tufA
OrganismiThermus aquaticus
Taxonomic identifieri271 [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 methionineiRemoved1 Publication
ChainiPRO_00000914202 – 406Elongation factor TuAdd BLAST405

Proteomic databases

PRIDEiQ01698.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi498848.TaqDRAFT_4960.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 18Combined sources7
Helixi25 – 37Combined sources13
Beta strandi41 – 43Combined sources3
Helixi48 – 50Combined sources3
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 – 125Combined sources11
Turni126 – 128Combined sources3
Beta strandi132 – 137Combined sources6
Helixi139 – 141Combined sources3
Helixi147 – 160Combined sources14
Turni161 – 163Combined sources3
Turni166 – 168Combined sources3
Beta strandi171 – 173Combined sources3
Helixi176 – 185Combined sources10
Turni191 – 193Combined sources3
Helixi195 – 210Combined sources16
Beta strandi218 – 220Combined sources3
Beta strandi223 – 232Combined sources10
Turni233 – 235Combined sources3
Beta strandi236 – 242Combined sources7
Beta strandi245 – 249Combined sources5
Beta strandi253 – 256Combined sources4
Beta strandi258 – 262Combined sources5
Beta strandi264 – 273Combined sources10
Beta strandi276 – 282Combined sources7
Beta strandi286 – 291Combined sources6
Turni296 – 298Combined sources3
Beta strandi304 – 307Combined sources4
Turni308 – 310Combined sources3
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
1B23X-ray2.60P2-406[»]
1EFTX-ray2.50A2-406[»]
1H1Umodel-B2-406[»]
1IPMmodel-I1-406[»]
1IPOmodel-G1-406[»]
1IPQmodel-F1-406[»]
1IPRmodel-G1-406[»]
1IPUmodel-H1-406[»]
1L1Umodel-11-406[»]
1MJ1electron microscopy13.00A2-406[»]
1OB5X-ray3.10A/C/E2-406[»]
1TTTX-ray2.70A/B/C2-406[»]
1TUIX-ray2.70A/B/C2-406[»]
ProteinModelPortaliQ01698.
SMRiQ01698.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01698.

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.

Q01698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGEFIRTK 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 EEMHKNPKTK RGENEWVDKI
210 220 230 240 250
WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV
260 270 280 290 300
GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGLL LRGVSREEVE
310 320 330 340 350
RGQVLAKPGS ITPHTKFEAS VYILKKEEGG RHTGFFTGYR PQFYFRTTDV
360 370 380 390 400
TGVVRLPQGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV

VTKILE
Length:406
Mass (Da):44,814
Last modified:January 23, 2007 - v2
Checksum:iA5E642800075E5D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66322 Genomic DNA. Translation: CAA46998.1.
PIRiS29293.
RefSeqiWP_003043841.1. NZ_LHCI01000106.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66322 Genomic DNA. Translation: CAA46998.1.
PIRiS29293.
RefSeqiWP_003043841.1. NZ_LHCI01000106.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B23X-ray2.60P2-406[»]
1EFTX-ray2.50A2-406[»]
1H1Umodel-B2-406[»]
1IPMmodel-I1-406[»]
1IPOmodel-G1-406[»]
1IPQmodel-F1-406[»]
1IPRmodel-G1-406[»]
1IPUmodel-H1-406[»]
1L1Umodel-11-406[»]
1MJ1electron microscopy13.00A2-406[»]
1OB5X-ray3.10A/C/E2-406[»]
1TTTX-ray2.70A/B/C2-406[»]
1TUIX-ray2.70A/B/C2-406[»]
ProteinModelPortaliQ01698.
SMRiQ01698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498848.TaqDRAFT_4960.

Proteomic databases

PRIDEiQ01698.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CGV. Bacteria.
COG0050. LUCA.

Enzyme and pathway databases

BRENDAi3.6.5.3. 6334.

Miscellaneous databases

EvolutionaryTraceiQ01698.

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 nameiEFTU_THEAQ
AccessioniPrimary (citable) accession number: Q01698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.