The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Trypsin-like serine proteases
".

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 46527: Inactive serine protease 45

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 10 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
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 P20231 (/IPI) P21845 (/IPI) Q15661 (/IPI)
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
3 P20231 (/TAS) Q15661 (/TAS) Q9BZJ3 (/TAS)
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
2 P20231 (/NAS) Q15661 (/NAS)
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
2 Q15661 (/TAS) Q6IE62 (/TAS)
Heparin binding GO:0008201
Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
2 P21845 (/IDA) Q80UR4 (/IDA)
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
2 P21845 (/IDA) Q02844 (/IDA)
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
2 Q80UR4 (/IDA) Q99MS4 (/IDA)
Glycosaminoglycan binding GO:0005539
Interacting selectively and non-covalently with any glycan (polysaccharide) containing a substantial proportion of aminomonosaccharide residues.
1 Q80UR4 (/IDA)
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
1 Q99MS4 (/IMP)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
1 Q99MS4 (/IPI)

There are 11 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
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
2 Q02844 (/IDA) Q99MS4 (/IDA)
Blastocyst hatching GO:0001835
The hatching of the cellular blastocyst from the zona pellucida.
1 Q99MS4 (/IGI)
Blastocyst hatching GO:0001835
The hatching of the cellular blastocyst from the zona pellucida.
1 Q99MS4 (/IMP)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q80UR4 (/IC)
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
1 Q99MS4 (/IMP)
Defense response GO:0006952
Reactions, triggered in response to the presence of a foreign body or the occurrence of an injury, which result in restriction of damage to the organism attacked or prevention/recovery from the infection caused by the attack.
1 Q15661 (/TAS)
Inflammatory response GO:0006954
The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
1 P21845 (/TAS)
Embryo implantation GO:0007566
Attachment of the blastocyst to the uterine lining.
1 Q99MS4 (/IGI)
Peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan GO:0019800
The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain.
1 Q80UR4 (/IDA)
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
1 Q15661 (/TAS)
Negative regulation of blood coagulation GO:0030195
Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation.
1 Q02844 (/TAS)

There are 5 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
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.
4 Q02844 (/IDA) Q15661 (/IDA) Q80UR4 (/IDA) Q99MS4 (/IDA)
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
2 P21845 (/TAS) Q15661 (/TAS)
Proteinaceous extracellular matrix GO:0005578
A layer consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that forms a sheet underlying or overlying cells such as endothelial and epithelial cells. The proteins are secreted by cells in the vicinity. An example of this component is found in Mus musculus.
1 Q80UR4 (/IDA)
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 P21845 (/ISO)
Mast cell granule GO:0042629
Coarse, bluish-black staining cytoplasmic granules, bounded by a plasma membrane and found in mast cells and basophils. Contents include histamine, heparin, chondroitin sulfates, chymase and tryptase.
1 Q02844 (/IDA)