|PROSITE documentation PDOC00806|
The YjeF C-terminal domain is an ~280-residue module found in the following proteins:
The YjeF C-terminal domain has an α/β fold and shows high structural homology to the members of a ribokinase-like superfamily. The members of the ribokinase-like superfamily are all phosphotransferases and catalyze the phosphorylation of the hydroxymethyl group of the substrate; magnesium and ATP (or ADP) are required for their activity. The YjeF C-terminal is found in association with the YjeF N-terminal domain, which belongs of a specialized family of Rossmann fold domains (see <PDOC51385>) [1,2,3].
The first pattern we developed covers residues that might be involved in forming the substrate-binding pocket. The second one corresponds to residues that could form a kinase anion hole, with the conserved aspartate predicted to be the catalytic base . We also developed a profile which covers the entire YjeF C-terminal domain.Last update:
May 2008 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Zhang R.-G., Grembecka J., Vinokour E., Collart F., Dementieva I., Minor W., Joachimiak A.|
|Title||Structure of Bacillus subtilis YXKO--a member of the UPF0031 family and a putative kinase.|
|Source||J. Struct. Biol. 139:161-170(2002).|
|2||Authors||Zhou Y.-F., Li L.-F., Yang C., Liang Y.-H., Su X.-D.|
|Title||Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans.|
|Source||Acta Crystallogr. F 64:47-49(2008).|
|3||Authors||Anantharaman V., Aravind L.|
|Title||Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability.|
|Source||BMC Genomics 5:45-45(2004).|