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Q9ZT91

- EFTM_ARATH

UniProt

Q9ZT91 - EFTM_ARATH

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Protein

Elongation factor Tu, mitochondrial

Gene

TUFA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 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 bindingi74 – 818GTPBy similarity
Nucleotide bindingi136 – 1405GTPBy similarity
Nucleotide bindingi191 – 1944GTPBy similarity

GO - Molecular functioni

  1. ATP binding Source: TAIR
  2. cobalt ion binding Source: TAIR
  3. GTPase activity Source: InterPro
  4. GTP binding Source: UniProtKB-KW
  5. translation elongation factor activity Source: UniProtKB-KW
  6. zinc ion binding Source: TAIR

GO - Biological processi

  1. response to cadmium ion Source: TAIR
Complete GO annotation...

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:TUFA
Ordered Locus Names:At4g02930
ORF Names:T4I9.19, T5J8.25
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G02930.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

  1. cell wall Source: TAIR
  2. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5151MitochondrionSequence AnalysisAdd
BLAST
Chaini52 – 454403Elongation factor Tu, mitochondrialPRO_0000007466Add
BLAST

Proteomic databases

PaxDbiQ9ZT91.
PRIDEiQ9ZT91.

Expressioni

Gene expression databases

ExpressionAtlasiQ9ZT91. baseline and differential.
GenevestigatoriQ9ZT91.

Interactioni

Protein-protein interaction databases

BioGridi13423. 2 interactions.
STRINGi3702.AT4G02930.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9ZT91.
SMRiQ9ZT91. Positions 65-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 261197tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 818G1By similarity
Regioni115 – 1195G2By similarity
Regioni136 – 1394G3By similarity
Regioni191 – 1944G4By similarity
Regioni229 – 2313G5By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0050.
HOGENOMiHOG000229290.
KOiK02358.
OMAiSSYSISH.
PhylomeDBiQ9ZT91.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_B. EF_Tu_B.
InterProiIPR000795. 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]
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.
TIGR00231. small_GTP. 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.

Q9ZT91-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASVVLRNPS SKRLVPFSSQ IYSRCGASVT SSYSISHSIG GDDLSSSTFG
60 70 80 90 100
TSSFWRSMAT FTRNKPHVNV GTIGHVDHGK TTLTAAITKV LAEEGKAKAI
110 120 130 140 150
AFDEIDKAPE EKKRGITIAT AHVEYETAKR HYAHVDCPGH ADYVKNMITG
160 170 180 190 200
AAQMDGGILV VSGPDGPMPQ TKEHILLARQ VGVPSLVCFL NKVDVVDDPE
210 220 230 240 250
LLELVEMELR ELLSFYKFPG DDIPIIRGSA LSALQGTNDE IGRQAILKLM
260 270 280 290 300
DAVDEYIPDP VRVLDKPFLM PIEDVFSIQG RGTVATGRIE QGVIKVGEEV
310 320 330 340 350
EILGLREGGV PLKSTVTGVE MFKKILDNGQ AGDNVGLLLR GLKREDIQRG
360 370 380 390 400
MVIAKPGSCK TYKKFEAEIY VLTKDEGGRH TAFFSNYRPQ FYLRTADITG
410 420 430 440 450
KVELPENVKM VMPGDNVTAV FELIMPVPLE TGQRFALREG GRTVGAGVVS

KVMT
Length:454
Mass (Da):49,410
Last modified:May 1, 1999 - v1
Checksum:iB7C2CA1DCC432FDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1010MASVVLRNPS → MEEPVDREDIDLRVSSTDIG WNEFAAA in CAA61511. (PubMed:8555448)Curated
Sequence conflicti310 – 3123VPL → CST in CAA61511. (PubMed:8555448)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89227 mRNA. Translation: CAA61511.1.
AC004044 Genomic DNA. Translation: AAD15337.1.
AF069442 Genomic DNA. Translation: AAC79113.1.
AL161495 Genomic DNA. Translation: CAB77778.1.
CP002687 Genomic DNA. Translation: AEE82252.1.
AY136421 mRNA. Translation: AAM97087.1.
BT008755 mRNA. Translation: AAP49517.1.
F14375 mRNA. Translation: CAA23078.1.
PIRiT01400.
RefSeqiNP_192202.1. NM_116527.3.
UniGeneiAt.22275.

Genome annotation databases

EnsemblPlantsiAT4G02930.1; AT4G02930.1; AT4G02930.
GeneIDi828134.
KEGGiath:AT4G02930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89227 mRNA. Translation: CAA61511.1 .
AC004044 Genomic DNA. Translation: AAD15337.1 .
AF069442 Genomic DNA. Translation: AAC79113.1 .
AL161495 Genomic DNA. Translation: CAB77778.1 .
CP002687 Genomic DNA. Translation: AEE82252.1 .
AY136421 mRNA. Translation: AAM97087.1 .
BT008755 mRNA. Translation: AAP49517.1 .
F14375 mRNA. Translation: CAA23078.1 .
PIRi T01400.
RefSeqi NP_192202.1. NM_116527.3.
UniGenei At.22275.

3D structure databases

ProteinModelPortali Q9ZT91.
SMRi Q9ZT91. Positions 65-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 13423. 2 interactions.
STRINGi 3702.AT4G02930.1-P.

Proteomic databases

PaxDbi Q9ZT91.
PRIDEi Q9ZT91.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G02930.1 ; AT4G02930.1 ; AT4G02930 .
GeneIDi 828134.
KEGGi ath:AT4G02930.

Organism-specific databases

GeneFarmi 4096. 415.
TAIRi AT4G02930.

Phylogenomic databases

eggNOGi COG0050.
HOGENOMi HOG000229290.
KOi K02358.
OMAi SSYSISH.
PhylomeDBi Q9ZT91.

Gene expression databases

ExpressionAtlasi Q9ZT91. baseline and differential.
Genevestigatori Q9ZT91.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00118_B. EF_Tu_B.
InterProi IPR000795. 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 ]
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.
TIGR00231. small_GTP. 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. "Isolation, expression, and evolution of the gene encoding mitochondrial elongation factor Tu in Arabidopsis thaliana."
    Kuhlman P., Palmer J.D.
    Plant Mol. Biol. 29:1057-1070(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-454.
    Strain: cv. Columbia.
  6. "Proteomic approach to identify novel mitochondrial proteins in Arabidopsis."
    Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.
    Plant Physiol. 127:1694-1710(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 296-306, SUBCELLULAR LOCATION.
    Tissue: Leaf and Stem.
  7. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiEFTM_ARATH
AccessioniPrimary (citable) accession number: Q9ZT91
Secondary accession number(s): Q39206
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3