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Literature summary for 3.1.26.5 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

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

Synonyms

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

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