ID   EFTU_RECAM              Reviewed;         394 AA.
AC   O21245;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
GN   Name=TUFA;
OS   Reclinomonas americana.
OG   Mitochondrion.
OC   Eukaryota; Discoba; Jakobida; Histionina; Histionidae; Reclinomonas.
OX   NCBI_TaxID=48483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 50394;
RX   PubMed=9168110; DOI=10.1038/387493a0;
RA   Lang B.F., Burger G., O'Kelly C.J., Cedergren R., Golding G.B., Lemieux C.,
RA   Sankoff D., Turmel M., Gray M.W.;
RT   "An ancestral mitochondrial DNA resembling a eubacterial genome in
RT   miniature.";
RL   Nature 387:493-497(1997).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF007261; AAD11872.1; -; Genomic_DNA.
DR   PIR; S78139; S78139.
DR   RefSeq; NP_044757.1; NC_001823.1.
DR   AlphaFoldDB; O21245; -.
DR   SMR; O21245; -.
DR   PRIDE; O21245; -.
DR   GeneID; 801090; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..394
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000091472"
FT   DOMAIN          10..204
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  43627 MW;  428202ADF3DBC4EF CRC64;
     MSKEKFERTK PHCNIGTIGH VDHGKTTLTA AITKVLSETG GAVFTDYDQI DKAPEEKKRG
     ITISTSHVEY ETTKRHYAHI DCPGHEDYVK NMITGAAQMD GAILVVSAVD GPMPQTREHI
     LLSRQVGVPS LVVFLNKVDM VNDPEMLDLV EMEVRELLLS YKYPGDEIPI IRGSALKALQ
     GEIEYKKSIL KLMEAVDNYI PQPERSFDRP FLMPVEDVFS IAGRGTVVTG RVEQGQIKIG
     DAVEIIGLGS TVKTTCTGIE MFHKLLDYGQ AGDNLGMLIR GIQRDAVQRG QVICAPGSVK
     PHTKYEAQVY ILTKEEGGRH KPFFNNYRPQ FFFRTADVTG TIQLPKDVEM VNPGDNVKLI
     IELITPIAME EGIRFAMREG GRTIGAGVVS KIIE