ID   EF2_METTE               Reviewed;         730 AA.
AC   O93640;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=fusA; Synonyms=fus;
OS   Methanosarcina thermophila.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
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; AF026165; AAC79200.1; -; Genomic_DNA.
DR   PIR; T44246; T44246.
DR   AlphaFoldDB; O93640; -.
DR   SMR; O93640; -.
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_0000091036"
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;  80565 MW;  3D5197BFC2000246 CRC64;
     MGRRKKMVER VTTLMNEPEK IRNIGIVAHI DHGKTTLSDN LLAGAGMISK ELAGRQLFMD
     SDEEEQERGI TIDASNVSMV HTYNNEDYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVVD
     AVEGTMPQTE TVLRQALREH VRPVLFVNKV DRLINELQVD SQEMQVRLGK VIDHVNKLIK
     NMNPEKFKAG WKVDAAAGTV AFGSALYNWA ISVPMMQKTG ISFTNVYDYC KAEDMKALAE
     KCPLHATVLD MVIRFLPNPL EAQKGRVPTI WHGDANSEIG KSMASANADG DLAFMVTDIS
     IDPHAGEVAT GRLFSGSFSR GMEVYISGTA RKSRVQQVGI FMGPERLEVE KIPAGNIAAV
     TGLKDAIVGS TVTTLDGMTP FESIRHVSEP VVTVAVEAKH TKDLPKLVEV LRQVAKEDPT
     LQITLDEETG EHLMAGMGEL HLEVIAHRIQ RDKNVEITTS KPIVVYRETI KKKIEPVEGK
     SPNRHNRFYI YVEPLDTAIV EMIKSGDISM NLPELERRQK LIELGMGKEE AKGIVGIHNS
     NIFIDITKGI QYLNETMELI LDGFEEVMRA GPLTREPVAN MKCVLVDAKL HEDAIHRGPA
     QVIPAARQAI QAGMLMAEDC LLEPYQKVFV QVPQLTMGGA TKELQGRRGI ILNMTTEGDL
     AIIEARVPVA EMFGFAGEIR SATEGRAMWS TEFGGFDIVP TSIQTEVVGQ IRERKGLKRD
     LPKASDYLSM