ID   EFTU_GYMST              Reviewed;         363 AA.
AC   O63930;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
DE   Flags: Fragment;
GN   Name=tufA;
OS   Gymnochlora stellata.
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Gymnochlora.
OX   NCBI_TaxID=67809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9419245; DOI=10.1007/pl00006272;
RA   Ishida K., Cao Y., Hasegawa M., Okada N., Hara Y.;
RT   "The origin of chlorarachniophyte plastids, as inferred from phylogenetic
RT   comparisons of amino acid sequences of EF-Tu.";
RL   J. Mol. Evol. 45:682-687(1997).
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, chloroplast.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AB008007; BAA25891.1; -; Genomic_DNA.
DR   AlphaFoldDB; O63930; -.
DR   SMR; O63930; -.
DR   PRIDE; O63930; -.
DR   GO; GO:0009507; C:chloroplast; 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   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; 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   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           <1..>363
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000091463"
FT   DOMAIN          <1..189
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         55..59
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         110..113
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         363
SQ   SEQUENCE   363 AA;  39642 MW;  8A92DD685563481E CRC64;
     TLTAAITMAL STISGKQGKK YDDIDSAPEE KARGITINTA HVEYETETRH YAHVDCPGHA
     DYVKNMITGA AQMDGAILVV SGADGPMPQT KEHLLLAKQV GVPSIVVFLN KEDQVDDEEL
     LELVELEVRE MLDNYDFPGD DTPIITGSAL LALQALTDTT DAIGRGSNPW VDKILTLMDN
     VDEYIPTPER ETEKPFLMAV EDVFSITGRG TVATGRVERG GIKIGDTVEI VGLKETRSTT
     VTGLKMFQKM LQESIAGDNV GMLLRGIQKT DIQRGMVIAQ PGSITPHVSF EAQVYVLTKE
     EGGRHTPFLS GYRPQFYVRT TDVTGKVESL KSDEDKSEMK MVVPGDRVTM SVELVQPIAI
     EKG