ID EF2_METMT Reviewed; 730 AA.
AC O93637;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 08-NOV-2023, entry version 114.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=ef-2, fus;
OS Methanococcoides methylutens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=2226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33938 / DSM 2657 / BCRC 16168 / OCM 158 / TMA-10;
RX PubMed=9845338; DOI=10.1016/s0014-5793(98)01375-1;
RA Thomas T., Cavicchioli R.;
RT "Archaeal cold-adapted proteins: structural and evolutionary analysis of
RT the elongation factor 2 proteins from psychrophilic, mesophilic and
RT thermophilic methanogens.";
RL FEBS Lett. 439:281-287(1998).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF022779; AAC79197.1; -; Genomic_DNA.
DR PIR; T44066; T44066.
DR RefSeq; WP_048195088.1; NZ_JRHO01000014.1.
DR AlphaFoldDB; O93637; -.
DR SMR; O93637; -.
DR OrthoDB; 6290at2157; -.
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 CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd01514; Elongation_Factor_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00490; aEF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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..730
FT /note="Elongation factor 2"
FT /id="PRO_0000091035"
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 596
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 730 AA; 80538 MW; 49450034651A20EE CRC64;
MGRRKKMVER VTALMSNPVM IRNIAIIAHI DHGKTTLSDN LLAGAGMISK DLAGRQLFMD
SDEEEQERGI TIDSANVSMV HEFEDEEYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVID
AVEGTMPQTE TVLRQALKEH VRPVLFINKV DRLINELQVD AQEMQIRLGK LIDHVNKLIK
GMNEERYNQG WRVDAAEGTV AFGSALYNWA ISVPMMQKTG VSFGEVFDYC RAEDMKSLGE
KCPLHEAVND MVIRFLPSPI DAQEDRVGVI WHGDLEAGIG KQMAVADATG DLAFMVTDIS
MDPHAGEVST GRLFSGSLSR GMEVYVSGAA KPNRIQQVGV FMGPERLEVD KIPAGNIAAV
TGLRDAIVGS TVTTLDGMSP FESIRHASEP VVTVAVEAKH MKDLPKLVEV LRQVAKEDPT
LKITLDEETG EHLMAGMGEL HLEVIAHRIE RDKGVEISTT PPIVVYRETI TGTAGPVEGK
SPNRHNRFYV VVEPLEPEVR ELIREGEISM RMPELERREK LIAAGLDKDE AKRIADIFES
NAYFDMTKGI QHLNETMELV LEGFVEVMKA GPLSKEPCMG VKVKLMDAKL HEDAVHRGPA
QVIPASRQAI QAAMLMADDT LFEPYQKVFI QTPQEQMGGA TKEIQGRRGI IIDMTSEGDT
TIIESKAPVS ELFGFAGDIR SATEGRAMWS TEFVGFEPLP TNMITEVVSG IRERKGLKKD
LPQAQDFMSM
//
