ID   EFTS_POLPP              Reviewed;         354 AA.
AC   D3BAV8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 47.
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=tsfm; ORFNames=PPL_05689;
OS   Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS   pallidum).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC   Acytosteliaceae; Heterostelium.
OX   NCBI_TaxID=670386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26659 / Pp 5 / PN500;
RX   PubMed=21757610; DOI=10.1101/gr.121137.111;
RA   Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA   Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA   Schaap P., Gloeckner G.;
RT   "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT   origins for complex intercellular communication.";
RL   Genome Res. 21:1882-1891(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; ADBJ01000025; EFA81695.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3BAV8; -.
DR   SMR; D3BAV8; -.
DR   STRING; 670386.D3BAV8; -.
DR   PRIDE; D3BAV8; -.
DR   InParanoid; D3BAV8; -.
DR   OMA; HTTRQLC; -.
DR   OrthoDB; 1048278at2759; -.
DR   Proteomes; UP000001396; Unassembled WGS sequence.
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; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT   CHAIN           48..354
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402323"
SQ   SEQUENCE   354 AA;  38965 MW;  EB9188792E11979C CRC64;
     MMRSTLSLLQ KCRLPNNNGS LLSFKNNQVV NQTALFSMKS NQQYRFYSTD VKDLAPLIKE
     LRNRTSAPLK DCKEALIQNK NDIEKATSWL HEKGKSTANK FADRAVVEGT ISIVVNNGKA
     VILEMNSETD FVSRGETFRA LADQISRATL ESNLLAQSLA EIKPDTIAPQ PASGSTVADL
     IVGTVAKLRE NIRLRRVHAI DASNQPNTIV AGYAHDPSGT NQFGRLGSLV QLQYEGGQPD
     IAALNQLARN IAVHIVGVGP SYVSIESVPK VLLDEAIANK RHPNSLYDEV VLLEQKYISG
     EDNETVKAAV QRISKQLKTN ITIKSFVRYS VGEGMEKKVE NYGAEVMEKI NKAK