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IF2G_METM6
ID   IF2G_METM6              Reviewed;         410 AA.
AC   A9AAA4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
GN   OrderedLocusNames=MmarC6_1464;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-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; CP000867; ABX02277.1; -; Genomic_DNA.
DR   RefSeq; WP_012194197.1; NC_009975.1.
DR   AlphaFoldDB; A9AAA4; -.
DR   SMR; A9AAA4; -.
DR   STRING; 444158.MmarC6_1464; -.
DR   EnsemblBacteria; ABX02277; ABX02277; MmarC6_1464.
DR   GeneID; 5737478; -.
DR   KEGG; mmx:MmarC6_1464; -.
DR   eggNOG; arCOG01563; Archaea.
DR   HOGENOM; CLU_027154_0_1_2; -.
DR   OMA; NIGMVGH; -.
DR   OrthoDB; 25592at2157; -.
DR   PhylomeDB; A9AAA4; -.
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..410
FT                   /note="Translation initiation factor 2 subunit gamma"
FT                   /id="PRO_1000095098"
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;  43930 MW;  39B9CC3A536B4A5C CRC64;
     MAASNQSEVN IGMVGHVDHG KTSLTRKLTG VWTDTHSEEL KRGISIRLGY ADCEIKKCET
     CDEPECYTVD KKCDACGGKV DTLRKISFVD APGHETLMAT MLSGASLMDG AILVIAASEE
     CPQPQTKEHL MALDALGVEH ILIVQNKIDL VTEEAAIENY NQIKEFTKGT VAENAPIIPV
     SAHHGANLDV LLKAIQEFIP TPKRDETLTP KLYVARSFDV NKPGSEIKDL KGGVIGGSII
     QGALKVGDDL EIRPGIKVTE GNKTHWVPII TKIISLGVGN KKLKTASPGG LIGVGTELDP
     NLTKSDALSG SLAGLPGTLP ETLEKMVIKP QLLERVVGSQ DELIIEPLKT NEVLMLNVGT
     STTVGVTVSA RADKAEIKLK LPVCADKGDR VAISRKIGSR WRLIGYGIIL
 
 
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