EFTS_BOVIN
ID EFTS_BOVIN Reviewed; 338 AA.
AC P43896; A6QQT8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 {ECO:0000255|HAMAP-Rule:MF_03135};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7615523; DOI=10.1074/jbc.270.29.17243;
RA Xin H., Woriax V., Burkhart W., Spremulli L.L.;
RT "Cloning and expression of mitochondrial translational elongation factor Ts
RT from bovine and human liver.";
RL J. Biol. Chem. 270:17243-17249(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 56-338 IN COMPLEX WITH TUFM.
RX PubMed=15557323; DOI=10.1074/jbc.m411782200;
RA Jeppesen M.G., Navratil T., Spremulli L.L., Nyborg J.;
RT "Crystal structure of the bovine mitochondrial elongation factor Tu.Ts
RT complex.";
RL J. Biol. Chem. 280:5071-5081(2005).
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.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_03135}.
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DR EMBL; L37935; AAA96807.1; -; mRNA.
DR EMBL; BC149988; AAI49989.1; -; mRNA.
DR PIR; I45941; I45941.
DR RefSeq; NP_776629.1; NM_174204.3.
DR PDB; 1XB2; X-ray; 2.20 A; B=56-338.
DR PDBsum; 1XB2; -.
DR AlphaFoldDB; P43896; -.
DR SMR; P43896; -.
DR IntAct; P43896; 1.
DR STRING; 9913.ENSBTAP00000022496; -.
DR PaxDb; P43896; -.
DR PRIDE; P43896; -.
DR GeneID; 281551; -.
DR KEGG; bta:281551; -.
DR CTD; 10102; -.
DR eggNOG; KOG1071; Eukaryota.
DR HOGENOM; CLU_047155_4_0_1; -.
DR InParanoid; P43896; -.
DR OrthoDB; 1048278at2759; -.
DR TreeFam; TF314154; -.
DR EvolutionaryTrace; P43896; -.
DR Proteomes; UP000009136; 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:0070129; P:regulation of mitochondrial translation; ISS:UniProtKB.
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 PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Elongation factor; Mitochondrion;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT CHAIN 56..338
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000007467"
FT MOD_RES 89
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 146
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 205
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43897"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1XB2"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 88..110
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 243..254
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:1XB2"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:1XB2"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:1XB2"
SQ SEQUENCE 338 AA; 36602 MW; 449236159482DD68 CRC64;
MSLLRSLRLC LVARTGSCPL SALGPGPLLP SLQAGLPLLQ SPQQWHTFHS GSWLSSASSK
ELLMKLRRKT GYSFINCKKA LETCGGDLKQ AESWLHKQAQ KEGWSKAARL HGRKTKEGLI
GLLQEGDTTV LVEVNCETDF VSRNLKFQQL VQQVALGTLL HCQNLKDQLS TYSKGFLNSS
ELSELPAGPE REGSLKDQLA LAIGKLGENM ILKRAAWVKV PAGFYVGSYV HGAMHSPSLH
NLVLGKYGAL VICETSELKA NLADLGRRLG QHVVGMAPLS VGSLDDEPGG EAETKMLSQP
YLLDPSITLG QYVQPHGVSV VDFVRFECGE GEDAADAE
