1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
| Type: | Domain | Name: | OBG-type guanine nucleotide-binding (G) domain |
| Description: | The P-loop guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling,and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state andan active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G)domain that is responsible for binding and hydrolysis of guanine nucleotides.Within the translation factor-related (TRAFAC) class of P-loop GTPases, the OBG family comprises a group of high-molecular mass GTPases conserved frombacteria to eukaryotes. The OBG family consists of []: Obg from bacteria and eukaryotes [, ].DRG from eukaryotes and archaea. DRG proteins may regulate fundamental cellular processes through RNA binding [].Nog1 from eukaryotes and archaea. It is involved in the assembly of the large ribosomal subunit.Yyaf/YchF from bacteria and eukaryotes. It consists of a central G domain, flanked by a coiled-coil domain and a TGS (ThrRS, GTPase, SpoT) domain.Members of this subfamily bind and hydolyze ATP more efficiently than GTP [, ].Ygr210 from archaea and fungi.The OBG-type G domain has a mononucleotide binding fold typical for the P-loop NTPases. A six-stranded mostly parallel beta-sheet is flanked by alpha-heliceson both sides. The OBG-type G domain contains five characteristic sequence motifs, termed G1-G5, involved in nucleotide bindingand hydrolysis. The G1/Walker A motif (GXXXXGK(S/T)), also referred to as P- loop, helps to position the triphosphate moiety of the bound nucleotide. TheG2 (X(T/S)X) and G3/Walker B (hhhDXXG) motifs are involved in the coordination of a Mg(2)+ ion that is required for nucleotide binding and hydrolysis.Specificity in nucleotide binding is conferred by the G4 motif, which has a (N/T)KXD signature in guanine nucleotide binding P-loop NTPases. The G5 motif((T/G)(C/S)A) supports guanine base recognition [, , , ]. | Short Name: | G_OBG |
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
