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:

"
Hemopexin-like 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 1: Matrix metallopeptidase 24

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 20 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 TermAnnotationsEvidence
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.
18 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(8 more)
Enzyme activator activity GO:0008047
Binds to and increases the activity of an enzyme.
17 P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(7 more)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
16 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(6 more)
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from 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.
16 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(6 more)
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.
15 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(5 more)
Metalloaminopeptidase activity GO:0070006
Catalysis of the hydrolysis of N-terminal amino acid residues from 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.
14 P50281 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(4 more)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
13 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(3 more)
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.
10 O54732 (/ISS) P50281 (/ISS) Q10739 (/ISS) Q5RES1 (/ISS) Q95220 (/ISS) Q99PW6 (/ISS) Q9GLE4 (/ISS) Q9XT90 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Metallopeptidase activity GO:0008237
Catalysis of the hydrolysis of peptide bonds 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.
5 B0R0I1 (/NAS) B3DFR2 (/NAS) F1Q899 (/NAS) Q7T2J1 (/NAS) Q7T2J2 (/NAS)
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
3 P50281 (/IPI) P51511 (/IPI) P51511 (/IPI)
Showing 1 to 10 of 20 entries

There are 90 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 TermAnnotationsEvidence
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
18 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(8 more)
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
16 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(6 more)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
14 P50281 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(4 more)
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
13 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(3 more)
Protein metabolic process GO:0019538
The chemical reactions and pathways involving a protein. Includes protein modification.
13 P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(3 more)
Positive regulation of myotube differentiation GO:0010831
Any process that activates, maintains or increases the frequency, rate or extent of myotube differentiation. Myotube differentiation is the process in which a relatively unspecialized cell acquires specialized features of a myotube cell. Myotubes are multinucleated cells that are formed when proliferating myoblasts exit the cell cycle, differentiate and fuse.
6 P50281 (/ISS) Q10739 (/ISS) Q5RES1 (/ISS) Q95220 (/ISS) Q9GLE4 (/ISS) Q9XT90 (/ISS)
Positive regulation of B cell differentiation GO:0045579
Any process that activates or increases the frequency, rate or extent of B cell differentiation.
6 P50281 (/ISS) Q10739 (/ISS) Q5RES1 (/ISS) Q95220 (/ISS) Q9GLE4 (/ISS) Q9XT90 (/ISS)
Negative regulation of Notch signaling pathway GO:0045746
Any process that stops, prevents, or reduces the frequency, rate or extent of the Notch signaling pathway.
6 P50281 (/ISS) Q10739 (/ISS) Q5RES1 (/ISS) Q95220 (/ISS) Q9GLE4 (/ISS) Q9XT90 (/ISS)
Anterior/posterior axis specification GO:0009948
The establishment, maintenance and elaboration of the anterior/posterior axis. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism.
5 B0R0I1 (/IMP) B3DFR2 (/IMP) F1Q899 (/IMP) Q7T2J1 (/IMP) Q7T2J2 (/IMP)
Establishment of cell polarity GO:0030010
The specification and formation of anisotropic intracellular organization or cell growth patterns.
5 B0R0I1 (/IGI) B3DFR2 (/IGI) F1Q899 (/IGI) Q7T2J1 (/IGI) Q7T2J2 (/IGI)
Showing 1 to 10 of 90 entries

There are 27 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 TermAnnotationsEvidence
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
16 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(6 more)
Golgi lumen GO:0005796
The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks.
14 P50281 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS) P51512 (/TAS)
(4 more)
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
14 P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA) P51512 (/IDA)
(4 more)
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
5 P50281 (/TAS) P51511 (/TAS) P51511 (/TAS) Q9Y5R2 (/TAS) Q9Y5R2 (/TAS)
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Trans-Golgi network membrane GO:0032588
The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network.
3 Q99PW6 (/ISS) Q9Y5R2 (/ISS) Q9Y5R2 (/ISS)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
2 Q9Y5R2 (/HDA) Q9Y5R2 (/HDA)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
1 P50281 (/IMP)
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
1 P53690 (/ISO)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P50281 (/IMP)
Showing 1 to 10 of 27 entries
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