caspase-2 isoform X1 [Strigops habroptila]
Protein Classification
caspase( domain architecture ID 10170012)
caspase is a cysteine-dependent aspartate-directed protease that mediates programmed cell death; belongs to the peptidase C14 family
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
158-413 | 2.83e-94 | |||||
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: 283.34 E-value: 2.83e-94
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| CARD_CASP2 | cd08332 | Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ... |
1-87 | 1.31e-44 | |||||
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. 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: 260040 Cd Length: 87 Bit Score: 149.88 E-value: 1.31e-44
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| Name | Accession | Description | Interval | E-value | |||||
| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
158-413 | 2.83e-94 | |||||
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: 283.34 E-value: 2.83e-94
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| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
159-414 | 1.90e-92 | |||||
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: 278.35 E-value: 1.90e-92
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| Peptidase_C14 | pfam00656 | Caspase domain; |
166-411 | 3.51e-59 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 192.15 E-value: 3.51e-59
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| CARD_CASP2 | cd08332 | Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ... |
1-87 | 1.31e-44 | |||||
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. 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: 260040 Cd Length: 87 Bit Score: 149.88 E-value: 1.31e-44
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| CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-84 | 8.21e-19 | |||||
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: 80.46 E-value: 8.21e-19
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-83 | 3.61e-18 | |||||
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: 78.76 E-value: 3.61e-18
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| Name | Accession | Description | Interval | E-value | |||||
| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
158-413 | 2.83e-94 | |||||
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: 283.34 E-value: 2.83e-94
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| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
159-414 | 1.90e-92 | |||||
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: 278.35 E-value: 1.90e-92
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| Peptidase_C14 | pfam00656 | Caspase domain; |
166-411 | 3.51e-59 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 192.15 E-value: 3.51e-59
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| CARD_CASP2 | cd08332 | Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ... |
1-87 | 1.31e-44 | |||||
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. 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: 260040 Cd Length: 87 Bit Score: 149.88 E-value: 1.31e-44
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| CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
9-83 | 2.14e-24 | |||||
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: 95.66 E-value: 2.14e-24
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| CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-84 | 8.21e-19 | |||||
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: 80.46 E-value: 8.21e-19
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-83 | 3.61e-18 | |||||
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: 78.76 E-value: 3.61e-18
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| CARD_CASP9 | cd08326 | Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ... |
5-83 | 3.31e-17 | |||||
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) 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: 176740 Cd Length: 84 Bit Score: 75.93 E-value: 3.31e-17
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| CARD_RAIDD | cd08327 | Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ... |
1-77 | 8.27e-10 | |||||
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs 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: 260037 Cd Length: 94 Bit Score: 55.55 E-value: 8.27e-10
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| CARD_BCL10 | cd08810 | Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ... |
6-81 | 2.10e-08 | |||||
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. 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: 260072 [Multi-domain] Cd Length: 85 Bit Score: 51.19 E-value: 2.10e-08
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| CARD_2 | pfam16739 | Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ... |
5-83 | 8.18e-04 | |||||
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain. Pssm-ID: 465251 Cd Length: 93 Bit Score: 38.34 E-value: 8.18e-04
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| CARD_CARD9-like | cd08785 | Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ... |
7-86 | 2.72e-03 | |||||
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. 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: 260055 Cd Length: 84 Bit Score: 36.58 E-value: 2.72e-03
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| CARD_MDA5_r2 | cd08819 | Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and ... |
20-83 | 2.77e-03 | |||||
Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), second repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates with IPS-1 through a CARD-CARD interaction. 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: 260078 Cd Length: 92 Bit Score: 36.93 E-value: 2.77e-03
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