IF2G_HALS3
ID IF2G_HALS3 Reviewed; 414 AA.
AC B0R6Y7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor 2 subunit gamma {ECO:0000255|HAMAP-Rule:MF_00119};
DE EC=3.6.5.3 {ECO:0000255|HAMAP-Rule:MF_00119};
DE AltName: Full=aIF2-gamma {ECO:0000255|HAMAP-Rule:MF_00119};
DE AltName: Full=eIF-2-gamma {ECO:0000255|HAMAP-Rule:MF_00119};
GN Name=eif2g {ECO:0000255|HAMAP-Rule:MF_00119}; OrderedLocusNames=OE_3876R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00119};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00119};
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
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DR EMBL; AM774415; CAP14506.1; -; Genomic_DNA.
DR RefSeq; WP_010903512.1; NC_010364.1.
DR AlphaFoldDB; B0R6Y7; -.
DR SMR; B0R6Y7; -.
DR EnsemblBacteria; CAP14506; CAP14506; OE_3876R.
DR GeneID; 5953221; -.
DR GeneID; 62887370; -.
DR KEGG; hsl:OE_3876R; -.
DR HOGENOM; CLU_027154_0_1_2; -.
DR OMA; NIGMVGH; -.
DR PhylomeDB; B0R6Y7; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00119; eIF_2_gamma; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR022424; TIF2_gsu.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03680; eif2g_arch; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Initiation factor; Magnesium; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..414
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_1000095097"
FT DOMAIN 7..204
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 16..23
FT /note="G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 44..48
FT /note="G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 147..150
FT /note="G4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 182..184
FT /note="G5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 182..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
SQ SEQUENCE 414 AA; 43781 MW; 8729497CF020BD6D CRC64;
MADEHRQPEV NIGLVGHVDH GKTTLVRALS GEWTDQHSEE MKRGISIRLG YADATLRRCP
DCDEPECYTV AETCPEHDTA TEIERTVSFV DAPGHETLMA TMLSGAALMD GAVLVVGANE
PVPQPQTEEH LMALDIIGIE NIVIAQNKVD LVDAEEARQN YEEIQAFVEG TVAEDAPVVP
VSAEQEINVD LVIDALQTEI ATPDRDPSAD PLLYAARSFD INRPGTEWGG LLGGVIGGSL
VDGELEAGDE LELRPGREVE EGGKTEWRPV TTDVRSLQAG GEDVDSASPG GLLGVGTGLD
PSLTKGDALA GQVAGPPGSL PPTWESFEMD VDLLERLVGA ADGEQIDDIS TGEPLMLTVG
TATTVGSVTS ARDGECEVAL KRPVCAPAGA KIAINRRVGA RWRLIGVGTL TESE
