F9VN79 · RNH_SULTO
- ProteinRibonuclease HI
- GenernhA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids149 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Nuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. In the presence of Mn2+ or Co2+ can also cleave an RNA-RNA hybrid; the dsRNase activity is 10- 100-fold lower than RNase H activity. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.
Miscellaneous
The protein is hyperthermostable, melting temperature (TM) for wild-type is 102 degrees Celsius, for the double Cys mutant is 93 degrees Celsius and for a C-terminal deletion of 6 residues is 77 degrees Celsius.
Catalytic activity
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )
Note: Divalent metal cations; Mn2+ and Mg2+ are preferred over Co2+ or Ni2+.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 7 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 7 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 7 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 52 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 52 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 76 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 76 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | DNA binding | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA-DNA hybrid ribonuclease activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease HI
- EC number
- Short namesRNase HI; Sto-RNase HI
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfurisphaera
Accessions
- Primary accessionF9VN79
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 7 | Loss of RNase H activity, loss of dsRNase activity. Does not complement E.coli double deletion mutant. | ||||
Sequence: D → N | ||||||
Mutagenesis | 52 | Loss of RNase H activity, loss of dsRNase activity. Does not complement E.coli double deletion mutant. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 58 | RNase H and dsRNase activity increase slightly, decreased thermostability; when associated with A-145. | ||||
Sequence: C → A | ||||||
Mutagenesis | 76 | Loss of RNase H activity, loss of dsRNase activity. Does not complement E.coli double deletion mutant. | ||||
Sequence: D → N | ||||||
Mutagenesis | 91 | Retains RNase H activity, considerable loss of dsRNase activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 118 | 10-fold reduction in both RNase H and dsRNase activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 125 | Retains RNase H activity, loss of dsRNase activity. Complements E.coli double deletion mutant. | ||||
Sequence: D → N | ||||||
Mutagenesis | 144-149 | 20% reduction in RNase H activity, 40% reduction in dsRNase activity, partial loss of thermostability. | ||||
Sequence: Missing | ||||||
Mutagenesis | 145 | RNase H and dsRNase activity increase slightly, decreased thermostability; when associated with A-58. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000420870 | 1-149 | Ribonuclease HI | |||
Sequence: MIIGYFDGLCEPKNPGGIATFGFVIYLDNRKIEGYGLAEKPFSINSTNNVAEYSGLICLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKLRDIGCIILT | ||||||
Disulfide bond | 58↔145 | |||||
Sequence: CLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKLRDIGC |
Post-translational modification
The disulfide bond confers considerable stability to the protein.
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-140 | RNase H type-1 | ||||
Sequence: MIIGYFDGLCEPKNPGGIATFGFVIYLDNRKIEGYGLAEKPFSINSTNNVAEYSGLICLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKL |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length149
- Mass (Da)16,813
- Last updated2011-10-19 v1
- Checksum195DB9BAA869A571
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000023 EMBL· GenBank· DDBJ | BAK54376.1 EMBL· GenBank· DDBJ | Genomic DNA |