EFTU_DERMA
ID EFTU_DERMA Reviewed; 235 AA.
AC P50375;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Elongation factor Tu, chloroplastic;
DE Short=EF-Tu;
DE Flags: Fragment;
GN Name=tufA;
OS Derbesia marina.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Bryopsidales; Bryopsidineae; Derbesiaceae; Derbesia.
OX NCBI_TaxID=33107;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7663757; DOI=10.1006/mpev.1995.1012;
RA Delwiche C.F., Kuhsel M., Palmer J.D.;
RT "Phylogenetic analysis of tufA sequences indicates a cyanobacterial origin
RT of all plastids.";
RL Mol. Phylogenet. Evol. 4:110-128(1995).
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:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; U09431; AAA87689.1; -; Genomic_DNA.
DR AlphaFoldDB; P50375; -.
DR SMR; P50375; -.
DR PRIDE; P50375; -.
DR GO; GO:0009507; C:chloroplast; 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; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 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..>235
FT /note="Elongation factor Tu, chloroplastic"
FT /id="PRO_0000091457"
FT DOMAIN <1..125
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 47..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 235
SQ SEQUENCE 235 AA; 25764 MW; 051225A5BB646A17 CRC64;
KNMITGAAQM DGAILVVSGA DGPMPQTKEH ILLAKQVGVP SIVVFLNKAD QVDDEELLEL
VELEVQETLS EYEYPGEEIP IISGSALLAL EALTENPELD SANNEWVQKI YHLMDSVDDY
IPLPERDTDK PFLMAIEDVF SITGRGTVAT GRVERGSVDV GETVELVGLK ETKETIITGL
EMFQKTLDKS VAGDNVGILL RGIQKEEIQR GMVLAKPGSI TPHRCFKAQV YILKK