ID   EFTS_OSTTA              Reviewed;         338 AA.
AC   Q016E7; A0A096PAC1;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Elongation factor Ts, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-TsMt {ECO:0000255|HAMAP-Rule:MF_03135};
DE   Flags: Precursor;
GN   Name=EFTS {ECO:0000255|HAMAP-Rule:MF_03135};
GN   OrderedLocusNames=Ot02g04990 {ECO:0000312|EMBL:CEG01257.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595;
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC   -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC       exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC       Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_03135}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03135}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
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DR   EMBL; CAID01000002; CEG01257.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q016E7; -.
DR   SMR; Q016E7; -.
DR   STRING; 70448.Q016E7; -.
DR   eggNOG; KOG1071; Eukaryota.
DR   InParanoid; Q016E7; -.
DR   OrthoDB; 1048278at2759; -.
DR   Proteomes; UP000009170; Chromosome 2.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   Gene3D; 3.30.479.20; -; 2.
DR   HAMAP; MF_00050; EF_Ts; 1.
DR   InterPro; IPR036402; EF-Ts_dimer_sf.
DR   InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR   InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR   InterPro; IPR018101; Transl_elong_Ts_CS.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 2.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..338
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402328"
SQ   SEQUENCE   338 AA;  35984 MW;  C138049696F273FA CRC64;
     MSPSIAMFTL TPNARALASK TSKMDLIKNL RERTGAPIVD VKAALTAHDY DSEAAYDALR
     AKGLAAAAKK AGRTSADGAV AALSGDRGVV LFEVNSETDF VARGESFQSL IKECAEATLR
     AVESDRAMTE EHGTATAGAL RALRDERIGE LLTSDGKPLS DAVRDVAVHV RENVRLRRAF
     AYAATVGAGE VIGTYVHGAL APGVGKQAAC VVAKGVSEEF ANKLAMHVVA SSPLYLRSDC
     VPTDVMEREL AVFRTQTEGS GKPANIVEKI LAGRMNKYYE EVCLENQKFI LDDSMTVEKA
     VKAEGGELVA FSRVKVGEGI EVEEKDFAAE VAEAVRTT