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P85834

- EFTU_RAT

UniProt

P85834 - EFTU_RAT

Protein

Elongation factor Tu, mitochondrial

Gene

Tufm

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      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.By similarity

    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-KW

    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
    Gene namesi
    Name:TufmBy similarity
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi1305501. Tufm.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial nucleoid Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343MitochondrionBy similarityAdd
    BLAST
    Chaini44 – 452409Elongation factor Tu, mitochondrialPRO_0000339242Add
    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

    PaxDbiP85834.
    PRIDEiP85834.

    2D gel databases

    World-2DPAGE0004:P85834.

    Expressioni

    Gene expression databases

    GenevestigatoriP85834.

    Interactioni

    Protein-protein interaction databases

    IntActiP85834. 2 interactions.
    MINTiMINT-7139130.
    STRINGi10116.ENSRNOP00000025203.

    Structurei

    3D structure databases

    ProteinModelPortaliP85834.
    SMRiP85834. Positions 55-451.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    HOVERGENiHBG001535.
    KOiK02358.
    OMAiDNRHYGH.
    OrthoDBiEOG73BVCN.
    PhylomeDBiP85834.

    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.

    P85834-1 [UniParc]FASTAAdd to Basket

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    MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC RGLAVEAKKT    50
    YVRDKPHVNV GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE 100
    ERARGITINA AHVEYSTAAR HYAHTDCPGH ADYVKNMITG TAPLDGCILV 150
    VAANDGPMPQ TREHLLLAKQ IGVEHVVVYV NKADAVQDSE MVELVELEIR 200
    ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL DAVDTYIPVP 250
    TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR 300
    TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ 350
    KVEAQVYILS KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP 400
    GEDLKLSLIL RQPMILEKGQ RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK 450
    WS 452
    Length:452
    Mass (Da):49,522
    Last modified:June 10, 2008 - v1
    Checksum:i67C39530FE8EC7CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03000083 Genomic DNA. No translation available.
    RefSeqiNP_001099765.1. NM_001106295.1.
    UniGeneiRn.48850.

    Genome annotation databases

    EnsembliENSRNOT00000025203; ENSRNOP00000025203; ENSRNOG00000018604.
    GeneIDi293481.
    KEGGirno:293481.
    UCSCiRGD:1305501. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03000083 Genomic DNA. No translation available.
    RefSeqi NP_001099765.1. NM_001106295.1.
    UniGenei Rn.48850.

    3D structure databases

    ProteinModelPortali P85834.
    SMRi P85834. Positions 55-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P85834. 2 interactions.
    MINTi MINT-7139130.
    STRINGi 10116.ENSRNOP00000025203.

    2D gel databases

    World-2DPAGE 0004:P85834.

    Proteomic databases

    PaxDbi P85834.
    PRIDEi P85834.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025203 ; ENSRNOP00000025203 ; ENSRNOG00000018604 .
    GeneIDi 293481.
    KEGGi rno:293481.
    UCSCi RGD:1305501. rat.

    Organism-specific databases

    CTDi 7284.
    RGDi 1305501. Tufm.

    Phylogenomic databases

    eggNOGi COG0050.
    GeneTreei ENSGT00550000074682.
    HOVERGENi HBG001535.
    KOi K02358.
    OMAi DNRHYGH.
    OrthoDBi EOG73BVCN.
    PhylomeDBi P85834.

    Miscellaneous databases

    NextBioi 636196.
    PROi P85834.

    Gene expression databases

    Genevestigatori P85834.

    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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway1 Publication.
    2. "Proteome profile of the mature rat olfactory bulb."
      Maurya D.K., Sundaram C.S., Bhargava P.
      Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiEFTU_RAT
    AccessioniPrimary (citable) accession number: P85834
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 42 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3