1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
| Type: | Domain | Name: | HflX-type guanine nucleotide-binding (G) domain |
| Description: | This entry represents the HflX-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 HflX-type is a widely distributed family of GTPases that interact with thelarge ribosomal subunit. The broad phylogenetic distribution pattern of HflX GTPases in Bacteria, Archaea, and Eukaryotes (including human) suggests abasic cellular function for this protein family.The HflX-type G domain is composed of six beta-strands and five alpha-helices []. It consists of the following conserved sequence motifs:the G1 motif (or P-loop), consensus GX4GK(S/T), which is responsible for interacting with the alpha and beta-phosphates of nucleotide di- andtriphosphates; the G2 variable effector loop (DXnT); the G3 motif (DX2G), which interacts with the gamma-phosphate of nucleotide triphosphates; and theG4 motif (NKXD), which conveys specificity for guanine nucleotides through hydrogen bonding to the base []. | Short Name: | G_HFLX_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
