ID   EF2_PYRWO               Reviewed;         732 AA.
AC   P61878; P29050;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=fusA; Synonyms=fus;
OS   Pyrococcus woesei.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; X67205; CAA47641.1; -; Genomic_DNA.
DR   PIR; S54741; S23864.
DR   AlphaFoldDB; P61878; -.
DR   SMR; P61878; -.
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; 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; 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; PS00301; G_TR_1; 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..732
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091046"
FT   DOMAIN          19..260
FT                   /note="tr-type G"
FT   BINDING         28..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         597
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   732 AA;  82255 MW;  5226BFE1813D6C54 CRC64;
     MGRREEMIAK IKELMLQPER IRNIGIAAHI DHGKTTLSDN LLAGAGMISE ELAGKQLVLD
     FDEQEQARGI TINAANVSMV HNYEGKDYLI NLIDTPGHVD FGGDVTRAMR AIDGVIIVVD
     AVEGVMPQTE TVVRQALREY VKPVLFINKV DRLIRELKLT PQQMMERFSK IIMDVNRLIQ
     RYAPEEYKKK WMVRVEDGSV AFGSAYYNWA LSVPFMQRTG VKFNEIIDLT LKGDNKTLRQ
     RAPLHVVVLD MVVRHLPSPI EAQKYRIPHL WQGDINSKIG QAMLNCDPKG KMVMVITKII
     IDKHAGEVAT GRVWSGTVRS GQEVYLINSK RKGRIQQVGI YMGPERINME AVPAGNIVAV
     TGLRDAMAGE TVAEEQIEPF EALHYVSEPV VTVAIEAKNV KDLPRLIEAL RQLAKEDPTL
     HVKIDEETGQ HLLSGMGELH LEVKLYKLQK DWGIEVDVSE PIVVYRESIT KPSPIVEGKS
     PNKHNRFYVV VEPMPDEIYQ AIKEGIIPEG RVKDPKAVAK KLAELGMDYD IARGVVDIYN
     GNMFLDNTKG IQYLNEVMDL LIDGFHQAMD EGPLAKEPVM KVIVRLVDAQ VHEDNVHRGP
     AQIYPAIRTA IHCAMMKAGP VLYEPYQKVI INIPYEYMGA VSREISQRRG QLIDMRQEGE
     VMTIIAEAPV AEMFGFAGAI RSATSGRALW STEHAGFKRV PNELAQQIIR QIRQRKGLDP
     NPPTEKDVCP LF