EFTS_LEIIN
ID EFTS_LEIIN Reviewed; 276 AA.
AC A4I4C5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=LinJ29.0880, LinJ_29_0750;
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5;
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; FR796461; CAM69633.1; -; Genomic_DNA.
DR RefSeq; XP_001466594.1; XM_001466557.1.
DR AlphaFoldDB; A4I4C5; -.
DR SMR; A4I4C5; -.
DR STRING; 5671.XP_001466594.1; -.
DR GeneID; 5070626; -.
DR KEGG; lif:LINJ_29_0750; -.
DR VEuPathDB; TriTrypDB:LINF_290012200; -.
DR eggNOG; KOG1071; Eukaryota.
DR InParanoid; A4I4C5; -.
DR OMA; TETVGKW; -.
DR Proteomes; UP000008153; 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_0000402337"
SQ SEQUENCE 276 AA; 29921 MW; 840BAA042ACD7D13 CRC64;
MPHRSLVCFA APADKKAFME LVKTLRYRTE APISDCSAAL KETDGDMDAA MQVLRKRGAA
RAMKKGDRVT EHGFVVSCVG STPASGAAIV TICSETDFAA RNEHFQKVCV QARDQLCKLM
DATNGAVLAN PEEAVKHLSD VMAEELRVAI AVLGENMRVR SIAPLVPAPH MSERLLIGSY
THGSLNVDNV GRIVGLVALS QVRENEVVPK DVLTSVGRHF VATSGAEGNY AHQNFFGSET
ETVGKWLKQR GLKFSSSLVQ EFGKEPVVHT APEPHR