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P02992 (EFTU_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Alternative name(s):
tufM
Gene names
Name:TUF1
Synonyms:TUFM
Ordered Locus Names:YOR187W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

G-protein that, in its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled before binding another molecule of aminoacyl-tRNA. Required for mitochondrial protein biosynthesis and maintenance of mitochondrial DNA. Ref.4

Pathway

Protein biosynthesis; polypeptide chain elongation. HAMAP-Rule MF_00118_B

Subcellular location

Mitochondrion Ref.6 Ref.8.

Post-translational modification

The precursor is processed in two steps involving mitochondrial intermediate peptidase (MIP) and mitochondrial processing peptidase (MPP). HAMAP-Rule MF_00118_B

Miscellaneous

Present with 58527 molecules/cell in log phase SD medium.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion Probable
Chain39 – 437399Elongation factor Tu, mitochondrial HAMAP-Rule MF_00118_B
PRO_0000007465

Regions

Nucleotide binding55 – 628GTP By similarity
Nucleotide binding117 – 1215GTP By similarity
Nucleotide binding172 – 1754GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
P02992 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 26F4DFE805D1A93B

FASTA43747,972
        10         20         30         40         50         60 
MSALLPRLLT RTAFKASGKL LRLSSVISRT FSQTTTSYAA AFDRSKPHVN IGTIGHVDHG 

        70         80         90        100        110        120 
KTTLTAAITK TLAAKGGANF LDYAAIDKAP EERARGITIS TAHVEYETAK RHYSHVDCPG 

       130        140        150        160        170        180 
HADYIKNMIT GAAQMDGAII VVAATDGQMP QTREHLLLAR QVGVQHIVVF VNKVDTIDDP 

       190        200        210        220        230        240 
EMLELVEMEM RELLNEYGFD GDNAPIIMGS ALCALEGRQP EIGEQAIMKL LDAVDEYIPT 

       250        260        270        280        290        300 
PERDLNKPFL MPVEDIFSIS GRGTVVTGRV ERGNLKKGEE LEIVGHNSTP LKTTVTGIEM 

       310        320        330        340        350        360 
FRKELDSAMA GDNAGVLLRG IRRDQLKRGM VLAKPGTVKA HTKILASLYI LSKEEGGRHS 

       370        380        390        400        410        420 
GFGENYRPQM FIRTADVTVV MRFPKEVEDH SMQVMPGDNV EMECDLIHPT PLEVGQRFNI 

       430 
REGGRTVGTG LITRIIE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence determination of the nuclear gene coding for mitochondrial elongation factor Tu of Saccharomyces cerevisiae."
Nagata S., Tsunetsugu-Yokota Y., Naito A., Kaziro Y.
Proc. Natl. Acad. Sci. U.S.A. 80:6192-6196(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae."
Myers A.M., Pape L.K., Tzagoloff A.
EMBO J. 4:2087-2092(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase."
Branda S.S., Isaya G.
J. Biol. Chem. 270:27366-27373(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY MPP AND MIP, IDENTIFICATION OF PROBABLE CLEAVAGE SITE.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00428 Genomic DNA. No translation available.
Z75095 Genomic DNA. Translation: CAA99396.1.
BK006948 Genomic DNA. Translation: DAA10959.1.
PIREFBYT. A03520.
RefSeqNP_014830.1. NM_001183606.1.

3D structure databases

ProteinModelPortalP02992.
SMRP02992. Positions 45-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34582. 68 interactions.
DIPDIP-4130N.
IntActP02992. 12 interactions.
MINTMINT-497322.
STRING4932.YOR187W.

Proteomic databases

PaxDbP02992.
PeptideAtlasP02992.
PRIDEP02992.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR187W; YOR187W; YOR187W.
GeneID854359.
KEGGsce:YOR187W.

Organism-specific databases

CYGDYOR187w.
SGDS000005713. TUF1.

Phylogenomic databases

eggNOGCOG0050.
GeneTreeENSGT00550000074682.
HOGENOMHOG000229290.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG7GXPMZ.

Enzyme and pathway databases

BioCycYEAST:G3O-33697-MONOMER.
UniPathwayUPA00345.

Gene expression databases

GenevestigatorP02992.

Family and domain databases

HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
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.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976464.
PROP02992.

Entry information

Entry nameEFTU_YEAST
AccessionPrimary (citable) accession number: P02992
Secondary accession number(s): D6W2P3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 19, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways