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HAMAP rule MF_01842

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General rule information [?]

Accession MF_01842
Dates 15-DEC-2005 (Created)
19-NOV-2022 (Last updated, Version 16)
Name Archaemetzincin
Templates Q400G9 (AMZ1_HUMAN); Q8TXW1 (AMZA_METKA); O29917 (AMZA_ARCFU): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Archaemetzincin;
EC 3.4.-.-;
Gene name

Comments [?]

Function Probable zinc metalloprotease whose natural substrate is unknown.
Cofactor Zn(2+)
Note: Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.
Subunit Monomer.
Similarity Belongs to the peptidase M54 family.

Keywords [?]

Gene Ontology [?]

GO:0008237; Molecular function: metallopeptidase activity.
GO:0006508; Biological process: proteolysis.
GO:0008270; Molecular function: zinc ion binding.

Cross-references [?]

Pfam PF07998; Peptidase_M54; 1;
PIRSF PIRSF005785; Zn-prot_arch; 1;

Features [?]

Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     126     126       Proton acceptor     E  
BINDING     125     125       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     H  
BINDING     129     129       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     H  
BINDING     135     135       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /ligand_note="catalytic     H  
BINDING     136     136       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     C  
BINDING     141     141       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     C  
BINDING     160     160       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     C  
BINDING     163     163       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     C  

Additional information [?]

Size range 155-192 amino acids
Related rules None
Fusion None
Comments Although it has not been proved in prokaryotes, its function as metalloprotease is probable due to the strong similarities with the AMZ1 and AMZ2 enzymes. See: RX PubMed=15972818; DOI=10.1074/jbc.M504533200; RA Diaz-Perales A., Quesada V., Peinado J.R., Ugalde A.P., Alvarez J., RA Suarez M.F., Gomis-Rueth X., Lopez-Otin C.; RT "Identification and characterization of human archaemetzincin-1 and - RT 2, two novel members of a family of metalloproteases widely RT distributed in archae."; RL J. BiolQ400G9. Chem. 280:30367-30375(2005). The family has been identified in Archaea and described in: RX PubMed=12746556; RA Gomis-Rueth F.X.; RT "Structural aspects of the metzincin clan of metalloendopeptidases."; RL Mol. Biotechnol. 24:157-202(2003).