AC   MF_01492;
DC   Protein; auto
TR   HAMAP; MF_01492; -; 1; level=0
XX
Names: RNase_J_arch
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 activity. May be involved
CC       in RNA degradation.
CC   -!- SUBUNIT: Homodimer.
case <FTGroup:1> or <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
CC       Mg(2+) is physiologically important.;
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. Archaeal 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
XX
KW   Cytoplasm
KW   Exonuclease
KW   Hydrolase
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
KW   Zinc
end case
KW   Nuclease
KW   RNA-binding
XX
GO   GO:0004534; F:5'-3' RNA exonuclease activity
GO   GO:0006401; P:RNA catabolic process
case <FTGroup:1> or <FTGroup:2>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: RNJ_PYRAB (Q9V076)
FT   BINDING         84
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         86
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         88
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         89
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         155
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         177
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         177
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         410
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         384..388
FT                   /ligand="substrate"
FT   Condition: H-[VTA]-S-[GS]-H
XX
Size: 399-475;
Related: MF_01491;
Template: Q9V076;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in HALRX, HALTV, METFS, NATSJ, METAR
Plasmid: None
Comments: Duplicated in a few Archaea. A closely-related protein exists in
 bacteria, which is about 100 residues longer at the C-terminus and has exo-
 and endoribonuclease activity.
XX
# Revision 1.12 2023/06/01
//