Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | - |
- |
- |
Saccharolobus solfataricus P2 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
Subunits | Comment | Organism |
---|---|---|
More | in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex. The complex is composed of a HerA hexamer bound to a NurA dimer | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
HerA helicase | - |
Saccharolobus solfataricus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 95 | no unfolding in the temperature range 3095°C, indicating that its Tm is greater than 95°C | Saccharolobus solfataricus |
General Information | Comment | Organism |
---|---|---|
physiological function | in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair | Saccharolobus solfataricus |