Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Homo sapiens | - |
- |
- |
Methanothermobacter thermautotrophicus | - |
- |
- |
Mus musculus | - |
- |
- |
Mycoplasmopsis fermentans | - |
- |
- |
Pyrococcus furiosus | - |
- |
- |
Saccharolobus solfataricus | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
[Candida] glabrata | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
RNase P | - |
Mus musculus |
RNase P | - |
Escherichia coli |
RNase P | - |
Homo sapiens |
RNase P | - |
Saccharomyces cerevisiae |
RNase P | - |
Methanothermobacter thermautotrophicus |
RNase P | - |
Pyrococcus furiosus |
RNase P | - |
Saccharolobus solfataricus |
RNase P | - |
Mycoplasmopsis fermentans |
RNase P | - |
[Candida] glabrata |
General Information | Comment | Organism |
---|---|---|
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Mus musculus |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Escherichia coli |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Homo sapiens |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Saccharomyces cerevisiae |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Methanothermobacter thermautotrophicus |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Pyrococcus furiosus |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Saccharolobus solfataricus |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | Mycoplasmopsis fermentans |
evolution | the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs | [Candida] glabrata |
physiological function | RNase P plays a role in precursor tRNA processing | Mus musculus |
physiological function | RNase P plays a role in precursor tRNA processing | Escherichia coli |
physiological function | RNase P plays a role in precursor tRNA processing | Homo sapiens |
physiological function | RNase P plays a role in precursor tRNA processing | Saccharomyces cerevisiae |
physiological function | RNase P plays a role in precursor tRNA processing | Methanothermobacter thermautotrophicus |
physiological function | RNase P plays a role in precursor tRNA processing | Pyrococcus furiosus |
physiological function | RNase P plays a role in precursor tRNA processing | Saccharolobus solfataricus |
physiological function | RNase P plays a role in precursor tRNA processing | Mycoplasmopsis fermentans |
physiological function | RNase P plays a role in precursor tRNA processing | [Candida] glabrata |