EC Number   |
General Information |
Reference |
|---|
   3.1.26.3 | evolution |
class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as RNase III in Escherichia coli. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains |
730533 |
| 3.1.26.3 | evolution |
class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains |
730533 |
| 3.1.26.3 | evolution |
members of the ribonuclease (RNase) III family of enzymes are metal-dependent double-strand specific endoribonucleases. They are ubiquitously found and eukaryotic RNase III-like enzymes include Dicer and Drosha, involved in RNA processing and RNA interference. SmRNase III is a typical double-strand specific endoribonuclease, but with a minimal substrate length requirement different from that of its enterobacterial orthologue |
750621 |
| 3.1.26.3 | evolution |
mRPN1 is a homologue of the REN endonucleases |
716905 |
| 3.1.26.3 | evolution |
RNase III is a member of the phylogenetically highly conserved endoribonuclease III family |
751291 |
| 3.1.26.3 | evolution |
the enzyme belongs to the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. RNase III family members share a unique fold (RNase III domain) that can dimerize to form a structure that binds dsRNA and cleaves phosphodiesters on each strand, providing the characteristic 2 nt, 3'-overhang product ends. Domain structures of ribonuclease III family polypeptides, overview |
-, 731020 |
| 3.1.26.3 | evolution |
the enzyme belongs to the the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. RNase III family members share a unique fold (RNase III domain) that can dimerize to form a structure that binds dsRNA and cleaves phosphodiesters on each strand, providing the characteristic 2 nt, 3'-overhang product ends. Domain structures of ribonuclease III family polypeptides, overview |
731020 |
| 3.1.26.3 | evolution |
the enzyme is a member of the ribonuclease III (RNase III) family |
-, 730394, 750986, 751733 |
| 3.1.26.3 | evolution |
the enzyme is a member of the RNase III superfamily |
-, 750689 |
| 3.1.26.3 | evolution |
the enzyme RNase III is a member of the ubiquitous family of double-strand-specific endoribonucleases |
-, 730670 |
