EFTS_BRUMA
ID EFTS_BRUMA Reviewed; 331 AA.
AC A8QE76;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-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};
DE Flags: Precursor;
GN ORFNames=Bm1_50845;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(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 -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_03135}.
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DR EMBL; DS239431; EDP29196.1; -; Genomic_DNA.
DR RefSeq; XP_001901637.1; XM_001901602.1.
DR AlphaFoldDB; A8QE76; -.
DR SMR; A8QE76; -.
DR STRING; 6279.A8QE76; -.
DR EnsemblMetazoa; Bm4414.1; Bm4414.1; WBGene00224675.
DR GeneID; 6105054; -.
DR KEGG; bmy:BM_BM4414; -.
DR WBParaSite; Bm4414.1; Bm4414.1; WBGene00224675.
DR CTD; 6105054; -.
DR WormBase; Bm4414; BM23865; WBGene00224675; Bma-tsfm-1.
DR InParanoid; A8QE76; -.
DR OMA; HTTRQLC; -.
DR OrthoDB; 1048278at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
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; -; 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;
KW Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT CHAIN 15..331
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000402320"
SQ SEQUENCE 331 AA; 36859 MW; 0390042EDC8840CE CRC64;
MIVSRQVIRS VVRKSFNRLC SANVVALPSG STKEALKELR RKTGYSYVNC RKALNEFGPD
NLDEAIKWLK KRAIEEGWEK AAKLGDRPTR QGIVSVMTKG NKAAIVELNC ETDFVSRNED
FKRLVEDVTK AVLHAADRDG TSTHGFELLN SNINSLKTSE NGMLVKDLIT EAIGRLGENI
TLSRAQLILA PPNVQLFGYA HPKEGTDRVY MGRYVSVVGL KGSNKTDFPT EKLGFQLCQH
VVGMRSLTLG TPLPVKKTSV KDEVSQDDEI NAFYNGEVTH IDENETQLLR QSFMLNPSQT
VHEYVTGHGA SIVDFYRTEL SSNVSEESFQ S