ID   EFTU_HELSJ              Reviewed;         409 AA.
AC   Q2EEV7; Q6RH24;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Elongation factor Tu, plastid;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Helicosporidium sp. subsp. Simulium jonesii (Green alga).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium; unclassified Helicosporidium.
OX   NCBI_TaxID=145475;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15043882; DOI=10.1016/j.femsle.2004.02.006;
RA   Tartar A., Boucias D.G.;
RT   "The non-photosynthetic, pathogenic green alga Helicosporidium sp. has
RT   retained a modified, functional plastid genome.";
RL   FEMS Microbiol. Lett. 233:153-157(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16630350; DOI=10.1186/1741-7007-4-12;
RA   de Koning A.P., Keeling P.J.;
RT   "The complete plastid genome sequence of the parasitic green alga,
RT   Helicosporidium sp. is highly reduced and structured.";
RL   BMC Biol. 4:12-12(2006).
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.
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; AY498714; AAS21040.1; -; Genomic_DNA.
DR   EMBL; DQ398104; ABD33985.1; -; Genomic_DNA.
DR   RefSeq; YP_635937.1; NC_008100.1.
DR   AlphaFoldDB; Q2EEV7; -.
DR   SMR; Q2EEV7; -.
DR   GeneID; 4100448; -.
DR   GO; GO:0009536; C:plastid; 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; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..409
FT                   /note="Elongation factor Tu, plastid"
FT                   /id="PRO_0000293969"
FT   DOMAIN          10..214
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"
FT   CONFLICT        139
FT                   /note="D -> G (in Ref. 2; ABD33985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="D -> E (in Ref. 2; ABD33985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  44683 MW;  0C287EEF6E0260B2 CRC64;
     MAREKFERIK PHINIGTIGH VDHGKTTLTA AITMALASIG NTKGKNYADI DSAPEEKARG
     ITINTTHVEY ETAKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSGAD GPMPQTREHI
     VLAKQVGVPS MVVFINKEDQ VDDPEILELV ELEVRDLLTS YKFEGEEVPV ITGSALLALE
     AFIKNPKILK GENPWVDKIY NLMDSVDSYI PTPVREIDKP FLMAIEDVFS ISGRGTVATG
     RIERGKIKMG DSIEIIGGSL RKTTTVTGIE MFQKTLTDGV AGDNVGILMR GIQKKEIDRG
     MVLTKPKSID PLTSFEAQVY LLTKEEGGRS KGFTIGYRPQ FYVRTTDVTG AILNMLSDDN
     TPLKIASPGD RITMSVKLIQ PIALEKNMRF AIREGGKTVG AGVVSKLIN