EFTS_RICCO
ID EFTS_RICCO Reviewed; 379 AA.
AC B9SEZ6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=EFTS {ECO:0000255|HAMAP-Rule:MF_03135}; ORFNames=RCOM_1211470;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ973941; EEF37773.1; -; Genomic_DNA.
DR RefSeq; XP_002524565.1; XM_002524519.2.
DR AlphaFoldDB; B9SEZ6; -.
DR SMR; B9SEZ6; -.
DR STRING; 3988.XP_002524565.1; -.
DR PRIDE; B9SEZ6; -.
DR GeneID; 8288301; -.
DR KEGG; rcu:8288301; -.
DR eggNOG; KOG1071; Eukaryota.
DR InParanoid; B9SEZ6; -.
DR OrthoDB; 1048278at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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: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 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..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT CHAIN 46..379
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000402329"
SQ SEQUENCE 379 AA; 41438 MW; 9049EF79D5126AD7 CRC64;
MALYRTARRP LQMMLFSRLG NPEQNYSSWA RKDASQSAFG MFVRLFSAHA PAAAEQMSLI
KQLRERTSAP IKDVKASLVD CNWDIEAAQK DLRKRGKVLA SKKSGRAATE GLLALAQNEG
KAALIELNCE TDFVARNDIF QCLALSLAKQ ALLTENTAQQ ASGIHPVGPE CLEDLMINLE
HPKISGETTV QNAITEVAAM MGENVKLRRG FVMSTSLPGV LSTYLHTSPQ PGLGRIAGLL
SLEIEDGNSQ LDVLHHVGSE LAMHVVAAKP LFLTKELVSS DALESEREIL KSQAESTGKS
QMAIEKMVEG RLRKYYEEVV LMEQKFIIND AVNVKTVLNN LSKEVGSPVK IGSFFRMEVG
EGIQRLEATS ADEPVAQAA
