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Literature summary for 3.1.26.3 extracted from
- Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III (2004), Proc. Natl. Acad. Sci. USA, 101, 8307-8312.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | Q02555 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| double-stranded RNA + H2O | the observed interactions between helix alpha1 in the double-stranded RNA binding domain RNA complex in vitro are required for substrate recognition in the context of the entire protein in vivo. The endonuclease domain of Rnt1p is almost immediately N-terminal to the helix alpha1 | Saccharomyces cerevisiae | 5'-phosphooligonucleotides | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Rnt1p RNase III | - |
Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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