EF2_PYRAB
ID EF2_PYRAB Reviewed; 732 AA.
AC Q9V1Z8; G8ZHR0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=PYRAB02760; ORFNames=PAB0187;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB49200.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69653.1; -; Genomic_DNA.
DR PIR; A75219; A75219.
DR RefSeq; WP_010867400.1; NC_000868.1.
DR AlphaFoldDB; Q9V1Z8; -.
DR SMR; Q9V1Z8; -.
DR STRING; 272844.PAB0187; -.
DR EnsemblBacteria; CAB49200; CAB49200; PAB0187.
DR GeneID; 1495166; -.
DR KEGG; pab:PAB0187; -.
DR PATRIC; fig|272844.11.peg.296; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR PhylomeDB; Q9V1Z8; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..732
FT /note="Elongation factor 2"
FT /id="PRO_0000091041"
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 597
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 732 AA; 82326 MW; D999CA1B62C89690 CRC64;
MGRREEMIAK IKELMLQPER IRNIGIAAHI DHGKTTLSDN LLAGAGMISE ELAGKQLVLD
FDEQEQARGI TINAANVSMV HNYEGKDYLI NLIDTPGHVD FGGDVTRAMR AIDGVIIVVD
AVEGVMPQTE TVVRQALREY VKPVLFINKV DRLIRELKLT PQQMMERFSK IIMDVNRLIQ
RYAPEEYKKQ WMVKVEDGSV AFGSAYYNWA LSVPFMKRTG VKFNEIIDLT LKGDHKTLRQ
KAPLHVVVLD MVVKHLPNPI EAQKYRIPHL WQGDINSDVG QAMLNCDPKG KMVMVVTKII
IDKHAGEVAT GRVWSGTVKS GQEVYLINTK RKARIQQVGI YMGPERINME AVPAGNIVAV
TGLRDAMAGE TVAEEPIEPF EALHYVSEPV VTVAIEAKNV KDLPRLIEAL RQLAKEDPTL
HVKIDEETGQ HLLSGMGELH LEVKLYKLKK DWGIDIDVSE PIVVYRESIT KPSPMVEGKS
PNRHNRFYIV VEPMPDEIYN AIKEGIIPEG RIKNPKEVAK KLAELGMDYE IARGIVDVYN
GNMFLDNTKG VQYLNEVMDL LIDGFHQAMD EGPLAKEPVM KVIVRLIDAQ VHEDNVHRGP
AQIYPAIRTA IHCAMMKSNP VLYEPYQKVI INIPYEYMGA VSREITQRRG QLVDMKQEGE
VMTIIAEAPV AEMFGFAGAI RSATSGRALW STEHAGFKRV PNELAQQIIR QIRQRKGLDP
NPPTEKDVCP LF
