GenomeNet

Database: UniProt/SWISS-PROT
Entry: EFTU_HUMAN
LinkDB: EFTU_HUMAN
Original site: EFTU_HUMAN 
ID   EFTU_HUMAN              Reviewed;         455 AA.
AC   P49411; O15276;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2022, sequence version 3.
DT   24-JAN-2024, entry version 231.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
DE            Short=EF-Tu;
DE   AltName: Full=P43;
DE   Flags: Precursor;
GN   Name=TUFM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7828719; DOI=10.1016/0014-5793(94)01403-n;
RA   Wells J., Henkler F., Leversha M., Koshy R.;
RT   "A mitochondrial elongation factor-like protein is over-expressed in
RT   tumours and differentially expressed in normal tissues.";
RL   FEBS Lett. 358:119-125(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-455.
RC   TISSUE=Liver;
RX   PubMed=8547323; DOI=10.1016/0167-4781(95)00176-x;
RA   Woriax V.L., Burkhart W.A., Spremulli L.L.;
RT   "Cloning, sequence analysis and expression of mammalian mitochondrial
RT   protein synthesis elongation factor Tu.";
RL   Biochim. Biophys. Acta 1264:347-356(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-455.
RC   TISSUE=Heart, and Kidney;
RX   PubMed=9332382; DOI=10.1016/s0378-1119(97)00279-5;
RA   Ling M., Merante F., Chen H.-S., Duff C., Duncan A.M.V., Robinson B.H.;
RT   "The human mitochondrial elongation factor Tu (EF-Tu) gene: cDNA sequence,
RT   genomic localization, genomic structure, and identification of a
RT   pseudogene.";
RL   Gene 197:325-336(1997).
RN   [6]
RP   PROTEIN SEQUENCE OF 47-57.
RC   TISSUE=Heart;
RA   Dunn M.J.;
RL   Submitted (MAR-1996) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 47-56.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   PROTEIN SEQUENCE OF 242-274, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 382-398.
RA   Jacobs H.T., Smurthwaite L., Koshy R.;
RT   "Human genomic sequences encoding mitochondrial elongation factor EF-Tu:
RT   evidence for post-endosymbiotic intron insertion.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-91; LYS-259 AND LYS-421,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NLRX1 AND ATG16L1.
RX   PubMed=22749352; DOI=10.1016/j.immuni.2012.03.025;
RA   Lei Y., Wen H., Yu Y., Taxman D.J., Zhang L., Widman D.G., Swanson K.V.,
RA   Wen K.W., Damania B., Moore C.B., Giguere P.M., Siderovski D.P.,
RA   Hiscott J., Razani B., Semenkovich C.F., Chen X., Ting J.P.;
RT   "The mitochondrial proteins NLRX1 and TUFM form a complex that regulates
RT   type I interferon and autophagy.";
RL   Immunity 36:933-946(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-281, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [17]
RP   VARIANT COXPD4 GLN-339.
RX   PubMed=17160893; DOI=10.1086/510559;
RA   Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E.,
RA   Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C.,
RA   Comi G.P., Savasta S., Ferrero I., Zeviani M.;
RT   "Infantile encephalopathy and defective mitochondrial DNA translation in
RT   patients with mutations of mitochondrial elongation factors EFG1 and
RT   EFTu.";
RL   Am. J. Hum. Genet. 80:44-58(2007).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH HUMAN PARAINFLUENZA VIRUS TYPE 3 MATRIX
RP   PROTEIN (MICROBIAL INFECTION).
RX   PubMed=28407488; DOI=10.1016/j.chom.2017.03.004;
RA   Ding B., Zhang L., Li Z., Zhong Y., Tang Q., Qin Y., Chen M.;
RT   "The Matrix Protein of Human Parainfluenza Virus Type 3 Induces Mitophagy
RT   that Suppresses Interferon Responses.";
RL   Cell Host Microbe 21:538-547(2017).
RN   [19]
RP   INTERACTION WITH HANTAAN HANTAVIRUS GLYCOPROTEIN N (MICROBIAL INFECTION).
RX   PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061;
RA   Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L.,
RA   Zhang F.;
RT   "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate
RT   Autophagy Flux to Restrain Host Innate Immune Responses.";
RL   Cell Rep. 27:2075-2091.e5(2019).
