CATH Superfamily 3.30.60.30
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: waiting to be named.
FunFam 37: Ovomucoid
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 8 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 inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
4 | G1MZX1 (/IDA) P10184 (/IDA) Q8BT20 (/IDA) Q8BT20 (/IDA) |
Serine-type endopeptidase inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
2 | Q8BT20 (/ISM) Q8BT20 (/ISM) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
1 | P10184 (/IDA) |
Serine-type endopeptidase inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
1 | P10184 (/TAS) |
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).
|
1 | P10184 (/IPI) |
Ion channel inhibitor activity GO:0008200
Stops, prevents, or reduces the activity of an ion channel.
|
1 | P10184 (/IDA) |
Potassium channel inhibitor activity GO:0019870
Stops, prevents, or reduces the activity of a potassium channel.
|
1 | P10184 (/IDA) |
Peptidase inhibitor activity GO:0030414
Stops, prevents or reduces the activity of a peptidase, any enzyme that catalyzes the hydrolysis peptide bonds.
|
1 | P10184 (/IDA) |
There are 6 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 |
---|---|---|
Negative regulation of serine-type endopeptidase activity GO:1900004
Any process that stops, prevents or reduces the frequency, rate or extent of serine-type endopeptidase activity.
|
2 | Q8BT20 (/IDA) Q8BT20 (/IDA) |
Negative regulation of viral genome replication GO:0045071
Any process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication.
|
1 | P10184 (/IDA) |
Negative regulation of proteolysis GO:0045861
Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
|
1 | Q9D256 (/IDA) |
Defense response to Gram-positive bacterium GO:0050830
Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
|
1 | G1MZX1 (/IDA) |
Response to corticosterone GO:0051412
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a corticosterone stimulus. Corticosterone is a 21 carbon steroid hormone of the corticosteroid type, produced in the cortex of the adrenal glands. In many species, corticosterone is the principal glucocorticoid, involved in regulation of fuel metabolism, immune reactions, and stress responses.
|
1 | P10184 (/IDA) |
Cornification GO:0070268
A type of programmed cell death that occurs in the epidermis, morphologically and biochemically distinct from apoptosis. It leads to the formation of corneocytes, i.e. dead keratinocytes containing an amalgam of specific proteins (e.g., keratin, loricrin, SPR and involucrin) and lipids (e.g., fatty acids and ceramides), which are necessary for the function of the cornified skin layer (mechanical resistance, elasticity, water repellence and structural stability).
|
1 | Q6UWN8 (/TAS) |
There are 9 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.
|
2 | Q8BT20 (/IDA) Q8BT20 (/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 | P10184 (/TAS) Q6UWN8 (/TAS) |
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 | G1MZX1 (/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 | P10184 (/TAS) |
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
|
1 | G1MZX1 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | G1MZX1 (/IDA) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
1 | P10184 (/IDA) |
Apical cytoplasm GO:0090651
The region of the cytoplasm located at the apical side of the cell. Used in reference to animal polarized epithelial cells.
|
1 | G1MZX1 (/IDA) |
Sperm cytoplasmic droplet GO:0097598
A small amount of cytoplasm surrounded by a cell membrane that is generally retained in spermatozoa after spermiogenesis, when the majority of the cytoplasm is phagocytosed by Sertoli cells to produce \residual bodies\. Initially, the droplet is located at the neck just behind the head of an elongated spermatid. During epididymal transit, the cytoplasmic droplet migrates caudally to the annulus at the end of the midpiece; the exact position and time varies by species. The cytoplasmic droplet consists of lipids, lipoproteins, RNAs, a variety of hydrolytic enzymes, receptors, ion channels, and Golgi-derived vesicles. The droplet may be involved in regulatory volume loss (RVD) at ejaculation, and in most species, though not in humans, the cytoplasmic droplet is lost at ejaculation. Note that the cytoplasmic droplet is distinct from \excessive residual cytoplasm\ that sometimes remains in epididymal spermatozoa, particularly when spermiogenesis has been disrupted.
|
1 | G1MZX1 (/IDA) |