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P85834 (EFTU_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor Tu, mitochondrial
Gene names
Name:Tufm
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity. UniProtKB P49411

Subcellular location

Mitochondrion Ref.2.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion By similarity UniProtKB P49411
Chain44 – 452409Elongation factor Tu, mitochondrial UniProtKB P49411
PRO_0000339242

Regions

Nucleotide binding64 – 718GTP By similarity UniProtKB P49411
Nucleotide binding126 – 1305GTP By similarity UniProtKB P49411
Nucleotide binding181 – 1844GTP By similarity UniProtKB P49411

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue881N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine By similarity
Modified residue4181N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P85834 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 67C39530FE8EC7CD

FASTA45249,522
        10         20         30         40         50         60 
MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC RGLAVEAKKT YVRDKPHVNV 

        70         80         90        100        110        120 
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR 

       130        140        150        160        170        180 
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLAKQ IGVEHVVVYV 

       190        200        210        220        230        240 
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL 

       250        260        270        280        290        300 
DAVDTYIPVP TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR 

       310        320        330        340        350        360 
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ KVEAQVYILS 

       370        380        390        400        410        420 
KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP GEDLKLSLIL RQPMILEKGQ 

       430        440        450 
RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK WS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 Norway.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03000083 Genomic DNA. No translation available.
RefSeqNP_001099765.1. NM_001106295.1.
UniGeneRn.48850.

3D structure databases

ProteinModelPortalP85834.
SMRP85834. Positions 55-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP85834. 2 interactions.
MINTMINT-7139130.
STRING10116.ENSRNOP00000025203.

2D gel databases

World-2DPAGE0004:P85834.

Proteomic databases

PaxDbP85834.
PRIDEP85834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025203; ENSRNOP00000025203; ENSRNOG00000018604.
GeneID293481.
KEGGrno:293481.
UCSCRGD:1305501. rat.

Organism-specific databases

CTD7284.
RGD1305501. Tufm.

Phylogenomic databases

eggNOGCOG0050.
GeneTreeENSGT00550000074682.
HOVERGENHBG001535.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG73BVCN.
PhylomeDBP85834.

Gene expression databases

GenevestigatorP85834.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000795. 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]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio636196.
PROP85834.

Entry information

Entry nameEFTU_RAT
AccessionPrimary (citable) accession number: P85834
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families