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HAMAP rule MF_01818

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General rule information [?]

Accession MF_01818
Dates 12-DEC-2003 (Created)
1-JUN-2023 (Last updated, Version 26)
Name RNase_Z_BN
Templates P0A8V0 (RBN_ECOLI); Q58897 (RNZ_METJA); P54548 (RNZ_BACSU): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Enterobacterales>
Protein name
RecName: Full=Ribonuclease BN;
Short=RNase BN;
EC 3.1.-.-;
AltName: Full=Ribonuclease Z homolog;
Short=RNase Z homolog;
Gene name
Protein name
RecName: Full=Ribonuclease Z;
Short=RNase Z;
AltName: Full=tRNA 3 endonuclease;
AltName: Full=tRNase Z;
Gene name
end case

Comments [?]

case <OC:Enterobacterales>
Function Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities.
Function Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic activity Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.; EC=;
end case
case <FTGroup:1>
Cofactor Zn(2+)
Note: Binds 2 Zn(2+) ions.
end case
Subunit Homodimer.
case <OC:Enterobacterales>
Similarity Belongs to the RNase Z family. RNase BN subfamily.
Similarity Belongs to the RNase Z family.
end case

Keywords [?]

case <OC:Enterobacterales>
end case
case <FTGroup:1>
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
case <OC:Enterobacterales>
GO:0004519; Molecular function: endonuclease activity.
GO:0004527; Molecular function: exonuclease activity.
GO:0042781; Molecular function: 3'-tRNA processing endoribonuclease activity.
end case
GO:0008033; Biological process: tRNA processing.

Cross-references [?]

Pfam PF00753; Lactamase_B; 1;
NCBIfam TIGR02651; RNase_Z; 1;
TIGR02649; True_RNase_BN; 1;

Features [?]

From: RNZ_BACSU (P54548)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     67     67       Proton acceptor     D  
BINDING     63     63       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     H   1
BINDING     65     65       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     H   1
BINDING     67     67       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" /ligand_note="catalytic     D   1
BINDING     68     68       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" /ligand_note="catalytic     H   1
BINDING     140     140       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     H   1
BINDING     211     211       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     D   1
BINDING     211     211       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" /ligand_note="catalytic     D   1
BINDING     269     269       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" /ligand_note="catalytic     H   1

Additional information [?]

Size range 220-407 amino acids
Related rules None
Fusion Nter: None; Cter: <Unknown>
Comments Was initially thought to be an arylsulfatase, given its similarity with the atsA family.