CC   -!- FUNCTION: Promotes the GTP-dependent binding of aminoacyl-tRNA to the
CC       A-site of ribosomes during protein biosynthesis. Also plays a role in
CC       the regulation of autophagy and innate immunity. Recruits ATG5-ATG12
CC       and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS
CC       pathway. In turn, inhibits RLR-mediated type I interferon while
CC       promoting autophagy. {ECO:0000269|PubMed:22749352,
CC       ECO:0000269|PubMed:28407488}.
CC   -!- SUBUNIT: Interacts with NLRX1 (PubMed:22749352). Interacts with ATG16L1
CC       (PubMed:22749352). {ECO:0000269|PubMed:22749352}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human parainfluenza virus
CC       3 matrix protein; this interaction inhibits RLR-mediated type I
CC       interferon production while promoting autophagy.
CC       {ECO:0000269|PubMed:28407488}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC       glycoprotein N; this interaction contributes to the virus-induced
CC       degradation of mitochondria by autophagy, which leads to degradation of
CC       MAVS and inhibition of type I interferon (IFN) responses.
CC       {ECO:0000269|PubMed:31091447}.
CC   -!- INTERACTION:
CC       P49411; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-359097, EBI-714543;
CC       P49411; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-359097, EBI-2548702;
CC       P49411; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-359097, EBI-10175124;
CC       P49411; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-359097, EBI-3059266;
CC       P49411; Q86UT6: NLRX1; NbExp=2; IntAct=EBI-359097, EBI-3893071;
CC       P49411; P03427: PB2; Xeno; NbExp=9; IntAct=EBI-359097, EBI-8430745;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22749352}.
CC   -!- DISEASE: Combined oxidative phosphorylation deficiency 4 (COXPD4)
CC       [MIM:610678]: A mitochondrial disease resulting in neonatal lactic
CC       acidosis, rapidly progressive encephalopathy, severely decreased
CC       mitochondrial protein synthesis, and combined deficiency of mtDNA-
CC       related mitochondrial respiratory chain complexes.
CC       {ECO:0000269|PubMed:17160893}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB00499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:8547323};
CC       Sequence=CAA59169.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:9332382};
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DR   EMBL; S75463; AAC60647.1; -; mRNA.
DR   EMBL; AC133550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001633; AAH01633.2; -; mRNA.
DR   EMBL; BC010041; AAH10041.2; -; mRNA.
DR   EMBL; L38995; AAB00499.1; ALT_INIT; mRNA.
DR   EMBL; X84694; CAA59169.1; ALT_INIT; mRNA.
DR   EMBL; Y11797; CAA72493.1; -; Genomic_DNA.
DR   CCDS; CCDS10642.1; -.
DR   PIR; S62767; S62767.
DR   PIR; S68466; S68466.
DR   RefSeq; NP_003312.3; NM_003321.4.
DR   RefSeq; XP_016879108.1; XM_017023619.1.
DR   PDB; 7A5G; EM; 4.33 A; Z=4-455.
DR   PDB; 7O9K; EM; 3.10 A; t=4-455.
DR   PDBsum; 7A5G; -.
DR   PDBsum; 7O9K; -.
DR   AlphaFoldDB; P49411; -.
DR   EMDB; EMD-11642; -.
DR   EMDB; EMD-12763; -.
DR   SMR; P49411; -.
DR   BioGRID; 113135; 690.
DR   CORUM; P49411; -.
DR   IntAct; P49411; 125.
DR   MINT; P49411; -.
DR   STRING; 9606.ENSP00000322439; -.
DR   ChEMBL; CHEMBL4105970; -.
DR   DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   CarbonylDB; P49411; -.
DR   GlyCosmos; P49411; 2 sites, 1 glycan.
DR   iPTMnet; P49411; -.
DR   MetOSite; P49411; -.
DR   PhosphoSitePlus; P49411; -.
DR   SwissPalm; P49411; -.
DR   BioMuta; TUFM; -.
DR   DMDM; 1706611; -.
DR   DOSAC-COBS-2DPAGE; P49411; -.
DR   OGP; P49411; -.
DR   REPRODUCTION-2DPAGE; IPI00027107; -.
DR   SWISS-2DPAGE; P49411; -.
DR   UCD-2DPAGE; P49411; -.
DR   EPD; P49411; -.
DR   jPOST; P49411; -.
DR   MassIVE; P49411; -.
DR   MaxQB; P49411; -.
DR   PaxDb; 9606-ENSP00000322439; -.
DR   PeptideAtlas; P49411; -.
DR   ProteomicsDB; 56003; -.
