EF2_METVS
ID EF2_METVS Reviewed; 727 AA.
AC P09604; A6UQ13;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=Mevan_0679;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3419900; DOI=10.1093/nar/16.16.7817;
RA Lechner K., Heller G., Bueck A.;
RT "Gene for the diphtheria toxin-susceptible elongation factor 2 from
RT Methanococcus vannielii.";
RL Nucleic Acids Res. 16:7817-7826(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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 (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; X12384; CAA30941.1; -; Genomic_DNA.
DR EMBL; CP000742; ABR54585.1; -; Genomic_DNA.
DR PIR; S01289; S01289.
DR RefSeq; WP_011972487.1; NC_009634.1.
DR AlphaFoldDB; P09604; -.
DR SMR; P09604; -.
DR STRING; 406327.Mevan_0679; -.
DR PRIDE; P09604; -.
DR EnsemblBacteria; ABR54585; ABR54585; Mevan_0679.
DR GeneID; 5325021; -.
DR KEGG; mvn:Mevan_0679; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000001107; 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.
FT CHAIN 1..727
FT /note="Elongation factor 2"
FT /id="PRO_0000091038"
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 603
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT CONFLICT 31
FT /note="D -> A (in Ref. 1; CAA30941)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="N -> D (in Ref. 1; CAA30941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 80160 MW; 8D0EC29D31D610E1 CRC64;
MGRRAKMVEK VKSLMETHDQ IRNMGICAHI DHGKTTLSDN LLAGAGMISK DLAGDQLALD
FDEEEAARGI TIYAANVSMV HEYNGKEYLI NLIDTPGHVD FGGDVTRAMR AIDGAVVVCC
AVEGVMPQTE TVLRQALKEK VKPVLFINKV DRLINELKLT PEELQGRFMK IIAEVNKLIE
KMAPEEFKKE WLCDVVTGKV AFGSAYNNWA ISVPYMQKSG ISFKDIIDYC EQEKQSELAD
KAPLHEVILD MAIKHLPNPL QAQKYRIPNI WKGDAESEVG KSMAMCDPNG PLAGVVTKII
VDKHAGSISA CRLFSGRIKQ GDELYLVGSK QKARAQQVAI FMGAERVQVP SISAGNICAL
TGLREATAGE TVCSPSKILE PGFESLTHTS EPVITVAIEA KNTKDLPKLI EILRQIGRED
NTVRIEINEE TGEHLISGMG ELHIEVITNT KIGRDGGIEV DVGEPIIVYR ETITGTSPEI
EGKSPNKHNK LYMIAEPMEE SVYAAYVEGK IHDEDFKKKT NVDAETRLIE AGLEREQAKK
VMSIYNGNMI VNMTKGIVQL DEARELIIEG FKEGVKGGPL ASERAQGVKI KLIDATFHED
AIHRGPSQII PAIRFGVRDA VSSAKPILLE PMQKIYINTP QDYMGDAIRE INNRRGQIVD
MEQEGDMAII KGSVPVAEMF GFAGAIRGAT QGRCLWSVEF SGFERVPNEI QTKVVAQIRD
RKGLKSE
