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P49410

- EFTU_BOVIN

UniProt

P49410 - EFTU_BOVIN

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Protein
Elongation factor Tu, mitochondrial
Gene
TUFM
Organism
Bos taurus (Bovine)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 718GTP By similarity
Nucleotide bindingi126 – 1305GTP By similarity
Nucleotide bindingi181 – 1844GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTPase activity Source: InterPro
  3. translation elongation factor activity Source: UniProtKB

GO - Biological processi

  1. translational elongation Source: UniProtKB
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 Tu, mitochondrial
Short name:
EF-Tu
Gene namesi
Name:TUFM
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 25

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: AgBase
  2. mitochondrial nucleoid Source: Ensembl
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion
Add
BLAST
Chaini44 – 452409Elongation factor Tu, mitochondrial
PRO_0000007461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysine By similarity
Modified residuei88 – 881N6-acetyllysine By similarity
Modified residuei256 – 2561N6-acetyllysine By similarity
Modified residuei418 – 4181N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP49410.
PRIDEiP49410.

Interactioni

Protein-protein interaction databases

IntActiP49410. 1 interaction.
STRINGi9913.ENSBTAP00000025586.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 659
Helixi66 – 683
Helixi70 – 8314
Helixi92 – 965
Beta strandi100 – 1034
Beta strandi106 – 1094
Beta strandi111 – 1166
Beta strandi121 – 1266
Helixi130 – 13910
Beta strandi145 – 1528
Turni153 – 1553
Helixi159 – 17012
Beta strandi176 – 1816
Helixi183 – 1853
Helixi189 – 20517
Turni210 – 2123
Beta strandi215 – 2173
Helixi220 – 2245
Turni229 – 2324
Helixi233 – 24614
Beta strandi259 – 2613
Beta strandi264 – 2685
Turni269 – 2713
Beta strandi272 – 2787
Beta strandi281 – 2855
Beta strandi289 – 2946
Beta strandi297 – 30812
Beta strandi311 – 3177
Beta strandi321 – 3288
Helixi331 – 3333
Beta strandi339 – 3424
Beta strandi349 – 35810
Helixi361 – 3633
Beta strandi377 – 3804
Beta strandi383 – 3908
Beta strandi403 – 41412
Beta strandi421 – 4266
Beta strandi429 – 43810
Helixi444 – 4474

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2EX-ray1.94A/B/C/D55-451[»]
1XB2X-ray2.20A44-452[»]
ProteinModelPortaliP49410.
SMRiP49410. Positions 55-451.

Miscellaneous databases

EvolutionaryTraceiP49410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 251197tr-type G
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 718G1 By similarity
Regioni105 – 1095G2 By similarity
Regioni126 – 1294G3 By similarity
Regioni181 – 1844G4 By similarity
Regioni219 – 2213G5 By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0050.
GeneTreeiENSGT00550000074682.
HOGENOMiHOG000229290.
HOVERGENiHBG001535.
InParanoidiP49410.
KOiK02358.
OMAiDNRHYGH.
OrthoDBiEOG73BVCN.
TreeFamiTF300432.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. 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.
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.

P49410-1 [UniParc]FASTAAdd to Basket

« Hide

MAAATLLRAT PLFSGLGAGP APLLQGLLRP LKAQALPVLC RGLAVEAKKT    50
YVRDKPHVNV GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE 100
ERARGITINA AHVEYSTAAR HYAHTDCPGH ADYVKNMITG TAPLDGCILV 150
VAANDGPMPQ TREHLLLARQ IGVEHVVVYV NKADAVQDSE MVELVELEIR 200
ELLTEFGYKG EETPIIVGSA LCALEQRDPE LGLKSVQKLL DAVDTYIPVP 250
TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC EFLGHSKNIR 300
TVVTGIEMFH KSLDRAEAGD NLGALVRGLK REDLRRGLVM AKPGSIQPHQ 350
KVEAQVYILT KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPGKELAMP 400
GEDLKLTLIL RQPMILEKGQ RFTLRDGNRT IGTGLVTDTP AMTEEDKNIK 450
WS 452
Length:452
Mass (Da):49,398
Last modified:February 1, 1996 - v1
Checksum:i51031B10DA06A7F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271L → P.
Natural varianti355 – 3551Q → H.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L38996 mRNA. Translation: AAB00500.1.
BC120109 mRNA. Translation: AAI20110.1.
PIRiS62768.
RefSeqiNP_776632.1. NM_174207.2.
UniGeneiBt.53241.

Genome annotation databases

EnsembliENSBTAT00000025586; ENSBTAP00000025586; ENSBTAG00000019216.
GeneIDi281556.
KEGGibta:281556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L38996 mRNA. Translation: AAB00500.1 .
BC120109 mRNA. Translation: AAI20110.1 .
PIRi S62768.
RefSeqi NP_776632.1. NM_174207.2.
UniGenei Bt.53241.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D2E X-ray 1.94 A/B/C/D 55-451 [» ]
1XB2 X-ray 2.20 A 44-452 [» ]
ProteinModelPortali P49410.
SMRi P49410. Positions 55-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P49410. 1 interaction.
STRINGi 9913.ENSBTAP00000025586.

Proteomic databases

PaxDbi P49410.
PRIDEi P49410.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000025586 ; ENSBTAP00000025586 ; ENSBTAG00000019216 .
GeneIDi 281556.
KEGGi bta:281556.

Organism-specific databases

CTDi 7284.

Phylogenomic databases

eggNOGi COG0050.
GeneTreei ENSGT00550000074682.
HOGENOMi HOG000229290.
HOVERGENi HBG001535.
InParanoidi P49410.
KOi K02358.
OMAi DNRHYGH.
OrthoDBi EOG73BVCN.
TreeFami TF300432.

Miscellaneous databases

EvolutionaryTracei P49410.
NextBioi 20805507.
PROi P49410.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000795. 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 ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00485. EF-Tu. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiEFTU_BOVIN
AccessioniPrimary (citable) accession number: P49410
Secondary accession number(s): Q0VCL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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