ID   EFTU_EIMTE              Reviewed;         403 AA.
AC   Q33451;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Elongation factor Tu, apicoplast;
DE            Short=EF-Tu;
GN   Name=tufA; Synonyms=tuf;
OS   Eimeria tenella (Coccidian parasite).
OG   Plastid; Apicoplast.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H;
RA   Denny P.W., Wilson R.J.M.;
RT   "An elongation factor encoded by the Eimeria tenella putative plastid.";
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H;
RA   Denny P.W., Preiser P., Williamson D., Wilson I.;
RT   "Evidence for a single origin of the 35 kb plastid DNA in apicomplexans.";
RL   Protist 149:51-59(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Penn State;
RX   PubMed=14636990; DOI=10.1016/j.gene.2003.08.008;
RA   Cai X., Fuller A.L., McDougald L.R., Zhu G.;
RT   "Apicoplast genome of the coccidian Eimeria tenella.";
RL   Gene 321:39-46(2003).
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   -!- 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}.
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DR   EMBL; X89446; CAA61615.1; -; Genomic_DNA.
DR   EMBL; Y12332; CAA73000.1; -; Genomic_DNA.
DR   EMBL; AY217738; AAO40237.1; -; Genomic_DNA.
DR   PIR; S57945; S57945.
DR   RefSeq; NP_852636.1; NC_004823.1.
DR   AlphaFoldDB; Q33451; -.
DR   SMR; Q33451; -.
DR   GeneID; 1263692; -.
DR   VEuPathDB; ToxoDB:ETH2_API03600; -.
DR   VEuPathDB; ToxoDB:ETH_00014560; -.
DR   VEuPathDB; ToxoDB:ETH_00018510; -.
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; 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   Apicoplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..403
FT                   /note="Elongation factor Tu, apicoplast"
FT                   /id="PRO_0000337596"
FT   DOMAIN          10..210
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   403 AA;  44971 MW;  183FB831905BA697 CRC64;
     MAKKFFEKTK THLNIGTIGH VDHGKTTLTA AITSYLSKIN NTKAKSYSEI DSAPEEKARG
     ITINTSHIEY ETNLRHYAHI DCPGHADYIK NMITGAAQMD GAILVVSATD GPMPQTREHL
     LLAKQVGVPN IIVFLNKIDM VEDNELLELV ELEVRELLDI YEYNGDSTSI IKGSALKALE
     YIEKNDLNNK WVKNLKNLIE ALDKSIPEPK RDINKPFLLS IEDIFSITGR GTVVTGKIER
     GKVKLNDTVD ILGFNLLKTT TVTGIEMFQK ILNTAEAGDN VGILLRGIQK NEVRRGMVLA
     KPLSILTYSK FDAEVYILSS SEGGRKKPFF EGYKPQFYFY TTDVTGTIEF LRNPEKPEMI
     LPGDKVKLRI SLMYSIALEK GMRFAIREGG KTIGAGIIID LIN