EFGC1_SOYBN
ID EFGC1_SOYBN Reviewed; 787 AA.
AC P34811; I1MUX0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Elongation factor G-1, chloroplastic;
DE Short=cEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03063};
DE Flags: Precursor;
GN Name=fusA1;
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 [GENOMIC DNA].
RC STRAIN=cv. Maple Arrow;
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).
RN [2]
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).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA50573.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X71439; CAA50573.1; ALT_INIT; Genomic_DNA.
DR EMBL; BT096075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S35701; S35701.
DR RefSeq; XP_006600825.1; XM_006600762.2.
DR AlphaFoldDB; P34811; -.
DR SMR; P34811; -.
DR STRING; 3847.GLYMA17G14650.1; -.
DR PRIDE; P34811; -.
DR ProMEX; P34811; -.
DR EnsemblPlants; KRH04069; KRH04069; GLYMA_17G137600.
DR Gramene; KRH04069; KRH04069; GLYMA_17G137600.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; P34811; -.
DR OMA; MDDMVGG; -.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000008827; Chromosome 17.
DR Genevisible; P34811; 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..86
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT CHAIN 87..787
FT /note="Elongation factor G-1, chloroplastic"
FT /id="PRO_0000007439"
FT DOMAIN 98..373
FT /note="tr-type G"
FT REGION 14..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT BINDING 171..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT BINDING 225..228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT CONFLICT 89
FT /note="D -> DG (in Ref. 1; CAA50573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 86900 MW; 6B255A3DBD5AD130 CRC64;
MAAESSLRVA TPTLCNLNGS QRRPTTTTLS PLRFMGFRPR PSSHSLTSSS LSHFFGSTRI
HSNSSSSYSS ISRQHAPRRN FSVFAMSADD AKRSVPLKDY RNIGIMAHID AGKTTTTERI
LYYTGRNYKI GEVHEGTATM DWMEQEQERG ITITSAATTT FWNKHRINII DTPGHVDFTL
EVERALRVLD GAICLFDSVA GVEPQSETVW RQADKYGVPR ICFVNKMDRL GANFYRTRDM
IVTNLGAKPL VIQLPIGSED NFKGVIDLVR NKAIVWSGEE LGAKFDIVDI PEDLQEQAQD
YRAQMIENIV EFDDQAMENY LEGIEPDEET IKKLIRKGTI SASFVPVMCG SAFKNKGVQP
LLDAVVDYLP SPLDLPAMKG SDPENPEATI ERLASDDEPF AGLAFKIMSD PFVGSLTFVR
VYAGKLGAGS YVLNANKGKK ERIGRLLEMH ANSRDDVKVA LAGDIIALAG LKDTITGETL
CDPDNPIVLE RMDFPDPVIK VAIEPKTKAD VDKMATGLIK LAQEDPSFHF SRDEEINQTV
IEGMGELHLE IIVDRLKREF KVEANVGAPQ VNYRESISKI SEVKYVHKKQ SGGQGQFADI
TVRFEPMDPG SGYEFKSEIK GGAVPREYIP GVMKGLEECM SNGVLAGFPV VDVRAVLTDG
SYHDVDSSVL AFQLAARGAF REGIRKAGPR MLEPIMKVEV VTPEEHLGDV IGDLNSRRGQ
INSFGDKPGG LKVVDSLVPL AEMFQYVSTL RGMTKGRASY TMQLAMFDVV PQHIQNQLAT
KEQEVAA
