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PROSITE documentation PDOC00806 [for PROSITE entry PS51383] |
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 [1]. We also developed a profile which covers the entire YjeF C-terminal domain.
Last update:May 2008 / Text revised; profile added.
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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). | |
PubMed ID | 12457846 |
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). | |
PubMed ID | 18097102 | |
DOI | 10.1107/S1744309107065645 |
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). | |
PubMed ID | 15257761 | |
DOI | 10.1186/1471-2164-5-45 |