Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
More | archaeal RNase P comprises a catalytic RNase P RNA, RPR, and at least four protein cofactors, RPPs, which function as two binary complexes, POP5/RPP30 and RPP21/RPP29 | Pyrococcus furiosus |
Synonyms | Comment | Organism |
---|---|---|
RNase P | - |
Pyrococcus furiosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.1 | - |
assay at | Pyrococcus furiosus |
General Information | Comment | Organism |
---|---|---|
physiological function | RNase P is a catalytic ribonucleoprotein primarily involved in tRNA biogenesis. Insights into the role of protein cofactors RPPs in substrate recognition and cleavage-site selection. Cleavage of various model hairpin loop substrates in the presence of archaeal RPPs | Pyrococcus furiosus |