EzCatDB: T00252
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DB codeT00252
CATH domainDomain 13.40.970.10 : Ribonuclease HI; Chain A
Domain 2-.-.-.-
Domain 33.30.420.10 : Nucleotidyltransferase; domain 5Catalytic domain
E.C.3.1.26.4

CATH domainRelated DB codes (homologues)
3.30.420.10 : Nucleotidyltransferase; domain 5M00206,M00019,M00020,M00055,M00135,M00146,M00166,M00173,M00175,M00186

Enzyme Name
UniProtKBKEGG

Q04740
Protein nameRibonuclease Hcalf thymus ribonuclease H
endoribonuclease H (calf thymus)
RNase H
RNA*DNA hybrid ribonucleotidohydrolase
hybrid ribonuclease
hybridase
hybridase (ribonuclease H)
ribonuclease H
hybrid nuclease
SynonymsRNase H
EC 3.1.26.4
RefSeqNP_013961.1 (Protein)
NM_001182741.1 (DNA/RNA sequence)
PfamPF01693 (Cauli_VI)
PF00075 (RNase_H)
[Graphical view]


UniProtKB:Accession NumberQ04740
Entry nameRNH1_YEAST
ActivityEndonucleolytic cleavage to 5''- phosphomonoester.
Subunit
Subcellular location
CofactorBinds 1 magnesium ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding (By similarity).

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00046C00001C00960
CompoundMagnesiumRNAH2ORNA 5'-phosphate
Typedivalent metal (Ca2+, Mg2+)nucleic acidsH2Onucleic acids,phosphate group/phosphate ion
ChEBI18420

15377

PubChem888

962
22247451

            
1qhkAUnboundUnbound Unbound

Active-site residues
pdb
        
1qhkA


references
[1]
Commentsstructure by NMR of 6-52.
Medline ID99380410
PubMed ID10448044
JournalJ Mol Biol
Year1999
Volume291
Pages661-9
AuthorsEvans SP, Bycroft M
TitleNMR 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 PDB1qhk
Related UniProtKBQ04740

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).

createdupdated
2002-08-222009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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