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HAMAP rule MF_01492

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01492
Accession MF_01492
Dates 09-MAY-2014 (Created)
01-JUN-2023 (Last updated, Version 13)
Name RNase_J_arch
Scope(s) Archaea
Template(s) Q9V076; [ Recover all ]
Triggered by HAMAP; MF_01492 (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 activity. May be involved in RNA degradation.
SUBUNITHomodimer.
case <FTGroup:1> or <FTGroup:2>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.;
end case
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Archaeal RNase J subfamily.

Keywords [?]

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

Gene Ontology [?]

GO:0004534; Molecular function:5'-3' RNA exonuclease activity
GO:0006401; Biological process:RNA catabolic process
case <FTGroup:1> or <FTGroup:2>
GO:0008270; Molecular function:zinc ion binding
end case
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS01292; UPF0036; 1;
Pfam PF00753; Lactamase_B; 1;
Pfam PF07521; RMMBL; 1;
NCBIfam TIGR00649; MG423; 1;

Features [?]

From: RNJ_PYRAB (Q9V076)
Key From To Description Tag Condition FTGroup
BINDING 84 84 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"		 H 1
BINDING 86 86 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"		 H 1
BINDING 88 88 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
/ligand_note="catalytic"		 D 2
BINDING 89 89 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
/ligand_note="catalytic"		 H 2
BINDING 155 155 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"		 H 1
BINDING 177 177 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"		 [DE] 1
BINDING 177 177 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
/ligand_note="catalytic"		 [DE] 2
BINDING 410 410 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
/ligand_note="catalytic"		 H 2
BINDING 384 388 /ligand="substrate" H-[VTA]-S-[GS]-H

Additional information [?]

Size range 399-475 amino acids
Related rules MF_01491
Fusion Nter: None Cter: 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.



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