ID   EFTS_XENLA              Reviewed;         312 AA.
AC   A1L2P7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
GN   Name=tsfm;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Forelimb, and Hind limb;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; BC129644; AAI29645.1; -; mRNA.
DR   RefSeq; NP_001091158.1; NM_001097689.1.
DR   AlphaFoldDB; A1L2P7; -.
DR   SMR; A1L2P7; -.
DR   GeneID; 100036913; -.
DR   KEGG; xla:100036913; -.
DR   CTD; 100036913; -.
DR   Xenbase; XB-GENE-6255870; tsfm.L.
DR   OrthoDB; 1048278at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 100036913; Expressed in oocyte and 20 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; PS01126; EF_TS_1; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   2: Evidence at transcript level;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402314"
SQ   SEQUENCE   312 AA;  34419 MW;  0DACF2794F3C20EB CRC64;
     MAALCNNLRA KLVSWQPVGL FHTGVRLLAA DKDLLVKLRK KTGYSFMNCK KALEQCANDF
     KQAETWLHQQ AQKEGWDKAS KLQGRKTKEG LVGLLQDGST SVMVEVNCET DFVARNSKFQ
     QLVQQVAVST LRHCQSHPEN TSSYVKGFLC GDELLQLKAD ESLKDQLALA IGKLGENMIM
     KRAAWVKTPS DIFVGSYMHG ILMADLPSLT NMTFGKYGAL VICKDSDGNL KSNISEIGRR
     LGQHVVGMNP LLVGSLEDES GGETETKMLA QPFLLEPSLT VGQYLQPRGI NVLDFIRFEC
     GEEAESTEST PT