ID EF2_HALSA Reviewed; 728 AA.
AC Q9HM85; P14823;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=Elongation factor 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; Synonyms=fus;
GN OrderedLocusNames=VNG_2654G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R1 / S9;
RX PubMed=2513185; DOI=10.1111/j.1432-1033.1989.tb15197.x;
RA Itoh T.;
RT "Sequence analysis of the peptide-elongation factor EF-2 gene, downstream
RT from those of ribosomal proteins H-S12 and H-S7, from the archaebacterial
RT extreme halophile, Halobacterium halobium.";
RL Eur. J. Biochem. 186:213-219(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00054}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG20686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17148; CAA35029.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG20686.1; ALT_INIT; Genomic_DNA.
DR PIR; B84415; B84415.
DR PIR; S07558; S07558.
DR RefSeq; WP_010903990.1; NC_002607.1.
DR AlphaFoldDB; Q9HM85; -.
DR SMR; Q9HM85; -.
DR STRING; 64091.VNG_2654G; -.
DR PaxDb; 64091-VNG_2654G; -.
DR GeneID; 68695138; -.
DR KEGG; hal:VNG_2654G; -.
DR PATRIC; fig|64091.14.peg.2063; -.
DR HOGENOM; CLU_002794_11_1_2; -.
DR InParanoid; Q9HM85; -.
DR OrthoDB; 6290at2157; -.
DR PhylomeDB; Q9HM85; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 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; Reference proteome.
FT CHAIN 1..728
FT /note="Elongation factor 2"
FT /id="PRO_0000091029"
FT DOMAIN 19..261
FT /note="tr-type G"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT MOD_RES 596
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT CONFLICT 282
FT /note="E -> A (in Ref. 1; CAA35029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 80397 MW; 589C6347614E76C6 CRC64;
MGRRKKIVEQ CERLMDNPEQ IRNIAIAAHV DHGKTTLTDN LLAGAGMISE DTAGQQLAMD
TEEDEQERGI TIDAANVSMT HEYEGDDHLI NLIDTPGHVD FGGDVTRAMR AVDGALVVVD
AVEGAMPQTE TVVRQALREG VKPTLFINKV DRLISELQEG PEEMQERLLS VIGDVNELIR
GMTEEKDDIE DWTVSVEDGT VAFGSALYKW GVSMPSMQRT GMDFGDIIDL ERSDKREELH
EQTPLADVVL DMVAEHFPNP IDAQPRRIPT VWRGDADSEI AESMRLVDED GEVVLMVTDI
GVDPHAGEIA AGRVFSGTLE KGQELYVSGT AGKNRVQSVG IYMGGEREEV DEVPAGNIAA
VTGLKDAIAG STVSNEEMTP FESIDHISEP VITKSIEAQN MDDLPKLIET LRQVSKEDPT
ISIEINEDTG EHLISGQGEL HLEVQTQRIE RNQGIPVTTG EPIVVYRETP TSDSQEVEGV
SPNRHNKFYI TVEQLSDDVL EEIRLGEVSM DMPEQERREV LQEAGMDKET SQDVENIIGR
NIFIDDTKGI QHLNETMELV VDGLTDSLED GPLAAEPVEG ALIRLHDARL HEDAIHRGPA
QVIPATRDAV HRALIDADIR LLEPIQDVRI DVPSEHMGAA SGEVQGRRGR VDDMYQEGDL
MVVEGIAPVD EMIGFSSDIR SATEGRASWN TENAGFRVMA DNLQREIIME IRERKGMKTE
LPESITHF
//
