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:
"Peptidase S8 propeptide/proteinase inhibitor I9
".
FunFam 8: Alkaline protease 1
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 7 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 |
---|---|---|
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).
|
6 | P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P12547 (/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.
|
5 | P28296 (/IMP) P28296 (/IMP) P28296 (/IMP) P40903 (/IMP) Q00208 (/IMP) |
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.
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/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).
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
IgE binding GO:0019863
Interacting selectively and non-covalently with an immunoglobulin of the IgE isotype.
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
Fibrinogen binding GO:0070051
Interacting selectively and non-covalently with fibrinogen, a highly soluble hexameric glycoprotein complex that is found in blood plasma and is converted to fibrin by thrombin in the coagulation cascade.
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | P40903 (/IMP) |
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 |
---|---|---|
Complement activation GO:0006956
Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway.
|
3 | P28296 (/IMP) P28296 (/IMP) P28296 (/IMP) |
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
|
3 | P28296 (/IMP) P28296 (/IMP) P28296 (/IMP) |
Protein catabolic process GO:0030163
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
3 | P28296 (/IMP) P28296 (/IMP) P28296 (/IMP) |
Active evasion of host immune response via regulation of host complement system GO:0042784
Any mechanism of active immune avoidance which works by regulating the host complement system, e.g. by possessing complement receptors which mediate attachment to, then infection of, host macrophages, which are eventually destroyed. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
Active evasion of host immune response via regulation of host complement system GO:0042784
Any mechanism of active immune avoidance which works by regulating the host complement system, e.g. by possessing complement receptors which mediate attachment to, then infection of, host macrophages, which are eventually destroyed. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
3 | P28296 (/IMP) P28296 (/IMP) P28296 (/IMP) |
Elastin catabolic process GO:0060309
The chemical reactions and pathways resulting in the breakdown of elastin. Elastin is a glycoprotein which is randomly coiled and crosslinked to form elastic fibers that are found in connective tissue.
|
3 | P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
Elastin catabolic process GO:0060309
The chemical reactions and pathways resulting in the breakdown of elastin. Elastin is a glycoprotein which is randomly coiled and crosslinked to form elastic fibers that are found in connective tissue.
|
3 | P28296 (/IMP) P28296 (/IMP) P28296 (/IMP) |
Conjugation with cellular fusion GO:0000747
A conjugation process that results in the union of cellular and genetic information from compatible mating types. An example of this process is found in Saccharomyces cerevisiae.
|
1 | P40903 (/IMP) |
Autophagy GO:0006914
The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.
|
1 | P40903 (/IMP) |
Vacuole organization GO:0007033
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a vacuole.
|
1 | P40903 (/IMP) |
There are 4 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 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.
|
9 | P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P12547 (/IDA) P28296 (/IDA) P28296 (/IDA) P28296 (/IDA) |
Fungal-type vacuole GO:0000324
A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
|
1 | P40903 (/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.
|
1 | Q00208 (/IMP) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
1 | P40903 (/HDA) |