IF2G_HALSA
ID IF2G_HALSA Reviewed; 414 AA.
AC Q9HNK9; O93626;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=VNG_2056G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A9;
RX PubMed=9818089; DOI=10.1080/15216549800204022;
RA Hasegawa Y., Sawaoka N., Kado N., Ochi M., Itoh T.;
RT "Cloning and sequencing of the homologues of both the bacterial and
RT eukaryotic initiation factor genes (hIF-2 and heIF-2gamma) from archaeal
RT Halobacterium halobium.";
RL Biochem. Mol. Biol. Int. 46:495-507(1998).
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: 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; AB015764; BAA35082.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG20211.1; -; Genomic_DNA.
DR PIR; G84355; G84355.
DR PIR; T43851; T43851.
DR RefSeq; WP_010903512.1; NC_002607.1.
DR AlphaFoldDB; Q9HNK9; -.
DR SMR; Q9HNK9; -.
DR STRING; 64091.VNG_2056G; -.
DR PaxDb; Q9HNK9; -.
DR EnsemblBacteria; AAG20211; AAG20211; VNG_2056G.
DR GeneID; 5953221; -.
DR GeneID; 62887370; -.
DR KEGG; hal:VNG_2056G; -.
DR PATRIC; fig|64091.14.peg.1568; -.
DR HOGENOM; CLU_027154_0_1_2; -.
DR InParanoid; Q9HNK9; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 25592at2157; -.
DR PhylomeDB; Q9HNK9; -.
DR Proteomes; UP000000554; 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; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..414
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_0000137452"
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"
FT CONFLICT 64
FT /note="E -> D (in Ref. 1; BAA35082)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..319
FT /note="QVAGPPGS -> PGRRGRPAG (in Ref. 1; BAA35082)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..343
FT /note="DG -> AA (in Ref. 1; BAA35082)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="L -> P (in Ref. 1; BAA35082)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..371
FT /note="SA -> RP (in Ref. 1; BAA35082)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="Missing (in Ref. 1; BAA35082)"
FT /evidence="ECO:0000305"
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
