EFTS_LEIBR
ID EFTS_LEIBR Reviewed; 276 AA.
AC A4HH79;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=LbrM29_V2.0730, LbrM_29_0730;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
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; FR799004; CAM39929.1; -; Genomic_DNA.
DR RefSeq; XP_001566420.1; XM_001566370.1.
DR AlphaFoldDB; A4HH79; -.
DR SMR; A4HH79; -.
DR STRING; 5660.A4HH79; -.
DR GeneID; 5417305; -.
DR KEGG; lbz:LBRM_29_0730; -.
DR VEuPathDB; TriTrypDB:LbrM.29.0730; -.
DR VEuPathDB; TriTrypDB:LBRM2903_290013500; -.
DR InParanoid; A4HH79; -.
DR OMA; TETVGKW; -.
DR Proteomes; UP000007258; Chromosome 29.
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; -; 1.
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; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 1.
PE 3: Inferred from homology;
KW Elongation factor; Mitochondrion; Protein biosynthesis; Reference proteome.
FT CHAIN 1..276
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000402336"
SQ SEQUENCE 276 AA; 29864 MW; 5D8757C533BA19A6 CRC64;
MLHRSFFRFA ALADKKAFME LVKALRYRTE APISDCSAAL TEAAGDMDAA MQLLRKRGVA
RAMKKGDCVT EHGFVVSCVG STPASGAAII TMCSETDFAA RNEHFQRTCV QARDQLRKLM
DATNGAVLAN PEEAAKQLSD IMGEELRAAI AVLGENMRIR SIAPLVPAPH MSERLLVGSY
THGVLNVDGV GRIVGLVAVS QVRENEVISK DVLTSIGRHF VATSGAEGNY AHQNFFGSET
ETVGKWLKHH GLTFSSSLVQ EFGKEPVVHT AAEPHQ