The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Metalloproteases ("zincins"), catalytic domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 12: Metallopeptidase Oma1

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 2 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
4 P36163 (/IMP) P36163 (/IMP) P36163 (/IMP) P36163 (/IMP)
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
1 Q9P7G4 (/ISS)

There are 4 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein quality control for misfolded or incompletely synthesized proteins GO:0006515
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
4 P36163 (/IMP) P36163 (/IMP) P36163 (/IMP) P36163 (/IMP)
TOR signaling GO:0031929
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
4 P36163 (/IMP) P36163 (/IMP) P36163 (/IMP) P36163 (/IMP)
Mitochondrial protein catabolic process GO:0035694
The chemical reactions and pathways resulting in the breakdown of a mitochondrial protein. This process is necessary to maintain the healthy state of mitochondria and is thought to occur via the induction of an intramitochondrial lysosome-like organelle that acts to eliminate the damaged oxidised mitochondrial proteins without destroying the mitochondrial structure.
4 P36163 (/IMP) P36163 (/IMP) P36163 (/IMP) P36163 (/IMP)
Protein quality control for misfolded or incompletely synthesized proteins GO:0006515
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
1 Q9P7G4 (/ISS)

There are 3 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
5 P36163 (/HDA) P36163 (/HDA) P36163 (/HDA) P36163 (/HDA) Q9P7G4 (/HDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
4 P36163 (/IDA) P36163 (/IDA) P36163 (/IDA) P36163 (/IDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
1 Q9P7G4 (/ISS)