AC   MF_01491;
DC   Protein; auto
TR   HAMAP; MF_01491; -; 1; level=0
XX
Names: RNase_J_bact
XX
ID   RNJ
DE   RecName: Full=Ribonuclease J;
DE            Short=RNase J;
DE            EC=3.1.-.-;
GN   Name=rnj;
XX
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC       activity. Involved in maturation of rRNA and in some organisms also
CC       mRNA maturation and/or decay.
case <FTGroup:1> and <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+)
CC       or Mg(2+) is physiologically important.;
else case <FTGroup:1> and not <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 Zn(2+) ion per subunit. It is not clear if Zn(2+) or
CC       Mg(2+) is physiologically important.;
end case
CC   -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC       subfamily.
XX
DR   PROSITE; PS01292; UPF0036; 1; trigger=no
DR   Pfam; PF00753; Lactamase_B; 1; trigger=no
DR   Pfam; PF07521; RMMBL; 1; trigger=no
DR   NCBIfam; TIGR00649; MG423; 1; trigger=no
DR   PIRSF; PIRSF004803; RnjA; 1; trigger=no
XX
KW   Cytoplasm
KW   Endonuclease
KW   Exonuclease
KW   Hydrolase
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
KW   Zinc
end case
KW   Nuclease
KW   RNA-binding
KW   rRNA processing
XX
GO   GO:0004521; F:RNA endonuclease activity
GO   GO:0004534; F:5'-3' RNA exonuclease activity
case <FTGroup:1> or <FTGroup:2>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0005737; C:cytoplasm
GO   GO:0003723; F:RNA binding
GO   GO:0006364; P:rRNA processing
XX
FT   From: RNJ_THET2 (Q72JJ7)
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Optional; Group: 2; Condition: D
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Optional; Group: 2; Condition: H
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: [DE]
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Optional; Group: 2; Condition: [DE]
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#2"
FT                   /ligand_note="catalytic"
FT   Optional; Group: 2; Condition: H
FT   BINDING         390..394
FT                   /ligand="substrate"
FT   Condition: H-[VTA]-S-[GS]-H
XX
Size: 548-718;
Related: MF_01492;
Template: Q45493; O31760; Q72JJ7; A0QVT2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACCR, BACSU, CLOBH, LISMO, STAA8, STRP3
Plasmid: 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.
XX
# Revision 1.15 2023/06/01
//