ID A0A1J7IAF9_LUPAN Unreviewed; 786 AA.
AC A0A1J7IAF9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Elongation factor G, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03063};
DE Short=cEF-G {ECO:0000256|HAMAP-Rule:MF_03063};
GN ORFNames=TanjilG_20542 {ECO:0000313|EMBL:OIW09835.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW09835.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW09835.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW09835.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- FUNCTION: Chloroplast-localized elongation factor EF-G involved in
CC protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal
CC translocation step during translation elongation. During this step, the
CC ribosome changes from the pre-translocational (PRE) to the post-
CC translocational (POST) state as the newly formed A-site-bound peptidyl-
CC tRNA and P-site-bound deacylated tRNA move to the P and E sites,
CC respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome.
CC {ECO:0000256|HAMAP-Rule:MF_03063}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000256|HAMAP-Rule:MF_03063}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_03063}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP-
CC Rule:MF_03063}.
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DR EMBL; CM007366; OIW09835.1; -; Genomic_DNA.
DR RefSeq; XP_019446631.1; XM_019591086.1.
DR AlphaFoldDB; A0A1J7IAF9; -.
DR STRING; 3871.A0A1J7IAF9; -.
DR EnsemblPlants; OIW09835; OIW09835; TanjilG_20542.
DR GeneID; 109349991; -.
DR Gramene; OIW09835; OIW09835; TanjilG_20542.
DR OMA; YAGNIMG; -.
DR OrthoDB; 148165at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000188354; Chromosome LG06.
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:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR HAMAP; MF_03063; EF_G_plantC; 1.
DR InterPro; IPR030848; EF_G_plantC.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR047872; EFG_IV.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|HAMAP-
KW Rule:MF_03063};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_03063};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03063};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|HAMAP-Rule:MF_03063};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03063}; Reference proteome {ECO:0000313|Proteomes:UP000188354}.
FT DOMAIN 97..372
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 106..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03063"
FT BINDING 170..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03063"
FT BINDING 224..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03063"
SQ SEQUENCE 786 AA; 86868 MW; 3EBEC79358F55495 CRC64;
MAAESLSVAT TPSLCNFNAS KFHRRPTLLS PLHFTVLRSP LPSHSLTSSS SSLSHFFGTS
RVTSNSTNLS LLRQNGRRNF SVFAMSTEDT KRVVPLSDYR NIGIMAHIDA GKTTTTERVL
YYTGRNYKIG EVHEGTATMD WMEQEQERGI TITSAATTTF WNKHRINIID TPGHVDFTLE
VERALRVLDG AICLFDSVAG VEPQSETVWR QADKYGVPRI CFVNKMDRLG ANFYRTRDMI
VTNLGAKPLV IQLPIGSEDS FKGVVDLVRM KAIVWSGEEL GAKFEYVDIP EDLQDQAQDY
RSQMIETIVD LDDDAMENYL EGIEPDEETI KKLIRKGTIS ASFVPVLCGS AFKNKGVQPL
LDAVVDYLPS PLELPPMKGT DPENPEGTLE RIASDSEPFS GLAFKIMNDP FVGSLTFVRV
YSGTLTAGSY ALNANKGKRE RIGRLLEMHA NSREDVKTAL TGDIIALAGL KDTITGETLC
DPESPIVLER MEFPDPVIKV AIEPKTKADI DKMATGLIKL AQEDPSFHFS RDEEINQTVI
EGMGELHLEI IVDRLKREFK VEANVGAPQV NYRESISKIS EVKYVHKKQS GGQGQFADIT
VRFEPMEPGS GYEFKSEIKG GSVPREYIPG VMKGLEECMS NGVLAGYPVV DVRAVLVDGS
YHDVDSSVLA FQLAARGAFR EGVRKAGPRM LEPIMKVEVV TPEEHLGDVI GDLNSRRGQI
NSFGDKPGGL KVVDSLVPLA EMFQYVSTLR GMTKGRASYT MQLAMFDVVP QHIQNQLASK
EQEVAA
//
