1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
| Type: | Domain | Name: | EngB-type guanine nucleotide-binding (G) domain |
| Description: | This entry represents the EngB-type G domain.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 EngB-type is widespread, but not ubiquitous in all three superkingdoms(missing, for example, from the Crenarchaeota, Caenorhabditis, and Drosophila). Proteins of the EngB-type GTPase family are involved in thebiogenesis of ribosomes and are essential for the survival of a wide range of bacteria [, , ].The EngB-type GTPase is comprised of a central beta-sheet flanked by alpha- helices, in which semi-conserved residues involved innucleotide binding are located in five motifs, called G1-G5. The G1 region (GxxxxGKS) forms the P-loop that is responsible for binding the phosphategroups of the guanine nucleotide. The G2 region corresponds to the switch I loop, which contains the consensus motif PGxT. The invariant threonine residueis responsible for binding a magnesium ion required for catalysis. The G3 region corresponds to the Walker B motif (DxxG), which forms part of switchII. The G4 (TKxD) and G5 motifs are involved in interactions with the guanine moiety of the substrate [, ]. | Short Name: | G_ENGB_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
