ID   EF2_METMT               Reviewed;         730 AA.
AC   O93637;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=fusA; Synonyms=ef-2, fus;
OS   Methanococcoides methylutens.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=2226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33938 / DSM 2657 / BCRC 16168 / OCM 158 / TMA-10;
RX   PubMed=9845338; DOI=10.1016/s0014-5793(98)01375-1;
RA   Thomas T., Cavicchioli R.;
RT   "Archaeal cold-adapted proteins: structural and evolutionary analysis of
RT   the elongation factor 2 proteins from psychrophilic, mesophilic and
RT   thermophilic methanogens.";
RL   FEBS Lett. 439:281-287(1998).
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; AF022779; AAC79197.1; -; Genomic_DNA.
DR   PIR; T44066; T44066.
DR   RefSeq; WP_048195088.1; NZ_JRHO01000014.1.
DR   AlphaFoldDB; O93637; -.
DR   SMR; O93637; -.
DR   PRIDE; O93637; -.
DR   OrthoDB; 1642at2157; -.
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..730
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091035"
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         596
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   730 AA;  80538 MW;  49450034651A20EE CRC64;
     MGRRKKMVER VTALMSNPVM IRNIAIIAHI DHGKTTLSDN LLAGAGMISK DLAGRQLFMD
     SDEEEQERGI TIDSANVSMV HEFEDEEYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVID
     AVEGTMPQTE TVLRQALKEH VRPVLFINKV DRLINELQVD AQEMQIRLGK LIDHVNKLIK
     GMNEERYNQG WRVDAAEGTV AFGSALYNWA ISVPMMQKTG VSFGEVFDYC RAEDMKSLGE
     KCPLHEAVND MVIRFLPSPI DAQEDRVGVI WHGDLEAGIG KQMAVADATG DLAFMVTDIS
     MDPHAGEVST GRLFSGSLSR GMEVYVSGAA KPNRIQQVGV FMGPERLEVD KIPAGNIAAV
     TGLRDAIVGS TVTTLDGMSP FESIRHASEP VVTVAVEAKH MKDLPKLVEV LRQVAKEDPT
     LKITLDEETG EHLMAGMGEL HLEVIAHRIE RDKGVEISTT PPIVVYRETI TGTAGPVEGK
     SPNRHNRFYV VVEPLEPEVR ELIREGEISM RMPELERREK LIAAGLDKDE AKRIADIFES
     NAYFDMTKGI QHLNETMELV LEGFVEVMKA GPLSKEPCMG VKVKLMDAKL HEDAVHRGPA
     QVIPASRQAI QAAMLMADDT LFEPYQKVFI QTPQEQMGGA TKEIQGRRGI IIDMTSEGDT
     TIIESKAPVS ELFGFAGDIR SATEGRAMWS TEFVGFEPLP TNMITEVVSG IRERKGLKKD
     LPQAQDFMSM