ID   EFTU_TOXGO              Reviewed;         401 AA.
AC   Q9TMM9; O78325; Q26114;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Elongation factor Tu, apicoplast;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Toxoplasma gondii.
OG   Plastid; Apicoplast.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RH;
RA   Denny P.W., Wilson R.J.M.;
RT   "An elongation factor encoded by the toxoplasma gondii putative plastid.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RH;
RA   Kissinger J.C., Donald R.G., Moulton A.L., Gutell R., Aiello D.P.,
RA   Lang-Unnasch N., Roos D.S.;
RT   "Mapping, cloning, and complete sequence annotation of the 35-kb plastid
RT   genome of Toxoplasma gondii.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, apicoplast.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X88775; CAA61254.1; -; Genomic_DNA.
DR   EMBL; Y11431; CAA72239.1; -; Genomic_DNA.
DR   EMBL; U87145; AAD41145.1; -; Genomic_DNA.
DR   RefSeq; NP_044559.1; NC_001799.1.
DR   AlphaFoldDB; Q9TMM9; -.
DR   SMR; Q9TMM9; -.
DR   GeneID; 1466608; -.
DR   VEuPathDB; ToxoDB:TGARI_262380; -.
DR   VEuPathDB; ToxoDB:TGCAST_216960; -.
DR   VEuPathDB; ToxoDB:TGCAST_302050; -.
DR   VEuPathDB; ToxoDB:TGCAST_390980; -.
DR   VEuPathDB; ToxoDB:TGCOUG_302050; -.
DR   VEuPathDB; ToxoDB:TGDOM2_262380; -.
DR   VEuPathDB; ToxoDB:TGFOU_302050; -.
DR   VEuPathDB; ToxoDB:TGGT1_262380; -.
DR   VEuPathDB; ToxoDB:TGMAS_302050; -.
DR   VEuPathDB; ToxoDB:TGME49_302050; -.
DR   VEuPathDB; ToxoDB:TGP89_302050; -.
DR   VEuPathDB; ToxoDB:TGPRC2_302060; -.
DR   VEuPathDB; ToxoDB:TGRH88_086420; -.
DR   VEuPathDB; ToxoDB:TGRUB_302050; -.
DR   VEuPathDB; ToxoDB:TGVAND_262380; -.
DR   VEuPathDB; ToxoDB:TGVEG_262380; -.
DR   GO; GO:0020011; C:apicoplast; 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; 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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Apicoplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..401
FT                   /note="Elongation factor Tu, apicoplast"
FT                   /id="PRO_0000337597"
FT   DOMAIN          10..206
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          173..175
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"
FT   CONFLICT        376
FT                   /note="M -> I (in Ref. 2; CAA72239/CAA61254)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   401 AA;  44313 MW;  C7CCF9B7ACF7530F CRC64;
     MAKEIFKKQK PHINIGTIGH VDHGKTTLTA AITYVLAKNN QAKLKTYKEI DCAPEEIARG
     ITIKTSHIEY ETAVRHYAHI DCPGHADYIK NMITGAAQMD GAILVVSAVD GPMPQTKEHL
     LLAKQIGISN IIVFLNKIDL IDDNEILELV ELETRELLDK YNFSSDTPII TGSALKALDN
     NLTSNIWVDK IYELLTALDS YIPLPKRDLD KPFLLAIEDI FSITGRGTVV TGKIERGSIK
     LGDTVTMLGF NISKNVVVIG LEMFQKTLEI GEAGDNVGIL LRGIQKTEVK RGMILSKPLT
     MTLHSIFQAD VYILTVAEGG REKPIFEGYC PQFYLYTINI TGSIKFSSET KETGTKMILP
     GDRVKLNVTL IYSIAMEKGM RFAIREGGRT IGAGIITDII K