ID   EF2_DESMO               Reviewed;         734 AA.
AC   P33159;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=fusA; Synonyms=fus;
OS   Desulfurococcus mucosus (Desulfurococcus mobilis).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=2275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35582 / DSM 2161 / JCM 9186 / Hvv 3/9;
RX   PubMed=8159735; DOI=10.1073/pnas.91.8.3255;
RA   Creti R., Ceccarelli E., Bocchetta M., Sanangelantoni A.M., Tiboni O.,
RA   Palm P., Cammarano P.;
RT   "Evolution of translational elongation factor (EF) sequences: reliability
RT   of global phylogenies inferred from EF-1 alpha(Tu) and EF-2(G) proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3255-3259(1994).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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:0000305}.
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DR   EMBL; X68014; CAA48150.1; -; Genomic_DNA.
DR   PIR; S54740; S25166.
DR   AlphaFoldDB; P33159; -.
DR   SMR; P33159; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_A; EF_G_EF_2_A; 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; 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; IPR004543; Transl_elong_EFG/EF2_arc.
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; TIGR00490; aEF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..734
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091027"
FT   DOMAIN          18..259
FT                   /note="tr-type G"
FT   BINDING         27..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         600
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   734 AA;  82332 MW;  133E8A1376595609 CRC64;
     MVRFKQTSEV LKIMRNIEQI RNIGITAHVD HGKTTLSDSL LSAAGLLSEK IAGQALALDY
     LDVEQKRQMT VKAANASLYH EYKGKPYLIN LIDTPGHVDF QSKTIRALRV IDGAIVVVDA
     VEGVMTQTEM YLRVALEERV RPVLFINKID RLIKELRSPN EIQQRLVQIV KDVNTLIATY
     ADKEFQKAWL LDPMKGQAFG SARDRWGLTI PLVQQKGIKF SDIVDVYTKG KEAVAELQKA
     APLHEAILDM VVKYVPNPRD AQRYRIPKIW HGDLNHEAVK YMMEADPNGP LVMLVNDIRV
     DPHAGLVATG RIYSGTLRAG EEVWLVNARV PQRVLQVSLY MGPYRELADE ITAGNIAAAL
     ALEKARSGET VVAMKYKDSM TPFEKLRMIT ESVVTVAIEP KNPQQLTKLV DALYKLHLED
     PSLIVKINEE TGEYLLSGVG TLHIEIALTL LKDLYGLEVV ASPPVIVYRE TVRESSQVFE
     GKSPNKHNKF YISVAPLNEE TLRLMSEGII VEDMDARERA KILREQAGWD ADEARRIMAI
     DENLNMLVDM TTGVQYLREI KDTVIQGFRL AMKEGPLAME PVRGVKVVLH DAVVHEDPAH
     RGPAQIFPAV RNAIFAGFLT AKPTILEPIL KLDIRTPMEY IGNISTVITK KRGKLIEVQQ
     METSARVIAE IPVSESFDIA DMLRNVTAGK AIWGQEFSRW APVPESMLMD LVSKIRTRKG
     LKPEPPKLED FLSP