ID A0A498GDW1_9EURY Unreviewed; 729 AA.
AC A0A498GDW1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891, ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-2 {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN ORFNames=D3D02_03110 {ECO:0000313|EMBL:RLM90768.1};
OS Halobellus sp. Atlit-38R.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=2282131 {ECO:0000313|EMBL:RLM90768.1, ECO:0000313|Proteomes:UP000277703};
RN [1] {ECO:0000313|EMBL:RLM90768.1, ECO:0000313|Proteomes:UP000277703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Atlit-38R {ECO:0000313|EMBL:RLM90768.1,
RC ECO:0000313|Proteomes:UP000277703};
RA Turgeman-Grott I.;
RT "Pervasive acquisition of CRISPR memory from multiple replicons driven by
RT inter-species mating of archaea.";
RL Submitted (SEP-2018) 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. {ECO:0000256|ARBA:ARBA00024731,
CC ECO:0000256|HAMAP-Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00054}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLM90768.1}.
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; QXIJ01000002; RLM90768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498GDW1; -.
DR OrthoDB; 6290at2157; -.
DR Proteomes; UP000277703; Unassembled WGS sequence.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|HAMAP-Rule:MF_00054,
KW ECO:0000313|EMBL:RLM90768.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}; Reference proteome {ECO:0000313|Proteomes:UP000277703}.
FT DOMAIN 19..261
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT MOD_RES 597
FT /note="Diphthamide"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 729 AA; 80691 MW; 9B30AB9272180D93 CRC64;
MGRRKKIVQE CEQLMDKPEQ IRNIAIAAHV DHGKTTLTDN LLAGAGMIAD EGEATRLMMD
TEEDEQERGI TIDAANVSMT HEYGEDNHLI NLIDTPGHVD FGGDVTRAMR AVDGALVVVD
AVEGAMPQTE TVVRQALREG VKPALFINKV DRLISELQEG PQEMQERLMD VIGDVNELIR
GMTEDMDDVD DWTVSVEDGT VAFGSALYKW GVSAPSMAET GIGFPEIIEM ERNDQRRELH
EQTPLSDVVL DMVAEHFPDP LDAQPRRIPR VWRGDDESEI SRQMQEVDDD GEVVFMVTDI
SMDPHAGEIA TGRLFSGTIK QGQELYVSGT AGKNRVQSVG IFMGGEREEL DRGVPAGNIA
AVTGLRDAIA GSTVSSIEMT PFESIEHISE PVITKSVEAK NMDDLPKLIE TLQQVAKEDP
TIRVEINEDT GEHLISGQGE LHLEVITQRI QKNQGIPVQT GEPIVVYREA PQQESREVEG
VSPNRHNKFY ITVEPLSDDV VETIKLGEAS MDMPELERRE ALQEAGMDKD TSQNVEHIHG
TNILIDDTKG IQHLNETMEL VIEGLEEALN DGPLANEPVE GALLRLHDAK LHEDTIHRGP
AQVIPAVRDA VHRSLIDADI KLLEPIQNVR IDVPSEHMGS ASGEIQGRRG RVDDMYQEGD
LMVIEGIAPV EEMIGFSSDI RSATEGRASW NTENAGFRVL SDNLQREKIM EIRERKGMKL
ELPSSVDQF
//
