ribonuclease H | |||||||||
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Crystallographic structure of E. coli RNase HI.
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Identifiers | |||||||||
EC number | 3.1.26.4 | ||||||||
CAS number | 9050-76-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
retroviral ribonuclease H | |||||||||
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Identifiers | |||||||||
EC number | 3.1.26.13 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
Identifiers | |||||||||
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Symbol | RNase H | ||||||||
Pfam | PF00075 | ||||||||
Pfam clan | CL0219 | ||||||||
InterPro | IPR002156 | ||||||||
PROSITE | PS50879 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Identifiers | |||||||||
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Symbol | RNase HII | ||||||||
Pfam | PF01351 | ||||||||
Pfam clan | CL0219 | ||||||||
InterPro | IPR024567 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Ribonuclease H (abbreviated RNase H or RNH) is a family of non-sequence-specific endonuclease enzymes that catalyze the cleavage of RNA in an RNA/DNA substrate via a hydrolytic mechanism. Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes.
The family is divided into evolutionarily related groups with slightly different substrate preferences, broadly designated ribonuclease H1 and H2. The human genome encodes both H1 and H2. Human ribonuclease H2 is a heterotrimeric complex composed of three subunits, mutations in any of which are among the genetic causes of a rare disease known as Aicardi–Goutières syndrome. A third type, closely related to H2, is found only in a few prokaryotes, whereas H1 and H2 occur in all domains of life. Additionally, RNase H1-like retroviral ribonuclease H domains occur in multidomain reverse transcriptase proteins, which are encoded by retroviruses such as HIV and are required for viral replication.
In eukaryotes, ribonuclease H1 is involved in DNA replication of the . Both H1 and H2 are involved in genome maintenance tasks such as processing of R-loop structures.