ID   EFTS_DANRE              Reviewed;         305 AA.
AC   A1A5Z3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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; ORFNames=zgc:158429;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) 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; BC128869; AAI28870.1; -; mRNA.
DR   RefSeq; NP_001073504.1; NM_001080035.1.
DR   AlphaFoldDB; A1A5Z3; -.
DR   SMR; A1A5Z3; -.
DR   STRING; 7955.ENSDARP00000080380; -.
DR   PaxDb; A1A5Z3; -.
DR   PeptideAtlas; A1A5Z3; -.
DR   GeneID; 567785; -.
DR   KEGG; dre:567785; -.
DR   CTD; 10102; -.
DR   ZFIN; ZDB-GENE-061215-17; tsfm.
DR   eggNOG; KOG1071; Eukaryota.
DR   InParanoid; A1A5Z3; -.
DR   OrthoDB; 1048278at2759; -.
DR   PRO; PR:A1A5Z3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; 2.
DR   TIGRFAMs; TIGR00116; tsf; 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..305
FT                   /note="Elongation factor Ts, mitochondrial"
FT                   /id="PRO_0000402312"
SQ   SEQUENCE   305 AA;  33474 MW;  A467FFA8D28AA0D1 CRC64;
     MAMYSLFRSV RSEVVKGCLT QHVQSLFTSC PSLAADKALL LQLRKSTGYT FVNCKKALEK
     CNNDITQAES WLHEQAKKEG WSKATKLEGR KAKEGLIGLM MHDNAAVMVE VNCETDFVAR
     NEKFQQLVKD VALSVMAHQS TSKKTGFIKS VLSSEDMSKL NAPDGPSLAD QLALTIGRLG
     ENIAMRRAVS LSVPSDWHIG SYIHGTVAGQ VGIEMGRYGS LVVFQGEPKE GTYALGRKLA
     QHVMGEAPVS LGNMDDLSCG DSETRLLPQT FLPDPKYTVA QYLTLQDARV LDFIRFQCGE
     SSSQE