AC   MF_00119;
DC   Protein; auto
TR   HAMAP; MF_00119; -; 1; level=0
XX
Names: eIF_2_gamma
XX
ID   IF2G
DE   RecName: Full=Translation initiation factor 2 subunit gamma;
DE            EC=3.6.5.3;
DE   AltName: Full=aIF2-gamma;
DE   AltName: Full=eIF-2-gamma;
GN   Name=eif2g;
XX
CC   -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC       forming a ternary complex with GTP and initiator tRNA.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EIF2G subfamily.
XX
DR   Pfam; PF09173; eIF2_C; 1; trigger=no
DR   Pfam; PF00009; GTP_EFTU; 1; trigger=no
DR   NCBIfam; TIGR03680; eif2g_arch; 1; trigger=no
DR   NCBIfam; TIGR00231; small_GTP; 1; trigger=no
DR   PROSITE; PS51722; G_TR_2; 1; trigger=yes
XX
KW   Initiation factor
KW   Protein biosynthesis
KW   GTP-binding
KW   Hydrolase
KW   Nucleotide-binding
KW   Metal-binding
KW   Magnesium
case <FTGroup:1>
KW   Zinc
end case
XX
GO   GO:0005525; F:GTP binding
GO   GO:0003746; F:translation elongation factor activity
XX
FT   From: IF2G_SACS2 (Q980A5)
FT   BINDING         19..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: D-H-G-K-[ST]-[ST]
FT   BINDING         149..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: N-K-[VI]-[DE]
FT   BINDING         184..186
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: S-A-x
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: [ST]
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: G
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: [ST]
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
XX
Size: 408-443;
Related: None;
Template: Q980A5; Q8U082; Q9V1G0; O29663; Q58657;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.25 2023/06/01
//