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Literature summary for 3.1.26.4 extracted from
- RNase H as gene modifier, driver of evolution and antiviral defense (2017), Front. Microbiol., 8, 1745 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | calcium ions generally inactivate the enzyme and abolish catalysis | Escherichia coli |  |
| Ca2+ | calcium ions generally inactivate the enzyme and abolish catalysis | Homo sapiens | |
| Ca2+ | calcium ions generally inactivate the enzyme and abolish catalysis | Mus musculus | |
| Ca2+ | calcium ions generally inactivate the enzyme and abolish catalysis | Saccharomyces cerevisiae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Mus musculus | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Mus musculus | |
| Mg2+ | required | Homo sapiens | |
| Mg2+ | required | Saccharomyces cerevisiae | |
| Mg2+ | required | Escherichia coli | |
| additional information | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Mus musculus | |
| additional information | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Homo sapiens | |
| additional information | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Saccharomyces cerevisiae | |
| additional information | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A7Y4 | - |
- |
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Mus musculus |
| dimer | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Homo sapiens |
| dimer | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Saccharomyces cerevisiae |
| dimer | RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease H | - |
Mus musculus |
| ribonuclease H | - |
Homo sapiens |
| ribonuclease H | - |
Saccharomyces cerevisiae |
| ribonuclease H | - |
Escherichia coli |
| RNase H | - |
Mus musculus |
| RNase H | - |
Homo sapiens |
| RNase H | - |
Saccharomyces cerevisiae |
| RNase H | - |
Escherichia coli |
| RNase HI | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses | Mus musculus |
| evolution | reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses | Homo sapiens |
| evolution | reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses | Escherichia coli |
| evolution | the reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses | Saccharomyces cerevisiae |
| malfunction | mice deficient in RNase H1 that localizes to mitochondria die during embryogenesis, probably due to the defective processing of R-loops. RNase H2 knockout mice are also not viable, and mutations in either of the human genes can cause Aicardi-Goutieres Syndrome, a severe inheritable neurodevelopmental disorder. In this disease, uncleaved RNA-DNA hybrids accumulate within cells that possibly upregulate interferon via the nucleic acid sensor cyclic GMP-AMP synthase (cGAS) and its adaptor protein STING | Mus musculus |
| malfunction | RNase H2 and H1 knockout mutations in either of the human genes can cause Aicardi-Goutieres Syndrome, a severe inheritable neurodevelopmental disorder. In this disease, uncleaved RNA-DNA hybrids accumulate within cells that possibly upregulate interferon via the nucleic acid sensor cyclic GMP-AMP synthase (cGAS) and its adaptor protein STING | Homo sapiens |
| additional information | three-dimensional structure is solved, revealing a conserved protein architecture, the RNase H fold | Escherichia coli |
| physiological function | DNA replication requires RNA primers to initiate lagging strand DNA synthesis and their subsequent removal by the RNase. RNase H enzymes mediate viral and cellular replication and antiviral defense in eukaryotes and prokaryotes, splicing, R-loop resolvation, DNA repair. RNase H-like activities are also required for the activity of small regulatory RNAs. Virtually all known immune defense mechanisms against viruses, phages, transposable elements, and extracellular pathogens require RNase H-like enzymes. RNase H-like activities of retroviruses, transposable elements, and phages, have built up innate and adaptive immune systems throughout all domains of life | Saccharomyces cerevisiae |
| physiological function | the RNase H enzymes mediate viral and cellular replication and antiviral defense in eukaryotes and prokaryotes, splicing, R-loop resolvation, DNA repair. RNase H-like activities are also required for the activity of small regulatory RNAs. Virtually all known immune defense mechanisms against viruses, phages, transposable elements, and extracellular pathogens require RNase H-like enzymes. RNase H-like activities of retroviruses, transposable elements, and phages, have built up innate and adaptive immune systems throughout all domains of life | Homo sapiens |
| physiological function | the RNase H enzymes mediate viral and cellular replication and antiviral defense in eukaryotes and prokaryotes, splicing, R-loop resolvation, DNA repair. RNase H-like activities are also required for the activity of small regulatory RNAs. Virtually all known immune defense mechanisms against viruses, phages, transposable elements, and extracellular pathogens require RNase H-like enzymes. RNase H-like activities of retroviruses, transposable elements, and phages, have built up innate and adaptive immune systems throughout all domains of life | Escherichia coli |
| physiological function | the RNase H enzymes mediate viral and cellular replication and antiviral defense in eukaryotes and prokaryotes, splicing, R-loop resolvation, DNA repair. RNase H-like activities are also required for the activity of small regulatory RNAs. Virtually all known immune defense mechanisms against viruses, phages, transposable elements, and extracellular pathogens require RNase H-like enzymes. RNase H-like activities of retroviruses, transposable elements, and phages, have built up innate and adaptive immune systems throughout all domains of life. R-loops are formed when an RNA strand intercalates into dsDNA, resulting in RNA-DNA hybrids and single-stranded DNA loops. R-loops affect promoter activities, with a role in gene expression (e.g. of the c-Myc proto-oncogene), genome stability, CRISPR-Cas immunity, DNA repair, and cancer formation. RNases H can remove the RNA moiety and prevent deleterious DNA breaks | Mus musculus |
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