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HAMAP rule MF_01491

General rule information [?]

Accession	MF_01491
Dates	9-MAY-2014 (Created) 1-JUN-2023 (Last updated, Version 15)
Name	RNase_J_bact
Scope(s)	Bacteria
Template(s)	Q45493 (RNJ1_BACSU); O31760 (RNJ2_BACSU); Q72JJ7 (RNJ_THET2); A0QVT2 (RNJ_MYCS2); [ 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 [?]

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	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
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 [?]

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 [?]

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.