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IF2G_META3
ID   IF2G_META3              Reviewed;         410 AA.
AC   A6UTL4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Maeo_0246;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000743; ABR55836.1; -; Genomic_DNA.
DR   RefSeq; WP_011972968.1; NC_009635.1.
DR   AlphaFoldDB; A6UTL4; -.
DR   SMR; A6UTL4; -.
DR   STRING; 419665.Maeo_0246; -.
DR   EnsemblBacteria; ABR55836; ABR55836; Maeo_0246.
DR   GeneID; 5327768; -.
DR   KEGG; mae:Maeo_0246; -.
DR   eggNOG; arCOG01563; Archaea.
DR   HOGENOM; CLU_027154_0_1_2; -.
DR   OMA; NIGMVGH; -.
DR   OrthoDB; 25592at2157; -.
DR   Proteomes; UP000001106; 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; 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   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; Zinc.
FT   CHAIN           1..410
FT                   /note="Translation initiation factor 2 subunit gamma"
FT                   /id="PRO_1000015788"
FT   DOMAIN          6..203
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          43..47
FT                   /note="G2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          90..93
FT                   /note="G3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          146..149
FT                   /note="G4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   REGION          181..183
FT                   /note="G5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         18..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
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         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   410 AA;  43828 MW;  47D31BABD565899A CRC64;
     MVKVKQSEIN IGMVGHVDHG KTSLTRQLTG TWTDTHSEEL KRGISIRLGY ADCEIMKCPK
     CGAPEAYSVS KTCPVCGTKT KMSRKISFVD APGHETLMAT MLSGASLMNG AILVIAATEK
     CPQPQTKEHL MALDALGIEN IIIVQNKIDL VDEERAKESY NEIKEFVKDT VAEKAPIIPI
     SAHHGANIDI LLNAIEDLMP TPEMDEGAPA RLYVARSFDI NKPGCEISKL KGGVIGGSII
     QGTLNSGEKI EIKPGLKIVE GNKIRWESII TKITSLGVGG KTVKVAHPGG LVGIGTELDP
     ALTKSDSLSG CVAGAPGTLP ETLSEITVQT KLLDRIVGSD EELIISPLKS NEALMLNVGT
     ATTVGIITSA RGDMADMKLK LPICADKGDR IAMSRRIGSR WRLIGYGIIQ
 
 
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