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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 – 718GTPBy similarity
Nucleotide bindingi126 – 1305GTPBy similarity
Nucleotide bindingi181 – 1844GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl
  4. 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

Enzyme and pathway databases

ReactomeiREACT_271447. Mitochondrial translation elongation.

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. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: AgBase
  3. mitochondrial nucleoid Source: Ensembl
  4. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionAdd
BLAST
Chaini44 – 452409Elongation factor Tu, mitochondrialPRO_0000007461Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP49410.
PRIDEiP49410.

Interactioni

Protein-protein interaction databases

IntActiP49410. 1 interaction.
STRINGi9913.ENSBTAP00000025586.

Structurei

Secondary structure

1
452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 659Combined sources
Helixi66 – 683Combined sources
Helixi70 – 8314Combined sources
Helixi92 – 965Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi111 – 1166Combined sources
Beta strandi121 – 1266Combined sources
Helixi130 – 13910Combined sources
Beta strandi145 – 1528Combined sources
Turni153 – 1553Combined sources
Helixi159 – 17012Combined sources
Beta strandi176 – 1816Combined sources
Helixi183 – 1853Combined sources
Helixi189 – 20517Combined sources
Turni210 – 2123Combined sources
Beta strandi215 – 2173Combined sources
Helixi220 – 2245Combined sources
Turni229 – 2324Combined sources
Helixi233 – 24614Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi264 – 2685Combined sources
Turni269 – 2713Combined sources
Beta strandi272 – 2787Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi297 – 30812Combined sources
Beta strandi311 – 3177Combined sources
Beta strandi321 – 3288Combined sources
Helixi331 – 3333Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi349 – 35810Combined sources
Helixi361 – 3633Combined sources
Beta strandi377 – 3804Combined sources
Beta strandi383 – 3908Combined sources
Beta strandi403 – 41412Combined sources
Beta strandi421 – 4266Combined sources
Beta strandi429 – 43810Combined sources
Helixi444 – 4474Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP49410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 251197tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 718G1PROSITE-ProRule annotation
Regioni105 – 1095G2PROSITE-ProRule annotation
Regioni126 – 1294G3PROSITE-ProRule annotation
Regioni181 – 1844G4PROSITE-ProRule annotation
Regioni219 – 2213G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MAAATLLRAT PLFSGLGAGP APLLQGLLRP LKAQALPVLC RGLAVEAKKT
60 70 80 90 100
YVRDKPHVNV GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE
110 120 130 140 150
ERARGITINA AHVEYSTAAR HYAHTDCPGH ADYVKNMITG TAPLDGCILV
160 170 180 190 200
VAANDGPMPQ TREHLLLARQ IGVEHVVVYV NKADAVQDSE MVELVELEIR
210 220 230 240 250
ELLTEFGYKG EETPIIVGSA LCALEQRDPE LGLKSVQKLL DAVDTYIPVP
260 270 280 290 300
TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC EFLGHSKNIR
310 320 330 340 350
TVVTGIEMFH KSLDRAEAGD NLGALVRGLK REDLRRGLVM AKPGSIQPHQ
360 370 380 390 400
KVEAQVYILT KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPGKELAMP
410 420 430 440 450
GEDLKLTLIL RQPMILEKGQ RFTLRDGNRT IGTGLVTDTP AMTEEDKNIK

WS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

Enzyme and pathway databases

Reactomei REACT_271447. Mitochondrial translation elongation.

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: November 26, 2014
This is version 114 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