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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
 
 
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