HAMAP rule MF_01492
General rule information
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Accession | MF_01492 |
Dates | 9-MAY-2014 (Created)
1-JUN-2023 (Last updated, Version 12) |
Name | RNase_J_arch |
Scope(s) |
Archaea |
Template(s) | Q9V076 (RNJ_PYRAB); [ Recover all ] |
Triggered by |
HAMAP; MF_01492 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | RNJ |
Protein name | RecName: Full=Ribonuclease J; Short=RNase J; EC=3.1.-.-; |
Gene name | Name=rnj; |
Comments
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FUNCTION | An RNase that has 5'-3' exonuclease activity. May be involved in RNA degradation. |
SUBUNIT | Homodimer. |
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 LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Archaeal RNase J subfamily. |
Keywords
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Cytoplasm | |
Exonuclease | |
Hydrolase | |
case <FTGroup:1> or <FTGroup:2> | |
Metal-binding | |
Zinc | |
end case | |
Nuclease | |
RNA-binding |
Gene Ontology
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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
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PROSITE | PS01292; UPF0036; 1; |
Pfam | PF00753; Lactamase_B; 1; |
Pfam | PF07521; RMMBL; 1; |
NCBIfam | TIGR00649; MG423; 1; |
Features
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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
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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. |