ID EFTU_GUITH Reviewed; 408 AA.
AC P19457;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Elongation factor Tu, chloroplastic;
DE Short=EF-Tu;
GN Name=tufA;
OS Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1868578; DOI=10.1007/bf00355057;
RA Douglas S.E.;
RT "Unusual organization of a ribosomal protein operon in the plastid genome
RT of Cryptomonas phi: evolutionary considerations.";
RL Curr. Genet. 19:289-294(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9137835; DOI=10.1080/15216549700202101;
RA Wang S.L., Liu X.-Q., Douglas S.E.;
RT "The large ribosomal protein gene cluster of a cryptomonad plastid: gene
RT organization, sequence and evolutionary implications.";
RL Biochem. Mol. Biol. Int. 41:1035-1044(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:0000305}.
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DR EMBL; AF041468; AAC35730.1; -; Genomic_DNA.
DR RefSeq; NP_050796.1; NC_000926.1.
DR AlphaFoldDB; P19457; -.
DR SMR; P19457; -.
DR GeneID; 857104; -.
DR HOGENOM; CLU_007265_0_0_1; -.
DR OMA; KTHANIG; -.
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 CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 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..408
FT /note="Elongation factor Tu, chloroplastic"
FT /id="PRO_0000091462"
FT DOMAIN 10..213
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 59..63
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 80..83
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 135..138
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 173..175
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 80..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 44827 MW; 218420C0B1F82895 CRC64;
MARDKFERSK PHVNIGTIGH VDHGKTTLTA AISATLSQYT GKSKKFDEID SAPEERARGI
TINTAHVEYE TDKWYYAHVD CPGHADYVKN MITGAAQMDG AILVCSAANG PMPQTREHIL
LAKQVGVPYI VVFLNKADMV DDEELLELVQ LEVQELLEKY DFPGSEIPFV AGSALLALEA
VANNPTIKRG EDKWVDTIYQ LMDKVDEYIP TPERETDKAF LMAVEDVFSI TGRGTVATGR
IERGKVKVGD TIEIVGLRET RNTTITGLEM FQKSLDEALA GDNVGILVRG IQKTDIERGM
VLAAPGSITP HTKFEGEVYV LTKEEGGRHT PFFSGYRPQF YVRTTDVTGT IAQFTSDDGS
TAEMVMPGDR IKMTAQLIHP IAIEKGMRFA IREGGRTVGA GVVSKIIE
//
