caspase-1 [Rattus norvegicus]
Protein Classification
caspase family protein( domain architecture ID 10871135)
caspase family protein similar to caspases which are cysteine class enzymes that drive the terminal stages of apoptosis as well as other cellular remodeling and inflammatory events
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
152-400 | 5.88e-121 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. : Pssm-ID: 214521 Cd Length: 241 Bit Score: 350.39 E-value: 5.88e-121
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| CARD_CASP1-like | cd08325 | Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ... |
6-87 | 6.88e-33 | |||||
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. : Pssm-ID: 260036 Cd Length: 83 Bit Score: 118.46 E-value: 6.88e-33
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| Name | Accession | Description | Interval | E-value | |||||
| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
152-400 | 5.88e-121 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. Pssm-ID: 214521 Cd Length: 241 Bit Score: 350.39 E-value: 5.88e-121
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| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
151-399 | 3.56e-100 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. Pssm-ID: 237997 Cd Length: 243 Bit Score: 297.59 E-value: 3.56e-100
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| Peptidase_C14 | pfam00656 | Caspase domain; |
161-397 | 9.13e-74 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 229.13 E-value: 9.13e-74
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| CARD_CASP1-like | cd08325 | Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ... |
6-87 | 6.88e-33 | |||||
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260036 Cd Length: 83 Bit Score: 118.46 E-value: 6.88e-33
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
3-90 | 1.43e-24 | |||||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold. Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 96.09 E-value: 1.43e-24
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| CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
7-89 | 4.05e-16 | |||||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain. Pssm-ID: 128424 Cd Length: 88 Bit Score: 73.14 E-value: 4.05e-16
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| Name | Accession | Description | Interval | E-value | |||||
| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
152-400 | 5.88e-121 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. Pssm-ID: 214521 Cd Length: 241 Bit Score: 350.39 E-value: 5.88e-121
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| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
151-399 | 3.56e-100 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. Pssm-ID: 237997 Cd Length: 243 Bit Score: 297.59 E-value: 3.56e-100
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| Peptidase_C14 | pfam00656 | Caspase domain; |
161-397 | 9.13e-74 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 229.13 E-value: 9.13e-74
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| CARD_CASP1-like | cd08325 | Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ... |
6-87 | 6.88e-33 | |||||
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260036 Cd Length: 83 Bit Score: 118.46 E-value: 6.88e-33
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
3-90 | 1.43e-24 | |||||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold. Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 96.09 E-value: 1.43e-24
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| CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
7-89 | 4.05e-16 | |||||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain. Pssm-ID: 128424 Cd Length: 88 Bit Score: 73.14 E-value: 4.05e-16
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| CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
6-87 | 2.45e-10 | |||||
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260018 [Multi-domain] Cd Length: 79 Bit Score: 56.37 E-value: 2.45e-10
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| CARD_BIRC2_BIRC3 | cd08329 | Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
25-91 | 2.22e-05 | |||||
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260038 Cd Length: 94 Bit Score: 42.82 E-value: 2.22e-05
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| CARD_RIP2_CARD3 | cd08786 | Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ... |
4-93 | 6.44e-04 | |||||
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 176764 Cd Length: 87 Bit Score: 38.37 E-value: 6.44e-04
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| CARD_NOD2_2_CARD15 | cd08788 | Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ... |
20-76 | 8.37e-04 | |||||
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260056 Cd Length: 81 Bit Score: 37.84 E-value: 8.37e-04
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