EFGC2_SOYBN
ID EFGC2_SOYBN Reviewed; 780 AA.
AC I1K0K6;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Elongation factor G-2, chloroplastic;
DE Short=cEF-G 2 {ECO:0000255|HAMAP-Rule:MF_03063};
DE Flags: Precursor;
GN Name=fusA2;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2]
RP IDENTIFICATION.
RX PubMed=8357836; DOI=10.1016/0167-4781(93)90114-s;
RA Torres J.H., Breitenberger C.A., Spielmann A., Stutz E.;
RT "Cloning and sequencing of a soybean nuclear gene coding for a chloroplast
RT translation elongation factor EF-G.";
RL Biochim. Biophys. Acta 1174:191-194(1993).
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:0000255|HAMAP-Rule:MF_03063}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03063}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|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:0000255|HAMAP-Rule:MF_03063}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006579622.1; XM_006579559.2.
DR AlphaFoldDB; I1K0K6; -.
DR SMR; I1K0K6; -.
DR STRING; 3847.GLYMA05G04210.1; -.
DR PRIDE; I1K0K6; -.
DR EnsemblPlants; KRH57341; KRH57341; GLYMA_05G055500.
DR Gramene; KRH57341; KRH57341; GLYMA_05G055500.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; I1K0K6; -.
DR OMA; FRVVQMM; -.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000008827; Chromosome 5.
DR Genevisible; I1K0K6; GM.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 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; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT CHAIN 80..780
FT /note="Elongation factor G-2, chloroplastic"
FT /id="PRO_0000425112"
FT DOMAIN 91..366
FT /note="tr-type G"
FT BINDING 100..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT BINDING 164..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT BINDING 218..221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
SQ SEQUENCE 780 AA; 86083 MW; 4AEB47EEAF024D59 CRC64;
MAAESSLRVA TPTICNLNGS QRRPTTLSPL RFMGFSPRPS HSLTSSSLSH FFGSTRINSN
SSSISRQHAP RRNFSVFAMS GDDAKRSVPL KDYRNIGIMA HIDAGKTTTT ERILYYTGRN
YKIGEVHEGT ATMDWMEQEQ ERGITITSAA TTTFWNKHRI NIIDTPGHVD FTLEVERALR
VLDGAICLFD SVAGVEPQSE TVWRQADKYG VPRICFVNKM DRLGANFYRT RDMIVTNLGA
KPLVIQLPIG SEDNFKGVID LVRNKAIVWS GEELGAKFDI VDVPEDLQEQ AQEYRAQMIE
TIVEFDDQAM ENYLEGIEPD EETIKKLIRK GTISASFVPV MCGSAFKNKG VQPLLDAVVD
YLPSPLDLPA MKGSDPENPE ETIERVASDD EPFAGLAFKI MSDPFVGSLT FVRVYAGKLS
AGSYVLNANK GKKERIGRLL EMHANSREDV KVALAGDIIA LAGLKDTITG ETLCDPDNPI
VLERMDFPDP VIKVAIEPKT KADVDKMATG LIKLAQEDPS FHFSRDEEIN QTVIEGMGEL
HLEIIVDRLK REFKVEANVG APQVNYRESI SKTAEVKYVH KKQSGGQGQF ADITVRFEPM
DPGSGYEFKS EIKGGAVPKE YIPGVMKGLE ECMSNGVLAG FPVVDVRAVL TDGSYHDVDS
SVLAFQLAAR GAFREGIRKA GPRMLEPIMK VEVVTPEEHL GDVIGDLNSR RGQINSFGDK
PGGLKVVDAL VPLAEMFQYV STLRGMTKGR ASYTMQLAMF DVVPQHIQNQ LATKEQEVAA
