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Q1IX70 (EFTU_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor Tu

Short name=EF-Tu
Gene names
Name:tuf1
Ordered Locus Names:Dgeo_0646
AND
Name:tuf2
Ordered Locus Names:Dgeo_1869
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity. HAMAP-Rule MF_00118

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00118.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000337370

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding82 – 865GTP By similarity
Nucleotide binding137 – 1404GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IX70 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: C9F815B644937456

FASTA40544,215
        10         20         30         40         50         60 
MAKGTFERTK PHVNVGTIGH VDHGKTTLTA AITFTAAAMD PTVEKLAYDQ IDKAPEEKAR 

        70         80         90        100        110        120 
GITINTAHVE YNTPARHYSH VDCPGHADYV KNMITGAAQM DGAILVVSSA DGPMPQTREH 

       130        140        150        160        170        180 
ILLARQVGVP YIVVFMNKVD MVDDEELLEL VEMEVRELLS KYEFPGDDLP VIKGSALQAL 

       190        200        210        220        230        240 
EALQQNPKTA RGENPWVDKI WELLDAIDAY IPTPERATDK TFLMPVEDVF TITGRGTVAT 

       250        260        270        280        290        300 
GRVERGVCKV GDEVEIVGLR DTKKTTITGV EMHRKLLDQG MAGDNVGVLL RGVARDDVER 

       310        320        330        340        350        360 
GQVLAKPGSI TPHTKFEASV YVLSKDEGGR HSAFFGGYRP QFYFRTTDVT GVVELPAGVE 

       370        380        390        400 
MVMPGDNVSF TVELIKPIAM EEGLRFAIRE GGRTVGAGVV TKVLE 

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000359 Genomic DNA. Translation: ABF44948.1.
CP000359 Genomic DNA. Translation: ABF46164.1.
RefSeqYP_604117.1. NC_008025.1.
YP_605333.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IX70.
SMRQ1IX70. Positions 10-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319795.Dgeo_1869.

Proteomic databases

PRIDEQ1IX70.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF44948; ABF44948; Dgeo_0646.
ABF46164; ABF46164; Dgeo_1869.
GeneID4057611.
4058995.
KEGGdge:Dgeo_0646.
dge:Dgeo_1869.
PATRIC21623143. VBIDeiGeo41128_1212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAGTEMCMP.
OrthoDBEOG6R5C6X.

Enzyme and pathway databases

BioCycDGEO319795:GHMU-1904-MONOMER.
DGEO319795:GHMU-664-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFTU_DEIGD
AccessionPrimary (citable) accession number: Q1IX70
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families