Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its double-stranded RNA binding domains, dsRBD, to recognize a conserved tetraloop fold. The dsRBD adopts the same conformation in both the AAGU and AGAA complexes | ? | - |
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Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its double-stranded RNA binding domains, dsRBD, to recognize a conserved tetraloop fold. The dsRBD adopts the same conformation in both the AAGU and AGAA complexes | Saccharomyces cerevisiae | ? | - |
? | |
additional information | the AAGU hairpin binds to and is efficiently cleaved by Rnt1p in the context of the snR47 stem sequence | Saccharomyces cerevisiae | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
RNase III | - |
Saccharomyces cerevisiae |
Rnt1p | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
additional information | structure of RNase III double-stranded RNA binding domain complex with a noncanonical RNA substrate, analysis of the binding specificity, overview. The dsRBD adopts the same conformation in both the AAGU and AGAA complexes. The AAGU tetraloop in the complex adopts a backbone fold similar to that of the AGAA tetraloop | Saccharomyces cerevisiae |
physiological function | Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its dsRBD to recognize a conserved tetraloop fold | Saccharomyces cerevisiae |