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

Bacteria

Templates

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

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

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 [?]

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;
	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.

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