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P49410 (EFTU_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, mitochondrial

Short name=EF-Tu
Gene names
Name:TUFM
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Mitochondrion.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion
Chain44 – 452409Elongation factor Tu, mitochondrial
PRO_0000007461

Regions

Nucleotide binding64 – 718GTP By similarity
Nucleotide binding126 – 1305GTP By similarity
Nucleotide binding181 – 1844GTP By similarity

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue881N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine By similarity
Modified residue4181N6-acetyllysine By similarity

Natural variations

Natural variant271L → P.
Natural variant3551Q → H.

Secondary structure

.......................................................................... 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49410 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 51031B10DA06A7F9

FASTA45249,398
        10         20         30         40         50         60 
MAAATLLRAT PLFSGLGAGP APLLQGLLRP LKAQALPVLC RGLAVEAKKT YVRDKPHVNV 

        70         80         90        100        110        120 
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR 

       130        140        150        160        170        180 
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLARQ IGVEHVVVYV 

       190        200        210        220        230        240 
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPIIVGSA LCALEQRDPE LGLKSVQKLL 

       250        260        270        280        290        300 
DAVDTYIPVP TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC EFLGHSKNIR 

       310        320        330        340        350        360 
TVVTGIEMFH KSLDRAEAGD NLGALVRGLK REDLRRGLVM AKPGSIQPHQ KVEAQVYILT 

       370        380        390        400        410        420 
KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPGKELAMP GEDLKLTLIL RQPMILEKGQ 

       430        440        450 
RFTLRDGNRT IGTGLVTDTP AMTEEDKNIK WS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu."
Woriax V.L., Burkhart W.A., Spremulli L.L.
Biochim. Biophys. Acta 1264:347-356(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pons.
[3]"High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP."
Andersen G.R., Thirup S., Spremulli L.L., Nyborg J.
J. Mol. Biol. 297:421-436(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
[4]"Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex."
Jeppesen M.G., Navratil T., Spremulli L.L., Nyborg J.
J. Biol. Chem. 280:5071-5081(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH TSFM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38996 mRNA. Translation: AAB00500.1.
BC120109 mRNA. Translation: AAI20110.1.
PIRS62768.
RefSeqNP_776632.1. NM_174207.2.
UniGeneBt.53241.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2EX-ray1.94A/B/C/D55-451[»]
1XB2X-ray2.20A44-452[»]
ProteinModelPortalP49410.
SMRP49410. Positions 55-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49410. 1 interaction.
STRING9913.ENSBTAP00000025586.

Proteomic databases

PaxDbP49410.
PRIDEP49410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000025586; ENSBTAP00000025586; ENSBTAG00000019216.
GeneID281556.
KEGGbta:281556.

Organism-specific databases

CTD7284.

Phylogenomic databases

eggNOGCOG0050.
GeneTreeENSGT00550000074682.
HOGENOMHOG000229290.
HOVERGENHBG001535.
InParanoidP49410.
KOK02358.
OMADNRHYGH.
OrthoDBEOG73BVCN.
TreeFamTF300432.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
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.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49410.
NextBio20805507.
PROP49410.

Entry information

Entry nameEFTU_BOVIN
AccessionPrimary (citable) accession number: P49410
Secondary accession number(s): Q0VCL4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references