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P49410

- EFTU_BOVIN

UniProt

P49410 - EFTU_BOVIN

Protein

Elongation factor Tu, mitochondrial

Gene

TUFM

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    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. translation elongation factor activity Source: UniProtKB

    GO - Biological processi

    1. translational elongation Source: UniProtKB

    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

    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 – 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.
    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

    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

    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: October 1, 2014
    This is version 112 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