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
".
FunFam 21040: Acr protein
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 |
|---|---|---|
|
Amidase activity GO:0004040
Catalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3.
|
1 | P23578 (/ISS) |
|
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).
|
1 | P23578 (/ISO) |
|
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).
|
1 | P23578 (/ISS) |
|
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).
|
1 | P23578 (/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 | P23578 (/IPI) |
|
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
|
1 | P23578 (/ISO) |
|
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
|
1 | P23578 (/ISS) |
|
Drug binding GO:0008144
Interacting selectively and non-covalently with a drug, any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease.
|
1 | P23578 (/ISS) |
|
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.
|
1 | P23578 (/IMP) |
|
Fucose binding GO:0042806
Interacting selectively and non-covalently with fucose, the pentose 6-deoxygalactose.
|
1 | P23578 (/ISS) |
There are 9 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 |
|---|---|---|
|
Activation of adenylate cyclase activity GO:0007190
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
|
1 | P23578 (/ISO) |
|
Activation of adenylate cyclase activity GO:0007190
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
|
1 | P23578 (/ISS) |
|
Single fertilization GO:0007338
The union of male and female gametes to form a zygote.
|
1 | P23578 (/IMP) |
|
Binding of sperm to zona pellucida GO:0007339
The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place.
|
1 | P23578 (/IGI) |
|
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida surrounding the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the egg.
|
1 | P23578 (/ISO) |
|
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida surrounding the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the egg.
|
1 | P23578 (/ISS) |
|
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida surrounding the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the egg.
|
1 | P23578 (/TAS) |
|
Penetration of zona pellucida GO:0007341
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
|
1 | P23578 (/IGI) |
|
Penetration of zona pellucida GO:0007341
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
|
1 | P23578 (/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 |
|---|---|---|
|
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
|
1 | P23578 (/IDA) |
|
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 | P23578 (/ISO) |
|
Acrosomal matrix GO:0043159
A structural framework, or 'dense core' at the interior of an acrosome. May regulate the distribution of hydrolases within the acrosome and their release during the acrosome reaction.
|
1 | P23578 (/TAS) |
|
Protein complex GO:0043234
A stable macromolecular complex composed (only) of two or more polypeptide subunits along with any covalently attached molecules (such as lipid anchors or oligosaccharide) or non-protein prosthetic groups (such as nucleotides or metal ions). Prosthetic group in this context refers to a tightly bound cofactor. The component polypeptide subunits may be identical.
|
1 | P23578 (/ISO) |