ID   EFTU_EUGLO              Reviewed;         409 AA.
AC   P14634;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Elongation factor Tu, plastid;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Euglena longa (Euglenophycean alga) (Astasia longa).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=2338940; DOI=10.1007/bf00391749;
RA   Siemeister G., Buchholz C., Hachtel W.;
RT   "Genes for the plastid elongation factor Tu and ribosomal protein S7 and
RT   six tRNA genes on the 73 kb DNA from Astasia longa that resembles the
RT   chloroplast DNA of Euglena.";
RL   Mol. Gen. Genet. 220:425-432(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=7859309; DOI=10.1007/bf00309557;
RA   Gockel G., Hachtel W., Baier S., Fliss C., Henke M.;
RT   "Genes for components of the chloroplast translational apparatus are
RT   conserved in the reduced 73-kb plastid DNA of the nonphotosynthetic
RT   euglenoid flagellate Astasia longa.";
RL   Curr. Genet. 26:256-262(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=11212895; DOI=10.1078/s1434-4610(04)70033-4;
RA   Gockel G., Hachtel W.;
RT   "Complete gene map of the plastid genome of the nonphotosynthetic euglenoid
RT   flagellate Astasia longa.";
RL   Protist 151:347-351(2000).
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; AJ294725; CAC24610.1; -; Genomic_DNA.
DR   PIR; S14923; EFITT.
DR   RefSeq; NP_074999.1; NC_002652.1.
DR   AlphaFoldDB; P14634; -.
DR   SMR; P14634; -.
DR   GeneID; 802512; -.
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_0000091445"
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"
SQ   SEQUENCE   409 AA;  45184 MW;  AF82295BE9BE4498 CRC64;
     MSRQKFERIK PHINIGTIGH VDHGKTTLTA AITMALSVTG NTKSKKYEEI DSSPEEKARG
     ITINTAHVEY ETKNRHYAHV DCPGHADYIK NMITGAAQMD GAILVISATD GPMPQTKEHI
     LLAKQVGVPN LVVFLNKEDQ IDDNELLELI ELEIRETLNN YEFPGDEIPI ITGSALLAIE
     ALNKNPKIIK GENKWVDKIL DLMDKIDSYI PTPIRDTDKD FLLAIEDVLS ITGRGTVATG
     RIERGKIKVG ETVELIGLKN IKSTTITGLE MFQKSLDEAI AGDNVGVLLR GIQKNEVERG
     MVIAKPGTIQ PHIKFNSQVY ILTKEEGGRH TPFFEGYKPQ FYVRTTDVTG KIESFKSDDG
     TTVQMVMPGD KIKMIVELVQ PIAIEKGMRF AIREGGKTVG AGVIINIID