EFTU_EMIHU
ID EFTU_EMIHU Reviewed; 407 AA.
AC Q4G342;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Elongation factor Tu, chloroplastic;
DE Short=EF-Tu;
GN Name=tufA;
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OG Plastid; Chloroplast.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX PubMed=16303746; DOI=10.1093/dnares/12.2.151;
RA Sanchez-Puerta M.V., Bachvaroff T.R., Delwiche C.F.;
RT "The complete plastid genome sequence of the haptophyte Emiliania huxleyi:
RT a comparison to other plastid genomes.";
RL DNA Res. 12:151-156(2005).
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; AY741371; AAX13924.1; -; Genomic_DNA.
DR RefSeq; YP_277425.1; NC_007288.1.
DR AlphaFoldDB; Q4G342; -.
DR SMR; Q4G342; -.
DR GeneID; 3562528; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..407
FT /note="Elongation factor Tu, chloroplastic"
FT /id="PRO_0000275385"
FT DOMAIN 10..212
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 407 AA; 44252 MW; 1647388FA440AAFC CRC64;
MAREKFERSK PHVNIGTIGH VDHGKTTLTA AISATLAVYS GSKKDISLID SAPEEKARGI
TINTAHVEYE TETRHYAHVD CPGHADYVKN MITGAAQMDG GILVVSAADG PMPQTREHIL
LAKQVGVPHL VVFLNKADQV DDEELLELVE LEVQELLENY DFPGDDIPFV SGSALLALQA
VEGGPKAKGD DKWVDRIFDL MESVDNYIPA PERDTEKTFL MAVEDVFSIT GRGTVATGRI
ERGILKIGDT IEIVGLKDTQ TTTVTGIEMF QKTLDEGMAG DNVGILIRGV QKTDIERGMV
LAQPGTISPH KKFEAEVYVL GKDEGGRHTP FFTGYRPQFY VRTIDVTGTI VQFTGDDGSA
AEMVMPGDRI KMTAELINPI AIEQGMRFAI REGGRTVGAG VVSKILE