EF2_KORCO
ID EF2_KORCO Reviewed; 739 AA.
AC B1L7Q0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, 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=Kcr_0117;
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX NCBI_TaxID=374847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8;
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB06877.1; -; Genomic_DNA.
DR RefSeq; WP_012308774.1; NC_010482.1.
DR AlphaFoldDB; B1L7Q0; -.
DR SMR; B1L7Q0; -.
DR STRING; 374847.Kcr_0117; -.
DR EnsemblBacteria; ACB06877; ACB06877; Kcr_0117.
DR GeneID; 6093406; -.
DR KEGG; kcr:Kcr_0117; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR InParanoid; B1L7Q0; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR PhylomeDB; B1L7Q0; -.
DR Proteomes; UP000001686; 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..739
FT /note="Elongation factor 2"
FT /id="PRO_0000408960"
FT DOMAIN 19..261
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 739 AA; 83328 MW; 61BD97764307B888 CRC64;
MQKYKKVIDH LQELMRDPRN IRNIGIIAHV DHGKTTLSDN LLSAAGMISD KMAGEMRALD
YHEIEQQRGI TIKAANISLY YQRDGKEFAI NLVDTPGHID FTGHVTRSLR VIDGAIVVVD
SVEEVMVQTE TVTRQALEER VRPLLFINKI DRLIKELKLT PQEIQQKILR IIRDFNGLIE
AYGEPEFREK WKVKWDNDSV AFGSALHGWG LTNSIAAKKG IRFSDIVDIY NEDPEGLALR
RDIPVHEALL DMVALHVPDP IEAQSYRVER LWRDKQDEEL FNALKNCDPN GPLIMGVNAV
RIDPHAGIVV TGRVFSGTLR EGEDVYLINA KKKQKIQQTS IYMGPYRMRM DEIPAGNIAA
VLGLTSASSG ETVVADAIKD RVISGFEAIR YVTEPVVTVS VEAKNPQDLP KLIDTLRKLT
LQDPNLVMIH NQETGEILLK GTGELHLEIS LYEVRKAGLE FDVSEPTVVY RESVRGTSDV
VLAKSPNKLN RIWVTASPLN DEVVALIREG RVNERMDSRT LAKVLREEGK MDTEDARNVW
TIDEENYNLF INRTVGVQRL DEVREILRQG FMWVMKEGPL AGEPVMGVAI RLVNAMIHED
PAHRGPAQLT PAVRKAIFGA MLSANPVLLE PIYEIQVSTP PELIGSVISL ISQKRGKVVG
IEERGRISIV KGFIPVRETL GGFSNEMRSM TSGRAFWQTK FSHWEPLPKS LMEQVALEIR
RRKGMKEELP KAEEYMDTL
