apoptotic protease-activating factor 1 [Crotalus tigris]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
623-1206 | 6.89e-74 | |||||||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 251.75 E-value: 6.89e-74
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| APAF1_C | pfam17908 | APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
453-587 | 8.31e-60 | |||||||||
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein. : Pssm-ID: 465560 Cd Length: 135 Bit Score: 201.11 E-value: 8.31e-60
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| NB-ARC super family | cl26397 | NB-ARC domain; |
144-374 | 5.00e-50 | |||||||||
NB-ARC domain; The actual alignment was detected with superfamily member pfam00931: Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 177.57 E-value: 5.00e-50
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| DD super family | cl14633 | Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ... |
7-91 | 5.98e-41 | |||||||||
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer. The actual alignment was detected with superfamily member cd08323: Pssm-ID: 472698 Cd Length: 86 Bit Score: 145.34 E-value: 5.98e-41
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| Name | Accession | Description | Interval | E-value | |||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
623-1206 | 6.89e-74 | |||||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 251.75 E-value: 6.89e-74
|
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
614-906 | 1.18e-70 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 238.39 E-value: 1.18e-70
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| APAF1_C | pfam17908 | APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
453-587 | 8.31e-60 | |||||||||
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein. Pssm-ID: 465560 Cd Length: 135 Bit Score: 201.11 E-value: 8.31e-60
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| NB-ARC | pfam00931 | NB-ARC domain; |
144-374 | 5.00e-50 | |||||||||
NB-ARC domain; Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 177.57 E-value: 5.00e-50
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| CARD_APAF1 | cd08323 | Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-91 | 5.98e-41 | |||||||||
Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to 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: 260034 Cd Length: 86 Bit Score: 145.34 E-value: 5.98e-41
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
11-90 | 9.01e-17 | |||||||||
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: 76.44 E-value: 9.01e-17
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
559-910 | 7.13e-11 | |||||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 66.65 E-value: 7.13e-11
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
728-767 | 3.62e-10 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 56.17 E-value: 3.62e-10
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
731-767 | 2.06e-09 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.89 E-value: 2.06e-09
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| CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-78 | 4.87e-07 | |||||||||
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: 48.87 E-value: 4.87e-07
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
119-375 | 1.97e-04 | |||||||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 45.68 E-value: 1.97e-04
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| NACHT | COG5635 | Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
150-369 | 1.06e-03 | |||||||||
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 43.25 E-value: 1.06e-03
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| Name | Accession | Description | Interval | E-value | |||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
623-1206 | 6.89e-74 | |||||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 251.75 E-value: 6.89e-74
|
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
608-1033 | 5.51e-72 | |||||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 246.36 E-value: 5.51e-72
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
614-906 | 1.18e-70 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 238.39 E-value: 1.18e-70
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
801-1228 | 2.89e-69 | |||||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 238.66 E-value: 2.89e-69
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
960-1234 | 4.50e-62 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 213.74 E-value: 4.50e-62
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
652-1030 | 4.97e-60 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 207.96 E-value: 4.97e-60
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| APAF1_C | pfam17908 | APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
453-587 | 8.31e-60 | |||||||||
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein. Pssm-ID: 465560 Cd Length: 135 Bit Score: 201.11 E-value: 8.31e-60
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| NB-ARC | pfam00931 | NB-ARC domain; |
144-374 | 5.00e-50 | |||||||||
NB-ARC domain; Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 177.57 E-value: 5.00e-50
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
610-820 | 1.64e-47 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 171.75 E-value: 1.64e-47
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
968-1234 | 3.72e-45 | |||||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 168.55 E-value: 3.72e-45
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| CARD_APAF1 | cd08323 | Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-91 | 5.98e-41 | |||||||||
Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to 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: 260034 Cd Length: 86 Bit Score: 145.34 E-value: 5.98e-41
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1076-1248 | 9.99e-25 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 105.88 E-value: 9.99e-25
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| CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
9-87 | 7.10e-17 | |||||||||
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: 76.40 E-value: 7.10e-17
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
11-90 | 9.01e-17 | |||||||||
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: 76.44 E-value: 9.01e-17
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
