ID   EF2_BETVU               Reviewed;         843 AA.
AC   O23755;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RA   Vogel R., Rausch T.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC       {ECO:0000250}.
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|PROSITE-ProRule:PRU01059}.
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DR   EMBL; Z97178; CAB09900.1; -; mRNA.
DR   PIR; T14579; T14579.
DR   RefSeq; NP_001290010.1; NM_001303081.2.
DR   AlphaFoldDB; O23755; -.
DR   SMR; O23755; -.
DR   PRIDE; O23755; -.
DR   GeneID; 104906141; -.
DR   KEGG; bvg:104906141; -.
DR   GO; GO:0005737; C:cytoplasm; 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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/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; 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; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis.
FT   CHAIN           1..843
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091006"
FT   DOMAIN          17..253
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         26..33
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..108
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         59
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         700
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   843 AA;  93799 MW;  D11325B42A51F4F8 CRC64;
     MVKFTADELR AIMDCKHNIR NMSVIAHVDH GKSTLTDSLV AAAGIIAQEV AGDVRMTDTR
     ADEAERGITI KSTGISLYYQ MTDEALQSYK GERKGNDYLI NLIDSPGHVD FSSEVTAALR
     ITDGALVVVD CIEGVCVQTE TVLRQALGER IRPVLTVNKM DRCFLELQVD GEEAYTTFQK
     VIENANVIMA TYEDPLLGDV QVYPEKGTVA FSAGLHGWAF TLSNFAKMYA SKFGVDESKM
     MERLWGENFF DPATKKWTTK NSGNASCKRG FVQFCYEPIK QIIAACMNDQ KDKLLAHVTK
     LGIQMKTEEK DLMGRPLMKR VMQTWLPASS ALLEMMIHHL PSPATAQRYR VENLYEGPMD
     DVYATAIRNC DPEGPLMLYV SKMIPASDKG RFFAFGRVFA GKVSTGMKVR IMGPNYVPGE
     KKDLYVKNVQ RTVIWMGKKQ ETVEDVPCGN TVALVGLDQY ITKNATLTNE KESDAHPIRA
     MKFSVSPVVR VAVQCKVASD LPKLVEGLKR LAKSDPMVVC SIEESGEHII AGAGELHLEI
     CLKDLQDDFM GGAEIIKSDP VVSFRETVLD RSVRTVMSKS PNKHNRLYME ARPMEEGLAE
     AIDEGRIGPR DDPKNRSKIL AEEYGWDKDL AKKIWCFGPE TTGPNMVVDM CKGVQYLNEI
     KDSVVAGFQW ASKEGALAEE NMRGICFEVC DVVLHTDAIH RGGGQIIPTA RRVFYASQLT
     AKPRLLEPVY LVEIQAPENA LGGIYSVLNQ KRGHVFEEMQ RPGTPLYNIK AYLPVVESFG
     FSSTLRASTS GQAFPQCVFD HWEMMPSDPL EAGSQASTLV SVIRKRKGLK EQMTPLSEFE
     DKL