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P85834

- EFTU_RAT

UniProt

P85834 - EFTU_RAT

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Protein

Elongation factor Tu, mitochondrial

Gene

Tufm

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 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.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. poly(A) RNA binding Source: Ensembl
  4. translation elongation factor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_270070. Mitochondrial translation elongation.

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. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial nucleoid Source: Ensembl
Complete GO annotation...

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

BioGridi254286. 1 interaction.
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.
InParanoidiP85834.
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

« Hide

        10         20         30         40         50
MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC 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 TREHLLLAKQ IGVEHVVVYV NKADAVQDSE MVELVELEIR
210 220 230 240 250
ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL DAVDTYIPVP
260 270 280 290 300
TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR
310 320 330 340 350
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ
360 370 380 390 400
KVEAQVYILS KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP
410 420 430 440 450
GEDLKLSLIL RQPMILEKGQ RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK

WS
Length:452
Mass (Da):49,522
Last modified:June 10, 2008 - v1
Checksum:i67C39530FE8EC7CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

BioGridi 254286. 1 interaction.
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.
InParanoidi P85834.
KOi K02358.
OMAi DNRHYGH.
OrthoDBi EOG73BVCN.
PhylomeDBi P85834.

Enzyme and pathway databases

Reactomei REACT_270070. Mitochondrial translation elongation.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 44 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