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:
"Death Domain, Fas
".
FunFam 49: NLR family pyrin domain containing 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 5 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).
|
1 | Q9C000 (/IPI) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
1 | Q9C000 (/IDA) |
Cysteine-type endopeptidase activator activity involved in apoptotic process GO:0008656
Increases the rate of proteolysis catalyzed by a cysteine-type endopeptidase involved in the apoptotic process.
|
1 | Q9C000 (/NAS) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
1 | Q9C000 (/IPI) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
1 | Q9C000 (/IPI) |
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 |
---|---|---|
Apoptotic process GO:0006915
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
|
1 | Q9C000 (/NAS) |
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
|
1 | Q9C000 (/IDA) |
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
|
1 | Q9C000 (/NAS) |
Response to muramyl dipeptide GO:0032495
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan.
|
1 | Q9C000 (/ISS) |
Defense response to bacterium GO:0042742
Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
|
1 | Q9C000 (/ISS) |
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
|
1 | Q9C000 (/ISS) |
Regulation of inflammatory response GO:0050727
Any process that modulates the frequency, rate or extent of the inflammatory response, the immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents.
|
1 | Q9C000 (/IC) |
Neuron apoptotic process GO:0051402
Any apoptotic process in a neuron, the basic cellular unit of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system.
|
1 | Q9C000 (/IDA) |
NLRP1 inflammasome complex assembly GO:1904784
The aggregation, arrangement and bonding together of a set of components to form a NLRP1 inflammasome complex.
|
1 | Q9C000 (/IMP) |
There are 6 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 |
---|---|---|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | I3L2G5 (/IDA) Q9C000 (/IDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | I3L2G5 (/IDA) Q9C000 (/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 | Q9C000 (/IDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | Q9C000 (/TAS) |
NLRP1 inflammasome complex GO:0072558
A protein complex that consists of two components, NLRP1 (NALP1) and caspase-1 or caspase-5. The exact mechanisms of NLRP1 activation remain obscure, but potassium ion efflux appears to be essential.
|
1 | Q9C000 (/IDA) |
NLRP1 inflammasome complex GO:0072558
A protein complex that consists of two components, NLRP1 (NALP1) and caspase-1 or caspase-5. The exact mechanisms of NLRP1 activation remain obscure, but potassium ion efflux appears to be essential.
|
1 | Q9C000 (/TAS) |