EF2_THEKO
ID EF2_THEKO Reviewed; 732 AA.
AC Q5JFZ3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=TK0309;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD84498.1; -; Genomic_DNA.
DR RefSeq; WP_011249264.1; NC_006624.1.
DR AlphaFoldDB; Q5JFZ3; -.
DR SMR; Q5JFZ3; -.
DR IntAct; Q5JFZ3; 1.
DR MINT; Q5JFZ3; -.
DR STRING; 69014.TK0309; -.
DR EnsemblBacteria; BAD84498; BAD84498; TK0309.
DR GeneID; 3234818; -.
DR KEGG; tko:TK0309; -.
DR PATRIC; fig|69014.16.peg.308; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR InParanoid; Q5JFZ3; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR PhylomeDB; Q5JFZ3; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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..732
FT /note="Elongation factor 2"
FT /id="PRO_0000091045"
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 597
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 732 AA; 81990 MW; 87C5259E81C54BA9 CRC64;
MGRREEMIAK IKELMTQPER IRNMGIAAHI DHGKTTLSDN LLAGAGMISE ELAGKQLVLD
FDEQEQARGI TINAANVSMV HNYEGNDYLI NLIDTPGHVD FGGDVTRAMR AIDGAIIVVD
AVEGVMPQTE TVLRQALREY VKPVLFINKV DRLIKELKLT PQQMQERFVK VITDVNRLIR
RYAPPEFKDK WLVKVEDGSV AFGSAYYNWA LSVPYMKKTG VSFKDIIDLT NAGDLKTLRK
KAPLHVVVLD MVVKHLPNPL EAQKYRIPHL WRGDINSDVG QAMMNCDPKG PMTMVVTKII
LDKHAGEVAT GRVWSGTVKT GQEVYLINSK RKARIQQVGI YMGPERINME AVPAGNIVAV
TGLRDAMAGE TVSVQQIEPF EALHYTSEPV VTVAIEAKNV KDLPKLVEAL RQLAKEDPTL
HVKIDEETGQ HLLSGMGELH LEVKLHRLKT EWKLDVEVSP PIVVYRESVT KQSPIVEGKS
PNKHNRFYIT VEPMPDEIYQ AIREGEIPEG RPKDPKAVAK KLAELGMDYE IAKGIVDIYN
GNMFLDNTKG IQYLNEVMDL LVDGFHQAMD EGPLAKEPVM KVIVRLHDAK IHEDNVHRGP
AQIYPAIRSA IHCAMMKAGP VLYEPYQKVI INVPYEYMGA VSRELNQRRG QLIDMRQEGE
VMIIIGEAPV AEMFGFAGAI RGATSGKALW TTEHAGFKRV PNELAQQIIR QIRQRKGLDP
NPPKEQDVCP QQ
