ID   EFTS2_PARTE             Reviewed;         294 AA.
AC   A0C574;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Elongation factor Ts, mitochondrial 2 {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-Ts 2 {ECO:0000255|HAMAP-Rule:MF_03135};
DE            Short=EF-TsMt 2 {ECO:0000255|HAMAP-Rule:MF_03135};
GN   ORFNames=GSPATT00006440001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(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   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
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DR   EMBL; CT868041; CAK65941.1; -; Genomic_DNA.
DR   RefSeq; XP_001433338.1; XM_001433301.1.
DR   AlphaFoldDB; A0C574; -.
DR   SMR; A0C574; -.
DR   STRING; 5888.CAK65941; -.
DR   EnsemblProtists; CAK65941; CAK65941; GSPATT00006440001.
DR   GeneID; 5019123; -.
DR   KEGG; ptm:GSPATT00006440001; -.
DR   eggNOG; KOG1071; Eukaryota.
DR   HOGENOM; CLU_047155_0_0_1; -.
DR   InParanoid; A0C574; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
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; 1.
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.
FT   CHAIN           1..294
FT                   /note="Elongation factor Ts, mitochondrial 2"
FT                   /id="PRO_0000402332"
SQ   SEQUENCE   294 AA;  33354 MW;  D3917023A1389837 CRC64;
     MFRKIYTNIS ITLIKQLREA SGSPINDCKK ALESTDGNFE KAIQYLKERG LAQAEKKMGN
     QTKQGVIVAY TNNKVAALAE INCETDFVAR TSEFLEFSTN FIKTIVNQEQ DFSSSNIDSV
     LNDKRKQLVG KLQENIVIGN LNAFVATKNS VFGVYQHNCL KNTICGLGGS VVELITESEL
     TDVKTQILRE GANNLAVTYL GLKPRFLYQH EVSSDVVDQI RKEVEKEFGS KTAQQQNFIV
     KGKLQNYYSD NVFEHQEYFL NEDEPKTIKQ YMAKELEEVI KDKVKIGRCL YLTI