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Conserved domains on  [gi|262118805|pdb|3KAT|A]
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Chain A, NACHT, LRR and PYD domains-containing protein 1

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; ...
 20-100 4.59e-39

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: 125.02  E-value: 4.59e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KAT_A       20 HFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQ*RKLFSLSQSWDRKCKDGLYQALKETHPHLI*EL 99
Cdd:cd08330   1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                .
3KAT_A      100 W 100
Cdd:cd08330  81 E 81
 
Name Accession Description Interval E-value
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 20-100 4.59e-39

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: 125.02  E-value: 4.59e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KAT_A       20 HFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQ*RKLFSLSQSWDRKCKDGLYQALKETHPHLI*EL 99
Cdd:cd08330   1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                .
3KAT_A      100 W 100
Cdd:cd08330  81 E 81
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 19-100 2.91e-20

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: 77.60  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KAT_A         19 LHFVDQYREQLIARVTSVEVVLDKLHG-QVLSQEQYERVLAENTRPSQ*RKLFSLSQSWDRKCKDGLYQALKETHPHLI* 97
Cdd:pfam00619   1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                  ...
3KAT_A         98 ELW 100
Cdd:pfam00619  81 DLE 83
 
Name Accession Description Interval E-value
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 20-100 4.59e-39

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: 125.02  E-value: 4.59e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KAT_A       20 HFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQ*RKLFSLSQSWDRKCKDGLYQALKETHPHLI*EL 99
Cdd:cd08330   1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                .
3KAT_A      100 W 100
Cdd:cd08330  81 E 81
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 19-100 2.91e-20

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: 77.60  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3KAT_A         19 LHFVDQYREQLIARVTSVEVVLDKLHG-QVLSQEQYERVLAENTRPSQ*RKLFSLSQSWDRKCKDGLYQALKETHPHLI* 97
Cdd:pfam00619   1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                  ...
3KAT_A         98 ELW 100
Cdd:pfam00619  81 DLE 83
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 24-99 4.28e-11

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: 54.06  E-value: 4.28e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3KAT_A       24 QYREQLIARVtSVEVVLDKLHG-QVLSQEQYERVLAENTRPSQ*RKLFSLSQSWDRKCKDGLYQALKETH-PHLI*EL 99
Cdd:cd01671   3 KNRVELVEDL-DVEDILDHLIQkGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGqPHLAELL 79
 
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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