DB code: T00252
| CATH domain | 3.40.970.10 : Ribonuclease HI; Chain A | |
|---|---|---|
| -.-.-.- : | ||
| 3.30.420.10 : Nucleotidyltransferase; domain 5 | Catalytic domain | |
| E.C. | 3.1.26.4 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.30.420.10 : Nucleotidyltransferase; domain 5 | M00206 M00019 M00020 M00055 M00135 M00146 M00166 M00173 M00175 M00186 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| Q04740 |
Ribonuclease H
|
RNase H
EC 3.1.26.4 |
NP_013961.1
(Protein)
NM_001182741.1 (DNA/RNA sequence) |
PF01693
(Cauli_VI)
PF00075 (RNase_H) [Graphical View] |
| KEGG enzyme name |
|---|
|
calf thymus ribonuclease H
endoribonuclease H (calf thymus) RNase H RNA*DNA hybrid ribonucleotidohydrolase hybrid ribonuclease hybridase hybridase (ribonuclease H) ribonuclease H hybrid nuclease |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q04740 | RNH1_YEAST | Endonucleolytic cleavage to 5''- phosphomonoester. | Binds 1 magnesium ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding (By similarity). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||
| KEGG-id | C00305 | C00046 | C00001 | C00960 | ||||||
| E.C. | ||||||||||
| Compound | Magnesium | RNA | H2O | RNA 5'-phosphate | ||||||
| Type | divalent metal (Ca2+, Mg2+) | nucleic acids | H2O | nucleic acids,phosphate group/phosphate ion | ||||||
| ChEBI |
18420 18420 |
15377 15377 |
||||||||
| PubChem |
888 888 |
22247451 962 22247451 962 |
||||||||
| 1qhkA |
|
|
|
|
|
Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1qhkA |
|
|
|
|
|
|||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | structure by NMR of 6-52. |
| Medline ID | 99380410 |
| PubMed ID | 10448044 |
| Journal | J Mol Biol |
| Year | 1999 |
| Volume | 291 |
| Pages | 661-9 |
| Authors | Evans SP, Bycroft M |
| Title | NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9. |
| Related PDB | 1qhk |
| Related UniProtKB | Q04740 |
| Comments |
|---|
|
This enzyme is composed of three domains.
The determined structure has only a small N-terminal domain of this enzyme, |
| Created | Updated |
|---|---|
| 2002-08-22 | 2009-02-26 |