EFTS_BRAFL
ID EFTS_BRAFL Reviewed; 331 AA.
AC C3YEM5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 58.
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 ORFNames=BRAFLDRAFT_84221;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666507; EEN61119.1; -; Genomic_DNA.
DR RefSeq; XP_002605109.1; XM_002605063.1.
DR AlphaFoldDB; C3YEM5; -.
DR SMR; C3YEM5; -.
DR STRING; 7739.XP_002605109.1; -.
DR eggNOG; KOG1071; Eukaryota.
DR InParanoid; C3YEM5; -.
DR OrthoDB; 1048278at2759; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
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 3: Inferred from homology;
KW Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome.
FT CHAIN 1..331
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000402315"
FT REGION 254..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 36525 MW; E222BE1E3E288E39 CRC64;
MPCPTGVTRC SAGVSSLARC LHTCPVLEGV TKANLSKLRK KTGFTFVNCR KALEKFENDL
EQAEKWLKEQ AQKEGWAKAT KLQDRQTAQG LVGVAQEGTM ATMVEVNCET DFVARNPKFR
QLVTQVAMAT LGDVKAHPQW TLGWLKALHT GEELKQLQIG DTTLGDLTAL TIGTLGENIQ
IRRAMYYSVP PIPTKHVGVY VHAPVAGTTG GQSGSCALGK YGALVAFRRK NTEFQNFNAA
ELGRRLGQHV VGMSPLTVGE MPEVREEEGE KKDGDKQDEE ERSTDSDEDE TQMLRQTFLL
DPTMTVGEMT RQQGIELLDF VRFECGEVEE S