ID   EFTS_SCHJY              Reviewed;         310 AA.
AC   B6K2P1;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 51.
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=SJAG_05271;
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936;
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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; KE651166; EEB07422.1; -; Genomic_DNA.
DR   RefSeq; XP_002173715.1; XM_002173679.1.
DR   AlphaFoldDB; B6K2P1; -.
DR   SMR; B6K2P1; -.
DR   STRING; 4897.EEB07422; -.
DR   EnsemblFungi; EEB07422; EEB07422; SJAG_05271.
DR   GeneID; 7051135; -.
DR   VEuPathDB; FungiDB:SJAG_05271; -.
DR   eggNOG; KOG1071; Eukaryota.
DR   HOGENOM; CLU_940600_0_0_1; -.
DR   OMA; QGWISQC; -.
DR   OrthoDB; 1048278at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IEA:EnsemblFungi.
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; 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|HAMAP-Rule:MF_03135"
FT   CHAIN           43..310
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402349"
SQ   SEQUENCE   310 AA;  34238 MW;  3C34ACE02DC1659A CRC64;
     MGFQVLRSVI QAPLAKRSFL CKSCPSGLRV LYNNILLSSR SYSTKGSAFT LIKKLRQETN
     APIFLIKEAV EETNGQSFFE AKSVLSEKMK ARGQRLAQQL QGRVAKQGWI CTAILPDAQA
     ACMLELNCES DFVAQNPKIQ RLALSSASSI LHSLNRVNAD STEQRNVSTD LDSLKKIILH
     SDKDSSSNLG NTLFDAFSNA TSTTGERIEL SRAIVFQRTK PQHQLGRYTH GTDVRVHSSL
     GRVGCLVSLS NAQKAGLADD IAREFVAQDP ESIDDFLHNT SVYDNSKTMK DLLGSANVVD
     WVRWERGQAQ