HAMAP logo

HAMAP rule MF_01491

Send feedback

General rule information [?]

Accession MF_01491
Dates 9-MAY-2014 (Created)
1-JUN-2023 (Last updated, Version 15)
Name RNase_J_bact
Templates Q45493 (RNJ1_BACSU); O31760 (RNJ2_BACSU); Q72JJ7 (RNJ_THET2); A0QVT2 (RNJ_MYCS2): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Ribonuclease J;
Short=RNase J;
EC 3.1.-.-;
Gene name

Comments [?]

Function An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
case <FTGroup:1> and <FTGroup:2>
Cofactor Zn(2+)
Note: Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
else case <FTGroup:1> and not <FTGroup:2>
Cofactor Zn(2+)
Note: Binds 1 Zn(2+) ion per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
end case
Subunit Homodimer, may be a subunit of the RNA degradosome.
Subcellular location Cytoplasm.
Similarity Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.

Keywords [?]

case <FTGroup:1> or <FTGroup:2>
end case

Gene Ontology [?]

GO:0004521; Molecular function: RNA endonuclease activity.
GO:0004534; Molecular function: 5'-3' RNA exonuclease activity.
case <FTGroup:1> or <FTGroup:2>
GO:0008270; Molecular function: zinc ion binding.
end case
GO:0005737; Cellular component: cytoplasm.
GO:0003723; Molecular function: RNA binding.
GO:0006364; Biological process: rRNA processing.

Cross-references [?]

PROSITE PS01292; UPF0036; 1;
Pfam PF00753; Lactamase_B; 1;
PF07521; RMMBL; 1;
NCBIfam TIGR00649; MG423; 1;
PIRSF PIRSF004803; RnjA; 1;

Features [?]

From: RNJ_THET2 (Q72JJ7)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     93     93       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     H   1
BINDING     95     95       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     H   1
BINDING (Optional)     97     97       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic     D   2
BINDING (Optional)     98     98       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic     H   2
BINDING     168     168       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     H   1
BINDING     190     190       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic     [DE]   1
BINDING (Optional)     190     190       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic     [DE]   2
BINDING (Optional)     416     416       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic     H   2
BINDING     390     394       /ligand="substrate     H-[VTA]-S-[GS]-H  

Additional information [?]

Size range 548-718 amino acids
Related rules MF_01492 (RNJ)
Fusion None
Comments Duplicated in many Bacillota, often one of the copies can only bind 1 metal ion. In B.subtilis the 2 enzymes do not have exactly the same function. A closely-related protein exists in Archaea, which is about 100 residues shorter at the C-terminus. The archaeal protein does not seem to have endonuclease activity.