ID   EFTS_SCHPO              Reviewed;         299 AA.
AC   Q9HGL5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=tsf1; ORFNames=SPBC800.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15695360; DOI=10.1534/genetics.104.037473;
RA   Chiron S., Suleau A., Bonnefoy N.;
RT   "Mitochondrial translation: elongation factor tu is essential in fission
RT   yeast and depends on an exchange factor conserved in humans but not in
RT   budding yeast.";
RL   Genetics 169:1891-1901(2005).
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, ECO:0000269|PubMed:15695360}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03135,
CC       ECO:0000269|PubMed:15695360}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_03135}.
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DR   EMBL; CU329671; CAC01522.1; -; Genomic_DNA.
DR   RefSeq; NP_595108.1; NM_001021015.2.
DR   AlphaFoldDB; Q9HGL5; -.
DR   SMR; Q9HGL5; -.
DR   BioGRID; 277217; 32.
DR   STRING; 4896.SPBC800.07c.1; -.
DR   MaxQB; Q9HGL5; -.
DR   PaxDb; Q9HGL5; -.
DR   PRIDE; Q9HGL5; -.
DR   EnsemblFungi; SPBC800.07c.1; SPBC800.07c.1:pep; SPBC800.07c.
DR   GeneID; 2540692; -.
DR   KEGG; spo:SPBC800.07c; -.
DR   PomBase; SPBC800.07c; tsf1.
DR   VEuPathDB; FungiDB:SPBC800.07c; -.
DR   eggNOG; KOG1071; Eukaryota.
DR   HOGENOM; CLU_940600_0_0_1; -.
DR   InParanoid; Q9HGL5; -.
DR   OMA; QGWISQC; -.
DR   PhylomeDB; Q9HGL5; -.
DR   PRO; PR:Q9HGL5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005759; C:mitochondrial matrix; IGI:PomBase.
DR   GO; GO:0003746; F:translation elongation factor activity; IMP:PomBase.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IGI:PomBase.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   Gene3D; 3.30.479.20; -; 1.
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   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF54713; SSF54713; 2.
PE   3: Inferred from homology;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT   CHAIN           19..299
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000362143"
SQ   SEQUENCE   299 AA;  33563 MW;  92691173D90030E6 CRC64;
     MLFQRRLHFH QFFGKTRVTG SLSRQWYSKL PSKLADIKKL RSETNASMDL VKQSVEEAGV
     GNLELAREIL KKKIVQRGGK LAEKSKNRTA KEGWIIQCIS EDGRKAVMAE INCESDFVAQ
     TTPFQDLARR IASTFLHYLP TNHSSYSVEA TLKNEILKHQ AYVSKNHEAN EKDVSSNVSL
     EEEIVKMTSF TGEKVQVQRL HCMNARVPST AIGIFSHGAK QSSPLQQLGR IGSMVQINSD
     LSTRKGLSNQ IAKEIVAQDP SSTSELLSFR SLVDSEKTIK DVLGQSTILE WVRWERGGN