610-685 | 2.64e-12 | |||||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 68.90 E-value: 2.64e-12
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
559-910 | 7.13e-11 | |||||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 66.65 E-value: 7.13e-11
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
728-767 | 3.62e-10 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 56.17 E-value: 3.62e-10
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
731-767 | 2.06e-09 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.89 E-value: 2.06e-09
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| PTZ00421 | PTZ00421 | coronin; Provisional |
1013-1131 | 1.50e-08 | |||||||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 58.75 E-value: 1.50e-08
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
870-1170 | 2.10e-08 | |||||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 58.56 E-value: 2.10e-08
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
646-685 | 6.36e-08 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 49.62 E-value: 6.36e-08
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
647-685 | 1.44e-07 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 48.88 E-value: 1.44e-07
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| CARD_CASP9 | cd08326 | Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ... |
6-88 | 2.71e-07 | |||||||||
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: 49.35 E-value: 2.71e-07
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| CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-78 | 4.87e-07 | |||||||||
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: 48.87 E-value: 4.87e-07
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| CARD_BIRC2_BIRC3 | cd08329 | Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
7-85 | 6.23e-07 | |||||||||
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: 48.60 E-value: 6.23e-07
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| CARD_2 | pfam16739 | Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ... |
1-89 | 7.59e-07 | |||||||||
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: 48.36 E-value: 7.59e-07
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| CARD_CASP2 | cd08332 | Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ... |
1-87 | 8.20e-07 | |||||||||
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: 48.19 E-value: 8.20e-07
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| PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
1054-1226 | 3.82e-06 | |||||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 51.24 E-value: 3.82e-06
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
869-906 | 5.21e-06 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 44.26 E-value: 5.21e-06
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
867-906 | 5.67e-06 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 44.23 E-value: 5.67e-06
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
1119-1154 | 7.42e-06 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.87 E-value: 7.42e-06
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1119-1154 | 7.84e-06 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.84 E-value: 7.84e-06
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
992-1030 | 4.61e-05 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.56 E-value: 4.61e-05
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1073-1112 | 5.59e-05 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.53 E-value: 5.59e-05
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
991-1030 | 6.22e-05 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.14 E-value: 6.22e-05
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
688-725 | 6.54e-05 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.14 E-value: 6.54e-05
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
1074-1112 | 1.29e-04 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.41 E-value: 1.29e-04
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| FxSxx_TPR | NF040586 | FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
119-375 | 1.97e-04 | |||||||||
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids. Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 45.68 E-value: 1.97e-04
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
610-643 | 4.15e-04 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.83 E-value: 4.15e-04
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
689-725 | 5.33e-04 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 5.33e-04
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| NACHT | COG5635 | Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
150-369 | 1.06e-03 | |||||||||
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 43.25 E-value: 1.06e-03
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| CARD_BCL10 | cd08810 | Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ... |
14-79 | 1.50e-03 | |||||||||
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: 38.87 E-value: 1.50e-03
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| PTZ00421 | PTZ00421 | coronin; Provisional |
630-698 | 1.91e-03 | |||||||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 42.19 E-value: 1.91e-03
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| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1175-1203 | 2.78e-03 | |||||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 36.52 E-value: 2.78e-03
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| ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
712-805 | 3.86e-03 | |||||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 37.64 E-value: 3.86e-03
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| WD40 | pfam00400 | WD domain, G-beta repeat; |
610-642 | 4.79e-03 | |||||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 4.79e-03
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| CARD_MDA5_r2 | cd08819 | Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and ... |
19-88 | 7.24e-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: 7.24e-03
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| Ge1_WD40 | pfam16529 | WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ... |
639-750 | 8.34e-03 | |||||||||
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions. Pssm-ID: 465162 [Multi-domain] Cd Length: 328 Bit Score: 39.75 E-value: 8.34e-03
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| Blast search parameters | ||||
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