| Type: | Family | Name: | Uncharacterised conserved protein UCP036888, signal transduction HD-GYP-like, PA5346 type |
| Description: | Members of this group contain a modified version of the HD-GYP domain and an uncharacterised N-terminal domain. There is currently no experimental data for members of this group.HD-GYP is a conserved domain found in response regulator modules of various signal transduction systems. The involvement of the HD-GYP domain in signal transduction was originally proposed on the basis of its association with CheY-like and other signal transduction domains [] and was later directly demonstrated experimentally by showing that RpfG is involved in regulation of the biosynthesis of extracellular endoglucanase and polysaccharide [].A modification of the HD-GYP domain, which is found in this group, , , and several smaller groups, lacks the conserved distal portion of the domain and has certain substitutions in the characteristic metal-binding residues [] of the HD superfamily phosphohydrolases, which likely render it catalytically inactive. Note that the prototypical HD domain () is not recognised in many members of this group.The exact mode of action and targets of the HD-GYP output domain are not known []. HD-GYP proteins are associated to the HD domain superfamily of metal-dependent phosphohydrolases; HD designates the principal conserved residues implicated in metal binding and catalysis []. The version of the HD-type domain present in members of (and in some other groups) has many additional highly conserved residues, including a conserved GYP motif, and is therefore called HD-GYP [, ].It has been noted that the highly conserved sequence of the HD-GYP domain suggests high substrate specificity []. On the basis of its association with the GGDEF diguanylate cyclase domain, it has been also predicted that the HD-GYP domain may be involved in the metabolism of cyclic diguanylate or in dephosphorylation of some phosphotransfer domain []. | Short Name: | UCP036888_HDGYP-like |
