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Literature summary extracted from

  • Jarrous, N.; Gopalan, V.
    Archaeal/eukaryal RNase P: subunits, functions and RNA diversification (2010), Nucleic Acids Res., 38, 7885-7894.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Escherichia coli
-
-
-
3.1.26.5 Homo sapiens
-
-
-
3.1.26.5 Methanothermobacter thermautotrophicus
-
-
-
3.1.26.5 Mus musculus
-
-
-
3.1.26.5 Mycoplasmopsis fermentans
-
-
-
3.1.26.5 Pyrococcus furiosus
-
-
-
3.1.26.5 Saccharolobus solfataricus
-
-
-
3.1.26.5 Saccharomyces cerevisiae
-
-
-
3.1.26.5 [Candida] glabrata
-
-
-

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 RNase P
-
 Mus musculus
3.1.26.5 RNase P
-
 Escherichia coli
3.1.26.5 RNase P
-
 Homo sapiens
3.1.26.5 RNase P
-
 Saccharomyces cerevisiae
3.1.26.5 RNase P
-
 Methanothermobacter thermautotrophicus
3.1.26.5 RNase P
-
 Pyrococcus furiosus
3.1.26.5 RNase P
-
 Saccharolobus solfataricus
3.1.26.5 RNase P
-
 Mycoplasmopsis fermentans
3.1.26.5 RNase P
-
 [Candida] glabrata

General Information

EC Number General Information Comment Organism
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 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
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Mus musculus
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Escherichia coli
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Homo sapiens
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Saccharomyces cerevisiae
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Methanothermobacter thermautotrophicus
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Pyrococcus furiosus
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Saccharolobus solfataricus
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing Mycoplasmopsis fermentans
3.1.26.5 physiological function RNase P plays a role in precursor tRNA processing [Candida] glabrata