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Conserved domains on  [gi|21312030|ref|NP_081014|]
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caspase recruitment domain-containing protein 19 isoform 1 [Mus musculus]

Protein Classification

protein kinase family protein( domain architecture ID 10194960)

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_BinCARD_like cd13785
BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD ...
 10-95 3.88e-48

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: 151.47  E-value: 3.88e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312030  10 LVQDTPFLTGQGRLSEQQVDRIILQLNRYYPQILTNKEAEKFRNPKASLRVRLCDLLSHLQQRGERHCQEFYRALYIHAQ 89
Cdd:cd13785   1 LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEKFRNPKAPLRVRLADLLKHLQRKGERDCQEFYRALHIHAE 80


                ....*.
gi 21312030  90 PLHSHL 95
Cdd:cd13785  81 PLYSDL 86
 
Name Accession Description Interval E-value
CARD_BinCARD_like cd13785
BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD ...
 10-95 3.88e-48

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: 151.47  E-value: 3.88e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312030  10 LVQDTPFLTGQGRLSEQQVDRIILQLNRYYPQILTNKEAEKFRNPKASLRVRLCDLLSHLQQRGERHCQEFYRALYIHAQ 89
Cdd:cd13785   1 LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEKFRNPKAPLRVRLADLLKHLQRKGERDCQEFYRALHIHAE 80


                ....*.
gi 21312030  90 PLHSHL 95
Cdd:cd13785  81 PLYSDL 86
 
Name Accession Description Interval E-value
CARD_BinCARD_like cd13785
BinCARD (Bcl10-interacting protein with CARD); BinCARD was ubiquitously expressed CRAD ...
 10-95 3.88e-48

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: 151.47  E-value: 3.88e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312030  10 LVQDTPFLTGQGRLSEQQVDRIILQLNRYYPQILTNKEAEKFRNPKASLRVRLCDLLSHLQQRGERHCQEFYRALYIHAQ 89
Cdd:cd13785   1 LLQDTPFLTSDGRLSEQLVDRIILQLNRVYPQILTNKEAEKFRNPKAPLRVRLADLLKHLQRKGERDCQEFYRALHIHAE 80


                ....*.
gi 21312030  90 PLHSHL 95
Cdd:cd13785  81 PLYSDL 86
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 23-95 1.51e-04

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: 38.65  E-value: 1.51e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312030  23 LSEQQVDRIILQLNRYypQILTNKEAEKFRNPKaSLRVRLCDLLSHLQQRGERHCQEFYRALYIHAQP-LHSHL 95
Cdd:cd01671   9 VEDLDVEDILDHLIQK--GVLTEEDKEEILSEK-TRQDKARKLLDILPRRGPKAFEVFCEALRETGQPhLAELL 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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