ID   EFTU_CYAM1              Reviewed;         410 AA.
AC   Q85FT7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA; Synonyms=tuf;
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(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, 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:0000305}.
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DR   EMBL; AB002583; BAC76258.1; -; Genomic_DNA.
DR   RefSeq; NP_849096.1; NC_004799.1.
DR   AlphaFoldDB; Q85FT7; -.
DR   SMR; Q85FT7; -.
DR   STRING; 45157.CMV191CT; -.
DR   EnsemblPlants; CMV191CT; CMV191CT; CMV191C.
DR   GeneID; 845061; -.
DR   Gramene; CMV191CT; CMV191CT; CMV191C.
DR   KEGG; cme:CymeCp164; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   HOGENOM; CLU_007265_0_0_1; -.
DR   Proteomes; UP000007014; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009658; P:chloroplast organization; IEA:EnsemblPlants.
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   Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..410
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000091454"
FT   DOMAIN          10..215
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          61..65
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          82..85
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          137..140
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          175..177
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         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   410 AA;  45048 MW;  9EB163DBE1F6CB6B CRC64;
     MARTKFERTK PHVNIGTIGH VDHGKTTLTA AISAVLASKD NTVQLKKFEE IDSAPEERAR
     GITINTSHVE YQTEKRHYAH VDCPGHADYV KNMITGAAQM DGAILVVSAA DGPMPQTREH
     ILLAKQVGVP SIVVFLNKAD MVDDPELLEL VELEVRELLS KYDFPGDTIP FVTGSALLAL
     EACMKNPKIG EGKDKWVDKI FELMKIVDEY IPTPQRDVDK SFLMAVEDVF SITGRGTVAT
     GRIERGRVKV GETIEIVGLK NTKTTTVTGL EMFQKTLDEG IAGDNVGVLL RGVQKTDIER
     GMVLAKPGSI TPHTKFEAEV YVLTKEEGGR HTPFFPGYRP QFYVRTTDVT GTIEDFTADD
     GSKAEMVMPG DRIKMCVNLI YPVAIEQGMR FAIREGGRTV GAGVVTKILE