EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.12.1 | the crystal structure reveals a decameric toroid with a large 55 A diameter central channel formed by five tightly packed dimers | Saccharolobus solfataricus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.12.1 | C188A | the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates | Saccharolobus solfataricus |
3.1.12.1 | C191A | the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates | Saccharolobus solfataricus |
3.1.12.1 | C32A | the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates | Saccharolobus solfataricus |
3.1.12.1 | D99A | inactive mutant enzyme | Saccharolobus solfataricus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.12.1 | iron-sulfur centre | near the active site, each enzyme protomer contains one [4Fe-4S] cluster, which is important for both maintaining the decameric state and nuclease activity | Saccharolobus solfataricus | |
3.1.12.1 | K+ | nuclease activity of the enzyme is maximal in the presence of 20-200 mM KCl | Saccharolobus solfataricus | |
3.1.12.1 | Mg2+ | nuclease activity of the enzyme is maximal in the presence of Mg2+ or Mn2+ (5 mM) | Saccharolobus solfataricus | |
3.1.12.1 | Mn2+ | nuclease activity of the enzyme is maximal in the presence of Mg2+ or Mn2+ (5 mM). Mn2+ is bound in the active site located inside the internal tunnel | Saccharolobus solfataricus | |
3.1.12.1 | additional information | Ca2+ does not support the nuclease activity | Saccharolobus solfataricus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.12.1 | Saccharolobus solfataricus | Q97TX9 | - |
- |
3.1.12.1 | Saccharolobus solfataricus P2 | Q97TX9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.12.1 | - |
Saccharolobus solfataricus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.12.1 | additional information | the enzyme also exhibits ATP-independent DNA unwinding activity | Saccharolobus solfataricus | ? | - |
? | |
3.1.12.1 | additional information | the enzyme also exhibits ATP-independent DNA unwinding activity | Saccharolobus solfataricus P2 | ? | - |
? | |
3.1.12.1 | poly-dC10 + H2O | - |
Saccharolobus solfataricus | cytidine 3'-phosphate + ? | - |
? | |
3.1.12.1 | poly-dC10 + H2O | - |
Saccharolobus solfataricus P2 | cytidine 3'-phosphate + ? | - |
? | |
3.1.12.1 | single-stranded oligodeoxyribonucleotide + H2O | - |
Saccharolobus solfataricus | nucleoside 3'-phosphate + ? | - |
? | |
3.1.12.1 | single-stranded oligodeoxyribonucleotide + H2O | - |
Saccharolobus solfataricus P2 | nucleoside 3'-phosphate + ? | - |
? | |
3.1.12.1 | ssDNA + H2O | short oligonucleotides (17 nt) are cleaved faster than longer substrates (62 nt). Lack of significant sequence preference toward the substrates containing the Sulfolobus solfataricus protospacer adjacent motif (PAMs) in DNA binding and cleavage reactions in vitro. The rates of cleavage of ssRNA and dsDNA with blunt ends by the enzyme are approximately 20 times and 200 times lower, respectively compared to ssDNA | Saccharolobus solfataricus | nucleoside 3'-phosphate + ? | - |
? | |
3.1.12.1 | ssDNA + H2O | short oligonucleotides (17 nt) are cleaved faster than longer substrates (62 nt). Lack of significant sequence preference toward the substrates containing the Sulfolobus solfataricus protospacer adjacent motif (PAMs) in DNA binding and cleavage reactions in vitro. The rates of cleavage of ssRNA and dsDNA with blunt ends by the enzyme are approximately 20 times and 200 times lower, respectively compared to ssDNA | Saccharolobus solfataricus P2 | nucleoside 3'-phosphate + ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.12.1 | decamer | crystallized at room temperature using the sitting drop vapour diffusion method. The crystal structure reveals a decameric toroid with a large 55 A diameter central channel formed by five tightly packed dimers | Saccharolobus solfataricus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.12.1 | Cas4 | - |
Saccharolobus solfataricus |
3.1.12.1 | SSO0001 | locus name | Saccharolobus solfataricus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.12.1 | 65 | 70 | - |
Saccharolobus solfataricus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.12.1 | 9 | 10 | - |
Saccharolobus solfataricus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.12.1 | physiological function | a potential functional role of the enzyme and other Cas4 proteins in CRISPR (Clusters of Regularly interspaced Palindromic Repeats) immunity is based on the presence of 5' to 3' exonuclease and DNA unwinding activities, which produce 3'-ssDNA overhangs as potential intermediates in the process of new spacer addition. The toroidal structures of the enzyme can serve as sliding clamps for other Cas proteins | Saccharolobus solfataricus |