Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elongation factor Tu, mitochondrial

Gene

TUFM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi64 – 71GTPBy similarity8
Nucleotide bindingi126 – 130GTPBy similarity5
Nucleotide bindingi181 – 184GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: Ensembl
  • translation elongation factor activity Source: UniProtKB

GO - Biological processi

  • mitochondrial translational elongation Source: GO_Central
  • 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

ReactomeiR-BTA-5389840. 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
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 43MitochondrionAdd BLAST43
ChainiPRO_000000746144 – 452Elongation factor Tu, mitochondrialAdd BLAST409

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79N6-acetyllysineBy similarity1
Modified residuei88N6-acetyllysineBy similarity1
Modified residuei256N6-acetyllysineBy similarity1
Modified residuei278PhosphothreonineBy similarity1
Modified residuei418N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP49410.
PeptideAtlasiP49410.
PRIDEiP49410.

Expressioni

Gene expression databases

BgeeiENSBTAG00000019216.

Interactioni

Protein-protein interaction databases

IntActiP49410. 1 interactor.
STRINGi9913.ENSBTAP00000025586.

Structurei

Secondary structure

1452
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi57 – 65Combined sources9
Helixi66 – 68Combined sources3
Helixi70 – 83Combined sources14
Helixi92 – 96Combined sources5
Beta strandi100 – 103Combined sources4
Beta strandi106 – 109Combined sources4
Beta strandi111 – 116Combined sources6
Beta strandi121 – 126Combined sources6
Helixi130 – 139Combined sources10
Beta strandi145 – 152Combined sources8
Turni153 – 155Combined sources3
Helixi159 – 170Combined sources12
Beta strandi176 – 181Combined sources6
Helixi183 – 185Combined sources3
Helixi189 – 205Combined sources17
Turni210 – 212Combined sources3
Beta strandi215 – 217Combined sources3
Helixi220 – 224Combined sources5
Turni229 – 232Combined sources4
Helixi233 – 246Combined sources14
Beta strandi259 – 261Combined sources3
Beta strandi264 – 268Combined sources5
Turni269 – 271Combined sources3
Beta strandi272 – 278Combined sources7
Beta strandi281 – 285Combined sources5
Beta strandi289 – 294Combined sources6
Beta strandi297 – 308Combined sources12
Beta strandi311 – 317Combined sources7
Beta strandi321 – 328Combined sources8
Helixi331 – 333Combined sources3
Beta strandi339 – 342Combined sources4
Beta strandi349 – 358Combined sources10
Helixi361 – 363Combined sources3
Beta strandi377 – 380Combined sources4
Beta strandi383 – 390Combined sources8
Beta strandi403 – 414Combined sources12
Beta strandi421 – 426Combined sources6
Beta strandi429 – 438Combined sources10
Helixi444 – 447Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP49410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 251tr-type GPROSITE-ProRule annotationAdd BLAST197

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 71G1PROSITE-ProRule annotation8
Regioni105 – 109G2PROSITE-ProRule annotation5
Regioni126 – 129G3PROSITE-ProRule annotation4
Regioni181 – 184G4PROSITE-ProRule annotation4
Regioni219 – 221G5PROSITE-ProRule annotation3

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

eggNOGiKOG0460. Eukaryota.
COG0050. LUCA.
GeneTreeiENSGT00550000074682.
HOGENOMiHOG000229290.
HOVERGENiHBG001535.
InParanoidiP49410.
KOiK02358.
OMAiYSTATRH.
OrthoDBiEOG091G0BFD.
TreeFamiTF300432.

Family and domain databases

CDDicd03697. EFTU_II. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR033720. EFTU_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
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.
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)DescriptionActionsGraphical viewLength
Natural varianti27L → P.1
Natural varianti355Q → H.1

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.
PIRiS62768.
RefSeqiNP_776632.1. NM_174207.2.
UniGeneiBt.53241.

3D structure databases

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

Protein-protein interaction databases

IntActiP49410. 1 interactor.
STRINGi9913.ENSBTAP00000025586.

Proteomic databases

PaxDbiP49410.
PeptideAtlasiP49410.
PRIDEiP49410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7284.

Phylogenomic databases

eggNOGiKOG0460. Eukaryota.
COG0050. LUCA.
GeneTreeiENSGT00550000074682.
HOGENOMiHOG000229290.
HOVERGENiHBG001535.
InParanoidiP49410.
KOiK02358.
OMAiYSTATRH.
OrthoDBiEOG091G0BFD.
TreeFamiTF300432.

Enzyme and pathway databases

ReactomeiR-BTA-5389840. Mitochondrial translation elongation.

Miscellaneous databases

EvolutionaryTraceiP49410.

Gene expression databases

BgeeiENSBTAG00000019216.

Family and domain databases

CDDicd03697. EFTU_II. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR033720. EFTU_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
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.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 130 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

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.