ID   EF2_METM6               Reviewed;         727 AA.
AC   A9A9U4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Elongation factor 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=MmarC6_1304;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) 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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
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|HAMAP-Rule:MF_00054}.
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DR   EMBL; CP000867; ABX02117.1; -; Genomic_DNA.
DR   RefSeq; WP_012194061.1; NC_009975.1.
DR   AlphaFoldDB; A9A9U4; -.
DR   SMR; A9A9U4; -.
DR   STRING; 444158.MmarC6_1304; -.
DR   EnsemblBacteria; ABX02117; ABX02117; MmarC6_1304.
DR   GeneID; 5738174; -.
DR   KEGG; mmx:MmarC6_1304; -.
DR   eggNOG; arCOG01559; Archaea.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   OMA; GVMTQTE; -.
DR   OrthoDB; 1642at2157; -.
DR   PhylomeDB; A9A9U4; -.
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..727
FT                   /note="Elongation factor 2"
FT                   /id="PRO_1000091731"
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:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   MOD_RES         603
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   727 AA;  80115 MW;  0E80F326AA016D16 CRC64;
     MGRRAKMVEK VKTLMEKHDQ IRNMGICAHI DHGKTTLSDN LLAGAGMISK ELAGDQLALD
     FDEEEAARGI TIYAANVSMV HEYNGKEYLI NLIDTPGHVD FGGDVTRAMR AIDGAVVVCC
     AVEGVMPQTE TVLRQALKEK VKPVLFINKV DRLINELKLT PEELQGRFMK IIAEVNKLIE
     KMAPEEFKKD WLCDVVTGKV AFGSAYNNWA ISVPYMQRSG ISFKDIIDYC EQEKQGELAD
     RAPLHEVILD MAITHLPNPL QAQKYRIPNI WKGDSESTIG KSMVACDPNG PLAGVVTKII
     VDKHAGAISA CRLFSGRIKQ GDDLYLVGSK QKARAQQVSI FMGAERVQVP SISAGNICAL
     TGLREATAGE TVCSPSEILE PGFESLTHTS EPVITVAIEA KNTKDLPKLI EILRQIARED
     NTVRVEINEE TGEHLISGMG ELHIEVITNT KIGRDGGIEV DVGEPIVVYR ETITGTSPEI
     EGKSPNKHNK LYMIAEPMDE SVYAAYVEGK IHDEDYKKKT TADGEARLVE AGLEKEQAKR
     VMSIYNGNMI VNMTRGIVQL DEARELIIEG FKEGVRNGPL AAEKVQGVKI RLVDATFHED
     AIHRGPAQII PAVRFGVRDA VAQAKPVLLE PMQSVYINTP QDYMGDGMKE INNRRGQILD
     MEQEGDMSII KSSVPVAEMF GFAGAIRGAT QGRCLWSVEF SGFERVPAEL QPKIAKQIRD
     RKGLKSE