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Conserved domains on  [gi|221220216|gb|ACM08769|]
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Apoptosis-associated speck-like protein containing a CARD [Salmo salar]

Protein Classification

protein kinase family protein( domain architecture ID 10169997)

protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 15-97 5.74e-36

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. 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: 260039  Cd Length: 81  Bit Score: 116.93  E-value: 5.74e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221220216 15 HFVDHHRTALIDRVSQVEPLLDRLLDrGIITQNAYSEVRANRTNQKKMRELFDGPlKACGPKGKDIFLDILMDLEPFLII 94
Cdd:cd08330   1 HFVDRHREALIQRVTNVDPILDELRG-KVLTQEQYSSIRAERTNQEKMRKLYELV-PSWGRTCKDLFYQALKETNPYLVE 78


                ...
gi 221220216 95 DLK 97
Cdd:cd08330  79 DLE 81
 
Name Accession Description Interval E-value
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 15-97 5.74e-36

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. 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: 260039  Cd Length: 81  Bit Score: 116.93  E-value: 5.74e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221220216 15 HFVDHHRTALIDRVSQVEPLLDRLLDrGIITQNAYSEVRANRTNQKKMRELFDGPlKACGPKGKDIFLDILMDLEPFLII 94
Cdd:cd08330   1 HFVDRHREALIQRVTNVDPILDELRG-KVLTQEQYSSIRAERTNQEKMRKLYELV-PSWGRTCKDLFYQALKETNPYLVE 78


                ...
gi 221220216 95 DLK 97
Cdd:cd08330  79 DLE 81
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 14-96 1.10e-13

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: 60.65  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221220216  14 KHFVDHHRTALIDRVSQVEPLLDRLLDRGIITQNAYSEVRANRTNQKKMRELFDGpLKACGPKGKDIFLDILMDLEPFLI 93
Cdd:pfam00619  1 RKLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDL-VLKKGPKACQIFLEALKEGDPDLA 79


                 ...
gi 221220216  94 IDL 96
Cdd:pfam00619 80 SDL 82
 
Name Accession Description Interval E-value
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 15-97 5.74e-36

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. 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: 260039  Cd Length: 81  Bit Score: 116.93  E-value: 5.74e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221220216 15 HFVDHHRTALIDRVSQVEPLLDRLLDrGIITQNAYSEVRANRTNQKKMRELFDGPlKACGPKGKDIFLDILMDLEPFLII 94
Cdd:cd08330   1 HFVDRHREALIQRVTNVDPILDELRG-KVLTQEQYSSIRAERTNQEKMRKLYELV-PSWGRTCKDLFYQALKETNPYLVE 78


                ...
gi 221220216 95 DLK 97
Cdd:cd08330  79 DLE 81
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 14-96 1.10e-13

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: 60.65  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221220216  14 KHFVDHHRTALIDRVSQVEPLLDRLLDRGIITQNAYSEVRANRTNQKKMRELFDGpLKACGPKGKDIFLDILMDLEPFLI 93
Cdd:pfam00619  1 RKLLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDL-VLKKGPKACQIFLEALKEGDPDLA 79


                 ...
gi 221220216  94 IDL 96
Cdd:pfam00619 80 SDL 82
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 19-85 1.79e-09

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: 49.82  E-value: 1.79e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221220216 19 HHRTALIDRVsQVEPLLDRLLDRGIITQNAYSEVRANRTNQKKMRELFDGpLKACGPKGKDIFLDIL 85
Cdd:cd01671   3 KNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDI-LPRRGPKAFEVFCEAL 67
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 9-96 3.04e-08

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: 47.05  E-value: 3.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221220216  9 NMMKDKHFVDHHRTALIDRVSQVEPLLDRLLDRGIITQNAYSEVRANRTNQKKMRELFDGPLKacgpKGK---DIFLDIL 85
Cdd:cd08329   3 MASDDLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILV----KGNaaaEVFRNCL 78

                        90
                ....*....|.
gi 221220216 86 MDLEPFLIIDL 96
Cdd:cd08329  79 KEIDVVLYRDL 89
CARD_RAIDD cd08327
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ...
 12-87 2.36e-03

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: 34.36  E-value: 2.36e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221220216 12 KDKHFVDHHRTALIDRVSQVEPLLDRLLDRGIITQNAYSEVRANRTNQKKMRELFDgPLKACGPKGKDIFLDILMD 87
Cdd:cd08327   4 KHKQLLRSQRLELCAELLVDGLIVQYLYQEGILTESHVEEIQSQTTSRRKTLKLLD-ILPNRGPKAFHAFLDSLEE 78
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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