DR   Pumba; P49411; -.
DR   TopDownProteomics; P49411; -.
DR   ABCD; P49411; 2 sequenced antibodies.
DR   Antibodypedia; 13151; 370 antibodies from 30 providers.
DR   DNASU; 7284; -.
DR   Ensembl; ENST00000313511.8; ENSP00000322439.3; ENSG00000178952.11.
DR   GeneID; 7284; -.
DR   KEGG; hsa:7284; -.
DR   MANE-Select; ENST00000313511.8; ENSP00000322439.3; NM_003321.5; NP_003312.3.
DR   UCSC; uc002drh.2; human.
DR   AGR; HGNC:12420; -.
DR   CTD; 7284; -.
DR   DisGeNET; 7284; -.
DR   GeneCards; TUFM; -.
DR   HGNC; HGNC:12420; TUFM.
DR   HPA; ENSG00000178952; Low tissue specificity.
DR   MalaCards; TUFM; -.
DR   MIM; 602389; gene.
DR   MIM; 610678; phenotype.
DR   neXtProt; NX_P49411; -.
DR   OpenTargets; ENSG00000178952; -.
DR   Orphanet; 254925; Combined oxidative phosphorylation defect type 4.
DR   PharmGKB; PA37082; -.
DR   VEuPathDB; HostDB:ENSG00000178952; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   GeneTree; ENSGT00940000156748; -.
DR   HOGENOM; CLU_007265_0_0_1; -.
DR   InParanoid; P49411; -.
DR   OrthoDB; 167272at2759; -.
DR   PhylomeDB; P49411; -.
DR   TreeFam; TF300432; -.
DR   PathwayCommons; P49411; -.
DR   Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR   Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR   SignaLink; P49411; -.
DR   SIGNOR; P49411; -.
DR   BioGRID-ORCS; 7284; 277 hits in 1160 CRISPR screens.
DR   ChiTaRS; TUFM; human.
DR   GeneWiki; TUFM; -.
DR   GenomeRNAi; 7284; -.
DR   Pharos; P49411; Tchem.
DR   PRO; PR:P49411; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P49411; Protein.
DR   Bgee; ENSG00000178952; Expressed in mucosa of transverse colon and 99 other cell types or tissues.
DR   ExpressionAtlas; P49411; baseline and differential.
DR   Genevisible; P49411; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR   GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0006414; P:translational elongation; IDA:UniProtKB.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03706; mtEFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW   Elongation factor; GTP-binding; Host-virus interaction; Mitochondrion;
KW   Nucleotide-binding; Phosphoprotein; Primary mitochondrial disease;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.6"
FT   CHAIN           47..455
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000007462"
FT   DOMAIN          58..254
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          67..74
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          108..112
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          129..132
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          184..187
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          222..224
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         67..74
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..187
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         82
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         91
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         237
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         259
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         281
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         289
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         364
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         421
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         339
FT                   /note="R -> Q (in COXPD4; dbSNP:rs121434452)"
FT                   /evidence="ECO:0000269|PubMed:17160893"
FT                   /id="VAR_031902"
FT   CONFLICT        198..200
FT                   /note="Missing (in Ref. 1; AAC60647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="D -> N (in Ref. 4; AAB00499 and 9; CAA72493)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   455 AA;  49875 MW;  58CAE59637766D3D CRC64;
     MTTMAAATLL RATPHFSGLA AGRTFLLQGL LRLLKAPALP LLCRGLAVEA KKTYVRDKPH
     VNVGTIGHVD HGKTTLTAAI TKILAEGGGA KFKKYEEIDN APEERARGIT INAAHVEYST
     AARHYAHTDC PGHADYVKNM ITGTAPLDGC ILVVAANDGP MPQTREHLLL ARQIGVEHVV
     VYVNKADAVQ DSEMVELVEL EIRELLTEFG YKGEETPVIV GSALCALEGR DPELGLKSVQ
     KLLDAVDTYI PVPARDLEKP FLLPVEAVYS VPGRGTVVTG TLERGILKKG DECELLGHSK
     NIRTVVTGIE MFHKSLERAE AGDNLGALVR GLKREDLRRG LVMVKPGSIK PHQKVEAQVY
     ILSKEEGGRH KPFVSHFMPV MFSLTWDMAC RIILPPEKEL AMPGEDLKFN LILRQPMILE
     KGQRFTLRDG NRTIGTGLVT NTLAMTEEEK NIKWG
//
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