ID K4K4F6_9CHLO Unreviewed; 301 AA.
AC K4K4F6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Elongation factor Tu, chloroplastic {ECO:0000256|ARBA:ARBA00021392};
DE Flags: Fragment;
GN Name=tufA {ECO:0000313|EMBL:AFU93159.1};
OS Codium duthieae.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AFU93159.1}.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Bryopsidales; Bryopsidineae; Codiaceae; Codium.
OX NCBI_TaxID=414127 {ECO:0000313|EMBL:AFU93159.1};
RN [1] {ECO:0000313|EMBL:AFU93159.1}
RP NUCLEOTIDE SEQUENCE.
RA Verbruggen H.;
RT "Molecular phylogeny of the Codium decorticatum complex.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00003982}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR EMBL; JX463038; AFU93159.1; -; Genomic_DNA.
DR EMBL; JX463039; AFU93160.1; -; Genomic_DNA.
DR AlphaFoldDB; K4K4F6; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR43721:SF5; ELONGATION FACTOR TU, CHLOROPLASTIC; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AFU93159.1};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW ECO:0000313|EMBL:AFU93159.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AFU93159.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 1..137
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFU93159.1"
FT NON_TER 301
FT /evidence="ECO:0000313|EMBL:AFU93159.1"
SQ SEQUENCE 301 AA; 33573 MW; B2E181BB4A9AACB5 CRC64;
HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSGADGPMPQ TKEHILLAKQ VGVPAIVVFL
NKADQVDDDE LLELVELEIQ ETLTTYEYPG DEIPIITGSA LLALESLTEN NLENYDKWVQ
KIYDLMKTVD EYIPLPKRDT EKPFLMAIEN VVSITGRGTV ATGRVERGMI EVGQTVELVG
LKNTKETIIT GLEMFQKTLD KSVAGDNVGI LLRGIQKEEI QRGMVLAKPA SIMPHRHFKA
QVYILKKEEG GRHTSFFAGY RPQFYVRTTD VTGHIKTFQA DDNTEIKMVM PGDRIQMEVE
L
//