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HAMAP rule MF_01491

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01491
Accession MF_01491
Dates 09-MAY-2014 (Created)
01-JUN-2023 (Last updated, Version 16)
Name RNase_J_bact
Scope(s) Bacteria
Template(s) Q45493; O31760; Q72JJ7; A0QVT2; [ Recover all ]
Triggered by HAMAP; MF_01491 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

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

Comments [?]

FUNCTIONAn 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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105; 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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 Zn(2+) ion per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.;
end case
SUBUNITHomodimer, may be a subunit of the RNA degradosome.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.

Keywords [?]

Cytoplasm
Endonuclease
Exonuclease
Hydrolase
case <FTGroup:1> or <FTGroup:2>
Metal-binding
Zinc
end case
Nuclease
RNA-binding
rRNA processing

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;
Pfam 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 97 97 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="catalytic"		 D 2
BINDING 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 190 190 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="#2"
/ligand_note="catalytic"		 [DE] 2
BINDING 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
Fusion Nter: None Cter: 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.



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