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Protein

Elongation factor Ts, mitochondrial

Gene

TSFM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Ts, mitochondrialUniRule annotation
Short name:
EF-TsUniRule annotation
Short name:
EF-TsMtUniRule annotation
Gene namesi
Name:TSFMUniRule annotation
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555MitochondrionAdd
BLAST
Chaini56 – 338283Elongation factor Ts, mitochondrialPRO_0000007467Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891N6-succinyllysineBy similarity
Modified residuei146 – 1461N6-succinyllysineBy similarity
Modified residuei205 – 2051N6-succinyllysineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP43896.
PRIDEiP43896.

Interactioni

Protein-protein interaction databases

IntActiP43896. 1 interaction.
STRINGi9913.ENSBTAP00000022496.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 7014Combined sources
Helixi74 – 8310Combined sources
Turni84 – 863Combined sources
Helixi88 – 11023Combined sources
Beta strandi117 – 1259Combined sources
Beta strandi128 – 13710Combined sources
Helixi139 – 1424Combined sources
Helixi145 – 16218Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi173 – 1775Combined sources
Helixi179 – 1835Combined sources
Beta strandi189 – 1913Combined sources
Helixi195 – 20612Combined sources
Beta strandi210 – 21910Combined sources
Beta strandi224 – 2329Combined sources
Beta strandi243 – 25412Combined sources
Helixi259 – 2613Combined sources
Helixi263 – 27614Combined sources
Helixi290 – 2923Combined sources
Helixi296 – 2983Combined sources
Helixi309 – 3135Combined sources
Helixi314 – 3163Combined sources
Beta strandi319 – 3279Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XB2X-ray2.20B56-338[»]
ProteinModelPortaliP43896.
SMRiP43896. Positions 56-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43896.

Family & Domainsi

Sequence similaritiesi

Belongs to the EF-Ts family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1071. Eukaryota.
COG0264. LUCA.
GeneTreeiENSGT00390000016293.
HOGENOMiHOG000220988.
HOVERGENiHBG005571.
InParanoidiP43896.
KOiK02357.
OMAiVKVPSGF.
OrthoDBiEOG73JKVZ.
TreeFamiTF314154.

Family and domain databases

Gene3Di3.30.479.20. 2 hits.
HAMAPiMF_00050. EF_Ts.
InterProiIPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR11741. PTHR11741. 1 hit.
PfamiPF00889. EF_TS. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
PROSITEiPS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLRSLRLC LVARTGSCPL SALGPGPLLP SLQAGLPLLQ SPQQWHTFHS
60 70 80 90 100
GSWLSSASSK ELLMKLRRKT GYSFINCKKA LETCGGDLKQ AESWLHKQAQ
110 120 130 140 150
KEGWSKAARL HGRKTKEGLI GLLQEGDTTV LVEVNCETDF VSRNLKFQQL
160 170 180 190 200
VQQVALGTLL HCQNLKDQLS TYSKGFLNSS ELSELPAGPE REGSLKDQLA
210 220 230 240 250
LAIGKLGENM ILKRAAWVKV PAGFYVGSYV HGAMHSPSLH NLVLGKYGAL
260 270 280 290 300
VICETSELKA NLADLGRRLG QHVVGMAPLS VGSLDDEPGG EAETKMLSQP
310 320 330
YLLDPSITLG QYVQPHGVSV VDFVRFECGE GEDAADAE
Length:338
Mass (Da):36,602
Last modified:November 1, 1995 - v1
Checksum:i449236159482DD68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37935 mRNA. Translation: AAA96807.1.
BC149988 mRNA. Translation: AAI49989.1.
PIRiI45941.
RefSeqiNP_776629.1. NM_174204.3.
UniGeneiBt.103027.

Genome annotation databases

EnsembliENSBTAT00000022496; ENSBTAP00000022496; ENSBTAG00000016912.
GeneIDi281551.
KEGGibta:281551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37935 mRNA. Translation: AAA96807.1.
BC149988 mRNA. Translation: AAI49989.1.
PIRiI45941.
RefSeqiNP_776629.1. NM_174204.3.
UniGeneiBt.103027.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XB2X-ray2.20B56-338[»]
ProteinModelPortaliP43896.
SMRiP43896. Positions 56-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP43896. 1 interaction.
STRINGi9913.ENSBTAP00000022496.

Proteomic databases

PaxDbiP43896.
PRIDEiP43896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022496; ENSBTAP00000022496; ENSBTAG00000016912.
GeneIDi281551.
KEGGibta:281551.

Organism-specific databases

CTDi10102.

Phylogenomic databases

eggNOGiKOG1071. Eukaryota.
COG0264. LUCA.
GeneTreeiENSGT00390000016293.
HOGENOMiHOG000220988.
HOVERGENiHBG005571.
InParanoidiP43896.
KOiK02357.
OMAiVKVPSGF.
OrthoDBiEOG73JKVZ.
TreeFamiTF314154.

Miscellaneous databases

EvolutionaryTraceiP43896.
NextBioi20805502.

Family and domain databases

Gene3Di3.30.479.20. 2 hits.
HAMAPiMF_00050. EF_Ts.
InterProiIPR001816. Transl_elong_EFTs/EF1B.
IPR014039. Transl_elong_EFTs/EF1B_dimer.
IPR018101. Transl_elong_Ts_CS.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR11741. PTHR11741. 1 hit.
PfamiPF00889. EF_TS. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54713. SSF54713. 2 hits.
PROSITEiPS01126. EF_TS_1. 1 hit.
PS01127. EF_TS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of mitochondrial translational elongation factor Ts from bovine and human liver."
    Xin H., Woriax V., Burkhart W., Spremulli L.L.
    J. Biol. Chem. 270:17243-17249(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.
  3. "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) OF 56-338 IN COMPLEX WITH TUFM.

Entry informationi

Entry nameiEFTS_BOVIN
AccessioniPrimary (citable) accession number: P43896
Secondary accession number(s): A6QQT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 120 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.