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Conserved domains on  [gi|966751393|ref|NP_001304939|]
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caspase recruitment domain-containing protein 19 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
10-50 3.56e-22

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 cd13785:

Pssm-ID: 472698  Cd Length: 86  Bit Score: 82.52  E-value: 3.56e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 966751393  10 LVQDTPFLTGHGRLSEQQVDRIILQLNRYYPQILTNKEAEK 50
Cdd:cd13785    1 LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEK 41
 
Name Accession Description Interval E-value
CARD_BinCARD_like cd13785
BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD ...
10-50 3.56e-22

BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD (Caspase activation and recruitment domain) protein in all tissues. CARD proteins play important role in apoptosis by functioning as direct regulators of death-inducing caspases. BinCARD interacts with apoptosis inducer CARD protein Bcl10 through CARD. It inhibits Bcl10-mediated activation of NF-kappa B and to suppress Bcl10 phosphorylation. Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. In general, DDs domains 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: 260079  Cd Length: 86  Bit Score: 82.52  E-value: 3.56e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 966751393  10 LVQDTPFLTGHGRLSEQQVDRIILQLNRYYPQILTNKEAEK 50
Cdd:cd13785    1 LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEK 41
 
Name Accession Description Interval E-value
CARD_BinCARD_like cd13785
BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD ...
10-50 3.56e-22

BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD (Caspase activation and recruitment domain) protein in all tissues. CARD proteins play important role in apoptosis by functioning as direct regulators of death-inducing caspases. BinCARD interacts with apoptosis inducer CARD protein Bcl10 through CARD. It inhibits Bcl10-mediated activation of NF-kappa B and to suppress Bcl10 phosphorylation. Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. In general, DDs domains 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: 260079  Cd Length: 86  Bit Score: 82.52  E-value: 3.56e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 966751393  10 LVQDTPFLTGHGRLSEQQVDRIILQLNRYYPQILTNKEAEK 50
Cdd:cd13785    1 LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEK 41
 
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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