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Entry: A0A125RD33_9EURY
LinkDB: A0A125RD33_9EURY
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ID   A0A125RD33_9EURY        Unreviewed;       404 AA.
AC   A0A125RD33;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=TL18_06080 {ECO:0000313|EMBL:AMD17623.1};
OS   Methanobrevibacter sp. YE315.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=1609968 {ECO:0000313|EMBL:AMD17623.1, ECO:0000313|Proteomes:UP000057992};
RN   [1] {ECO:0000313|EMBL:AMD17623.1, ECO:0000313|Proteomes:UP000057992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE315 {ECO:0000313|EMBL:AMD17623.1,
RC   ECO:0000313|Proteomes:UP000057992};
RA   Ouwerkerk D., Gilbert R.A., Klieve A.V., Martinez E.;
RT   "Genome sequence of Methanobrevibacter sp. YE315.";
RL   Submitted (JAN-2015) 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: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; CP010834; AMD17623.1; -; Genomic_DNA.
DR   RefSeq; WP_067042893.1; NZ_CP010834.1.
DR   AlphaFoldDB; A0A125RD33; -.
DR   STRING; 1609968.TL18_06080; -.
DR   GeneID; 28487410; -.
DR   KEGG; meye:TL18_06080; -.
DR   PATRIC; fig|1609968.3.peg.1253; -.
DR   OrthoDB; 7798at2157; -.
DR   Proteomes; UP000057992; 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; 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   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   Pfam; PF03144; GTP_EFTU_D2; 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          4..201
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         16..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         20
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT   BINDING         179..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
SQ   SEQUENCE   404 AA;  43321 MW;  85D7B72CB9E54FD7 CRC64;
     MNVQSDVNIG LVGHVDHGKT TLTKALSGIW TDTHSEETKR GISIRLGYAD IEFRKCPNCD
     EPECYTTSDK CEICGTETEL IRKVSFVDAP GHETLMATML SGAAIMDGAV LVIAANETCP
     QPQTKEHLMA LDVIGVKDVI VVQNKIDIVS KERAIESYNE IREFVKGTCA EDALIIPVSA
     QQGANVDILI EAMLKQIQPP ERNIDDTALM HVARSFDINK PGSGADKIKG GVIGGTLVQG
     KFKLGDTIEI RPGPTNEGKR ITLKSEIIGL EANGKQVEEI GPGGLVGIAT KLDPSLTKSD
     SLSGTVAGEE GTLPDVLDSF KMEANLLDRV VGTKEERDVA PIKIKEPLMI NCGTTTTIGV
     VTSAKKNDVD VVLKLPVCAS PGDRVALSRR VGARWRLIGY GIIK
//
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