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EFTU_TETOB
ID   EFTU_TETOB              Reviewed;         419 AA.
AC   Q1KVS9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 393;
RX   PubMed=16638149; DOI=10.1186/1471-2148-6-37;
RA   de Cambiaire J.-C., Otis C., Lemieux C., Turmel M.;
RT   "The complete chloroplast genome sequence of the chlorophycean green alga
RT   Scenedesmus obliquus reveals a compact gene organization and a biased
RT   distribution of genes on the two DNA strands.";
RL   BMC Evol. Biol. 6:37-37(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, 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; DQ396875; ABD48278.1; -; Genomic_DNA.
DR   RefSeq; YP_635995.1; NC_008101.1.
DR   AlphaFoldDB; Q1KVS9; -.
DR   SMR; Q1KVS9; -.
DR   GeneID; 4099785; -.
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:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..419
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000275380"
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   419 AA;  45764 MW;  C5F45446C17F4CEC CRC64;
     MARAKFERSK PHVNIGTIGH VDHGKTTLTA AITMALAALG GATGKKYDEI DSAPEEKARG
     ITINTAHVEY ETPNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSGAD GPMPQTKEHI
     LLAKQVGVPN MVVFLNKEDQ VDDAELLELV ELEVRETLDK YEFPGDEIPI VSGSALLALE
     ALVENPKIQR GDNKWVDKIF DLMDKVDEYI PTPDRETDKP FLLAVEDVLS ITGRGTVATG
     RVERGTLKVG ENVELIGLKD TKATVVTGLE MFKKTLDETM AGDNVGVLLR GIQKKDVERG
     MVLAKPGSIT PHTKFEAQVY VLTKEEGGRH SPFLVGYQPQ FFIRTTDVTG KIVSFTHIQM
     KNPSSVAEEH SNKMAMPGDR IEVTVQLIYP VAVEKGMRFA IREGGRTVGA GVVTNILEE
 
 
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