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Database: UniProt
Entry: M1QGA1_METMZ
LinkDB: M1QGA1_METMZ
Original site: M1QGA1_METMZ 
ID   M1QGA1_METMZ            Unreviewed;       444 AA.
AC   M1QGA1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Translation initiation factor 2 subunit gamma {ECO:0000256|HAMAP-Rule:MF_00119};
DE            EC=3.6.5.3 {ECO:0000256|HAMAP-Rule:MF_00119};
DE   AltName: Full=aIF2-gamma {ECO:0000256|HAMAP-Rule:MF_00119};
DE   AltName: Full=eIF-2-gamma {ECO:0000256|HAMAP-Rule:MF_00119};
GN   Name=eif2g {ECO:0000256|HAMAP-Rule:MF_00119};
GN   ORFNames=MmTuc01_0601 {ECO:0000313|EMBL:AGF96019.1};
OS   Methanosarcina mazei Tuc01.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1236903 {ECO:0000313|EMBL:AGF96019.1, ECO:0000313|Proteomes:UP000011718};
RN   [1] {ECO:0000313|EMBL:AGF96019.1, ECO:0000313|Proteomes:UP000011718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc01 {ECO:0000313|EMBL:AGF96019.1,
RC   ECO:0000313|Proteomes:UP000011718};
RX   PubMed=23704185;
RA   Assis das Gracas D., Thiago Juca Ramos R., Vieira Araujo A.C., Zahlouth R.,
RA   Ribeiro Carneiro A., Souza Lopes T., Azevedo Barauna R., Azevedo V.,
RA   Cruz Schneider M.P., Pellizari V.H., Silva A.;
RT   "Complete Genome of a Methanosarcina mazei Strain Isolated from Sediment
RT   Samples from an Amazonian Flooded Area.";
RL   Genome Announc. 1:E00271-13(2013).
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:0000256|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:0000256|ARBA:ARBA00001874, ECO:0000256|HAMAP-
CC         Rule:MF_00119};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00119};
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC       {ECO:0000256|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:0000256|ARBA:ARBA00005388, ECO:0000256|HAMAP-Rule:MF_00119}.
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DR   EMBL; CP004144; AGF96019.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1QGA1; -.
DR   KEGG; mmaz:MmTuc01_0601; -.
DR   HOGENOM; CLU_027154_0_1_2; -.
DR   Proteomes; UP000011718; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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   NCBIfam; TIGR03680; eif2g_arch; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR   Pfam; PF09173; eIF2_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00119};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00119};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00119}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00119};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00119};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00119};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00119}; Zinc {ECO:0000256|HAMAP-Rule:MF_00119}.
FT   DOMAIN          39..236
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         51..56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         76
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         179..182
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         214..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
SQ   SEQUENCE   444 AA;  47833 MW;  23B3896273B064D8 CRC64;
     MKSESPREEK SPEGTGFGKN TCLISDYFHS TGGNYNLSQP CVNIGMVGHV DHGKTTLVRA
     LSGVWTDTHS EEVKRGISIR LGYADSSFMK CPKCPEPQCY TVEKTCPNCG EKTEEHRTVS
     FVDAPGHETL MATMLSGAAI MDGAVLVIAA NEDCPQPQTK EHLMALDIIG IKNIVIVQNK
     IDLVSREKII ENYHQIKEFV KGTVAENAPV IPISAQQNIN IDILIDALET QIPTPSHKVD
     KPASMLIARS FDINKPGASI EEIRGGVIGG TLTEGVLHPG DELEIRPGIK VTTEGSTRWI
     PILTTVSSIY AGATKVDEAT PGGLLAVGTY LDPTLTKGDS LTGQMAGVPG TLPETRHQFV
     MELHLLDRVV GVTREEKINE IKTSEPLMLN IGTATTVGVV TSARKNEAQV SLKRPISAAI
     GAMVAISRRV DSRWRLIGVG VIKS
//
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