EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.6.4.13 | additional information | the NS3 protease domain enhances the helicase activity of NS3 but has no effect on its NTPase activity. For the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B | Classical swine fever virus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.6.4.13 | expression of wild-type and mutant His-tagged NS3 helicase domain in Escherichia coli | Classical swine fever virus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.6.4.13 | K232A | site-directed mutagenesis in the helicase domain of NS3 | Classical swine fever virus |
3.6.4.13 | additional information | for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B | Classical swine fever virus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.6.4.13 | Mg2+ | activates | Classical swine fever virus | |
3.6.4.13 | Mg2+ | the helicase activity requires divalent ions. Mn2+ is preferred over Mg2+ | Classical swine fever virus | |
3.6.4.13 | Mn2+ | the helicase activity requires divalent ions. Mn2+ is preferred over Mg2+ | Classical swine fever virus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.4.13 | additional information | Classical swine fever virus | NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules | ? | - |
? | |
3.6.4.13 | additional information | Classical swine fever virus CSFV | NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.6.4.13 | Classical swine fever virus | - |
- |
- |
3.6.4.13 | Classical swine fever virus | Q9YS30 | CSFV | - |
3.6.4.13 | Classical swine fever virus CSFV | Q9YS30 | CSFV | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.4.13 | ATP + H2O | - |
Classical swine fever virus | ADP + phosphate | - |
? | |
3.6.4.13 | ATP + H2O | helicase activity requires the substrates possessing a 3' un-base-paired region on the RNA template strand. The NS3h helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of the RNA substrates. CSFV NS3 helicase activity requires a longer 3'-end single-stranded overhang for efficient duplex unwinding and the directionality of NS3 helicase unwinding is 3' to 5' with respect to the template strand | Classical swine fever virus | ADP + phosphate | - |
? | |
3.6.4.13 | ATP + H2O | - |
Classical swine fever virus CSFV | ADP + phosphate | - |
? | |
3.6.4.13 | CTP + H2O | helicase activity is about 85% of the activity with ATP | Classical swine fever virus | CDP + phosphate | - |
? | |
3.6.4.13 | dATP + H2O | helicase activity is about 10% of the activity with ATP | Classical swine fever virus | dADP + phosphate | - |
? | |
3.6.4.13 | dCTP + H2O | helicase activity is about 25% of the activity with ATP | Classical swine fever virus | dCDP + phosphate | - |
? | |
3.6.4.13 | dGTP + H2O | helicase activity is about 10% of the activity with ATP | Classical swine fever virus | dGDP + phosphate | - |
? | |
3.6.4.13 | dTTP + H2O | helicase activity is about 55% of the activity with ATP | Classical swine fever virus | dTDP + phosphate | - |
? | |
3.6.4.13 | GTP + H2O | helicase activity is about 55% of the activity with ATP | Classical swine fever virus | GDP + phosphate | - |
? | |
3.6.4.13 | additional information | nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus | Classical swine fever virus | ? | - |
? | |
3.6.4.13 | additional information | NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules | Classical swine fever virus | ? | - |
? | |
3.6.4.13 | additional information | NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules | Classical swine fever virus CSFV | ? | - |
? | |
3.6.4.13 | RNA + H2O | NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview | Classical swine fever virus | ? | - |
? | |
3.6.4.13 | RNA + H2O | NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview | Classical swine fever virus CSFV | ? | - |
? | |
3.6.4.13 | UTP + H2O | helicase activity is about 55% of the activity with ATP | Classical swine fever virus | UDP + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.6.4.13 | nonstructural protein 3 | - |
Classical swine fever virus |
3.6.4.13 | NS3 | - |
Classical swine fever virus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.6.4.13 | 37 | - |
assay at | Classical swine fever virus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.6.4.13 | 6.5 | - |
ATPase assay at | Classical swine fever virus |
3.6.4.13 | 7.5 | - |
- |
Classical swine fever virus |
3.6.4.13 | 7.5 | - |
RNA helicase assay at | Classical swine fever virus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.6.4.13 | 6.5 | - |
pH 6.5: about 50% of maximal activity, pH 8: about 80% of maximal activity | Classical swine fever virus |