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Annotation rule MF_00052
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General rule information [?]

Accession MF_00052
Dates 1-JUN-2001 (Created)
27-OCT-2018 (Last updated, Version 29)
Name RNase_HII
Scope
Bacteria
Archaea
Templates O31744 (RNH2_BACSU); P10442 (RNH2_ECOLI); O29634 (RNH2_ARCFU); Q57599 (RNH2_METJA); O74035 (RNH2_THEKO): [Recover all]
case <OC:Bacteria>
end case

case <OC:Archaea>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
RNH2
Protein name
RecName: Full=Ribonuclease HII;
Short=RNase HII;
EC=3.1.26.4;
Gene name
rnhB

Comments [?]

Function Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic activity Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;.
Cofactor Mn(2+)
Mg(2+)
Note: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Subcellular location Cytoplasm.
Similarity Belongs to the RNase HII family.

Keywords [?]


Gene Ontology [?]

GO:0030145; Molecular function: manganese ion binding.
GO:0004523; Molecular function: RNA-DNA hybrid ribonuclease activity.
GO:0006401; Biological process: RNA catabolic process.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF01351; RNase_HII; 1;
TIGRFAMs TIGR00729; TIGR00729; 1;

Features [?]

case <OC:Bacteria>
From: RNH2_ECOLI (P10442)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     16     16       Divalent metal cation     D  
METAL     17     17       Divalent metal cation     E  
METAL     108     108       Divalent metal cation     D  
end case
case <OC:Archaea>
From: RNH2_METJA (Q57599)
METAL     7     7       Divalent metal cation     D  
METAL     8     8       Divalent metal cation     E  
METAL     112     112       Divalent metal cation     D  
end case

Additional information [?]

case <OC:Bacteria>
Size range 181-315 amino acids
end case
case <OC:Archaea>
Size range 195-277 amino acids
end case
Related rules None
Fusion None
Comments Divergent CAUVC not shown in alignment. Possible wrong start in a number of cases.