ID   EF2_CENSY               Reviewed;         730 AA.
AC   A0RW30;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CENSYa_0915;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK77547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RW30; -.
DR   SMR; A0RW30; -.
DR   STRING; 414004.CENSYa_0915; -.
DR   EnsemblBacteria; ABK77547; ABK77547; CENSYa_0915.
DR   KEGG; csy:CENSYa_0915; -.
DR   PATRIC; fig|414004.10.peg.846; -.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   OMA; GVMTQTE; -.
DR   Proteomes; UP000000758; Chromosome.
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; Reference proteome.
FT   CHAIN           1..730
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000408958"
FT   DOMAIN          18..238
FT                   /note="tr-type G"
FT   REGION          711..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         147..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   MOD_RES         595
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   730 AA;  80421 MW;  DD027F817668FADA CRC64;
     MVKFKSTEQV LKIIKNKDQI RNFGVIAHVD HGKTTMSDSL LAHSGIIAPS AAGQALAMDF
     DKEEQERGIT IYQANVTLHY TQKEDEYVIN MIDTPGHVDF SGRVIRSLRA IDGAVVVCDA
     VEGIMTQTET VTRMALEELV RPVLFINKVD RLIKELRLTP EKMQETLASV VSNFNQLLDT
     YAEPEYRDAW KVSIQDASVT FGSAKDKWAI NVDVMKEKGI TFKDVIDAYS EGKVDELVER
     APLADAVLGM VVKHHPPPHV AQKYRIPKIW HGDLESDIGK ALLACKDDGP TIMMVVNMVL
     DKAAGSVAIG RLFSGTIRDG QTVNIIDAKR EGRVQSVNFF MGNQREQVGE LGAGNIPALI
     GLADSRAGNT LSSIAGIKVF EGVSYVSEPV VQIAVEPKHP KDLPRLVEVL KQLTIEDPNL
     VVKIDEESGE TIVSGMGVLH LDVATHRIQD AKVEIITSEP LINYRETVSS GCEAVMSKSP
     NRHNKIFMRV EPLEPTIGDM LRSGRISEMK DKKEMADLLK EQGWDTDTVK RVMKLDPRGN
     VMINGTKGVQ FVQESTDSIN SGFDDAMKEG PMCREQMRDC KFTFTHFVPH EDAAHRGLSQ
     LGPASRRACM GALLTAGTSL LEPILAIEVR VPTDMVGNVA TVLSSKSGKV MDMIQKGPAS
     IVTGEIPASE TFTLSEEMRG QTAGKAMWNS HFKRWAEVPK SRLAESISDI RKRKGLAPDP
     PTVSEFIDRE