F9VN79 · RNH_SULTO

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

  • Endonucleolytic cleavage to 5'-phosphomonoester.
    EC:3.1.26.4 (UniProtKB | ENZYME | Rhea)

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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.

TypeIDPosition(s)Description
Binding site7Mg2+ 1 (UniProtKB | ChEBI)
Binding site7Mg2+ 2 (UniProtKB | ChEBI)
Binding site7Mn2+ 1 (UniProtKB | ChEBI)
Binding site7Mn2+ 2 (UniProtKB | ChEBI)
Binding site52Mg2+ 1 (UniProtKB | ChEBI)
Binding site52Mn2+ 1 (UniProtKB | ChEBI)
Binding site76Mg2+ 1 (UniProtKB | ChEBI)
Binding site76Mn2+ 1 (UniProtKB | ChEBI)
Binding site125Mg2+ 2 (UniProtKB | ChEBI)
Binding site125Mn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Molecular FunctionRNA binding
Molecular FunctionRNA-DNA hybrid ribonuclease activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribonuclease HI
  • EC number
  • Short names
    RNase HI; Sto-RNase HI

Gene names

    • Name
      rnhA
    • Ordered locus names
      STK_07530

Organism names

Accessions

  • Primary accession
    F9VN79

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis7Loss of RNase H activity, loss of dsRNase activity. Does not complement E.coli double deletion mutant.
Mutagenesis52Loss of RNase H activity, loss of dsRNase activity. Does not complement E.coli double deletion mutant.
Mutagenesis58RNase H and dsRNase activity increase slightly, decreased thermostability; when associated with A-145.
Mutagenesis76Loss of RNase H activity, loss of dsRNase activity. Does not complement E.coli double deletion mutant.
Mutagenesis91Retains RNase H activity, considerable loss of dsRNase activity.
Mutagenesis11810-fold reduction in both RNase H and dsRNase activity.
Mutagenesis125Retains RNase H activity, loss of dsRNase activity. Complements E.coli double deletion mutant.
Mutagenesis144-14920% reduction in RNase H activity, 40% reduction in dsRNase activity, partial loss of thermostability.
Mutagenesis145RNase H and dsRNase activity increase slightly, decreased thermostability; when associated with A-58.

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00004208701-149Ribonuclease HI
Disulfide bond58↔145

Post-translational modification

The disulfide bond confers considerable stability to the protein.

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-140RNase H type-1

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    149
  • Mass (Da)
    16,813
  • Last updated
    2011-10-19 v1
  • Checksum
    195DB9BAA869A571
MIIGYFDGLCEPKNPGGIATFGFVIYLDNRKIEGYGLAEKPFSINSTNNVAEYSGLICLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKLRDIGCIILT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000023
EMBL· GenBank· DDBJ
BAK54376.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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