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
15377
PubChem 888
22247451
962
1qhkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

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, which does not contain the active site. However, homologous enzyme structures for the C-terminal domain suggest that it is a catalytic domain which binds two magnesium ions (see SwissProt Q04740).

Created Updated
2002-08-22 2009-02-26