IF2G_PYRHO
ID IF2G_PYRHO Reviewed; 411 AA.
AC O59410;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=PH1706;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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, ECO:0000305}.
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DR EMBL; BA000001; BAA30820.1; -; Genomic_DNA.
DR PIR; E71178; E71178.
DR RefSeq; WP_010885772.1; NC_000961.1.
DR AlphaFoldDB; O59410; -.
DR SMR; O59410; -.
DR STRING; 70601.3258137; -.
DR EnsemblBacteria; BAA30820; BAA30820; BAA30820.
DR GeneID; 1442553; -.
DR KEGG; pho:PH1706; -.
DR eggNOG; arCOG01563; Archaea.
DR OMA; NIGMVGH; -.
DR OrthoDB; 25592at2157; -.
DR Proteomes; UP000000752; 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 GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 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; IPR044127; eIF2g_dom_2.
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; Zinc.
FT CHAIN 1..411
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_0000137461"
FT DOMAIN 9..203
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 18..25
FT /note="G1"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 46..50
FT /note="G2"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 90..93
FT /note="G3"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 146..149
FT /note="G4"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT REGION 181..183
FT /note="G5"
FT /evidence="ECO:0000250|UniProtKB:Q980A5"
FT BINDING 21..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 181..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
SQ SEQUENCE 411 AA; 45099 MW; 0EB338A5D887744A CRC64;
MGERRKTRQA EVNIGMVGHV DHGKTTLTKA LTGVWTDTHS EELRRGITIK IGFADAEIRR
CPNCGRYSTS PVCPYCGHET EFVRRVSFID APGHEALMTT MLAGASLMDG AILVIAANEP
CPRPQTREHL MALQIIGQKN IIIAQNKIEL VDKEKALENY RQIKEFIKGT VAENAPIIPI
SALHGANIDV LVKAIEDFIP TPKRDPNKPP KMLVLRSFDV NKPGTPPEKL VGGVLGGSIV
QGKLKVGDEI EIRPGIPYEE HGRIRYEPIT TEIVSLQAGG QFVEEAYPGG LVGVGTKLDP
YLTKGDLMAG NVVGKPGKLP PVWDSLRLEV HLLERVVGTE QELRVEPIKR KEVLLLNVGT
ARTMGLVTNL GKDEIEVKLQ IPVCAEPGDR VAISRQIGSR WRLIGYGIIK E
