ID R1E5A2_NANST Unreviewed; 734 AA.
AC R1E5A2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
GN ORFNames=Nst1_257 {ECO:0000313|EMBL:EOD42527.1};
OS Nanobsidianus stetteri.
OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC Nanopusillaceae; Nanobsidianus.
OX NCBI_TaxID=1294122 {ECO:0000313|EMBL:EOD42527.1, ECO:0000313|Proteomes:UP000053279};
RN [1] {ECO:0000313|EMBL:EOD42527.1, ECO:0000313|Proteomes:UP000053279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Podar M., Makarova K.S., Graham D.E., Wolf Y.I., Koonin E.V.,
RA Reysenbach A.-L.;
RT "Insights into archaeal evolution and symbiosis from the genomes of a
RT Nanoarchaeon and its crenarchaeal host from Yellowstone National Park.";
RL Submitted (FEB-2013) 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.
CC {ECO:0000256|ARBA:ARBA00024731}.
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:EOD42527.1}.
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DR EMBL; APJZ01000002; EOD42527.1; -; Genomic_DNA.
DR AlphaFoldDB; R1E5A2; -.
DR PATRIC; fig|1294122.7.peg.249; -.
DR Proteomes; UP000053279; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 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 InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
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; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:EOD42527.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EOD42527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053279}.
FT DOMAIN 16..263
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 734 AA; 83074 MW; DAFDF956806CCFFD CRC64;
MASLTERILQ VMNNPNNIRN IGIIAHIHHG KTTLTDSLLA GAGMLAEELA GEAMFTWWHE
TERQREMTVY GAAVSMVHNY ENQDYLINLI DTPGHVEFSG QVTRATRAID GAIVVVDFVD
GIMPQTETVL RTALKEYVKP VLFINKTDRA ITELKLSPQQ IMERIGKIVI EVNRLIDKYS
PPEFKGKWNV NVNDGSVAFG SAKFHWALSV PFMKKYNVSF KDVIEIYNQF LEDKEKLKEE
MRKKAPVAKV VLDMVIRHLP SPVEAQKYRI PHIWKGDINS DVGKAMLNLD SNGPIVINVT
NVIIDKVSKQ EIATARIFSG TLSKGDDVYL IQAGRQIKIQ QVAIWKGIQR INVDSAKAGN
IIALVGIKGL YPGETIVGKV QDPKSVETFE EMRHWLDPVV TKSFEPKNPN DLPKLIETLD
LLTREDPTIK VEQKRDTGEI IVSGLGDLHL QIIEYRVQND FGIPVKVGDP IVIYRESVNK
ATQVYEGKSP NKHNKIYIQI EPLPYEIYEK MREYIREGKL PEGRIKKEDL WKVFNEIGFD
KEEARRIIMV HNGNVLIDMT RGIVHLPEVI EYIVEGFKEV MDQGPLAWEP GIMMKVKLID
AVLHEDAIHR GPAQIIPAAK EAIKSAILEQ PTLYEPLQII RIDAPPESVG DVTSILQSRR
GQILEMNIEE ERAMVKAKLP VANIFGFTDE LRSATSGKGV WFLEDQVYEK VPKDLQQQII
DSIRKRKGIP EGVH
//
