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Conserved domains on  [gi|81170679|sp|Q8VCF0|]
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RecName: Full=Mitochondrial antiviral-signaling protein; Short=MAVS; AltName: Full=CARD adapter inducing interferon beta; Short=Cardif; AltName: Full=Interferon beta promoter stimulator protein 1; Short=IPS-1; AltName: Full=Virus-induced-signaling adapter; Short=VISA

Protein Classification

protein kinase family protein( domain architecture ID 10172110)

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_IPS1 cd08811
Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and ...
 3-93 1.44e-46

Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and recruitment domain (CARD) found in IPS-1 (Interferon beta promoter stimulator protein 1), also known as CARDIF, VISA or MAVS. IPS-1 is an adaptor protein that plays an important role in interferon induction in response to viral infection. It is crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. The CARD of IPS-1 associates with the CARDs of two RNA helicases, RIG-I and MDA5, which bind viral DNA in the cytoplasm during the initial stage of intracellular antiviral response, leading to the induction of type I interferons. 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: 260073  Cd Length: 92  Bit Score: 156.75  E-value: 1.44e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679   3 FAEDKTYKYIRDNHSKFCC-VDVLEILPYLSCLTASDQDRLRASYRQIGNRDTLWGLFNNLQRRPGWVEVFIRALQICEL 81
Cdd:cd08811   1 FAEDKEYKYLRRNMGVFCHdIKVSEIIPYLPCLTRSDRDEILAKKDMSGNRDTAWTLLDHLQRRPGWVEDFIKALRNCEL 80

                        90
                ....*....|..
gi 81170679  82 PGLADQVTRVYQ 93
Cdd:cd08811  81 GHLADELERVYD 92
 
Name Accession Description Interval E-value
CARD_IPS1 cd08811
Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and ...
 3-93 1.44e-46

Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and recruitment domain (CARD) found in IPS-1 (Interferon beta promoter stimulator protein 1), also known as CARDIF, VISA or MAVS. IPS-1 is an adaptor protein that plays an important role in interferon induction in response to viral infection. It is crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. The CARD of IPS-1 associates with the CARDs of two RNA helicases, RIG-I and MDA5, which bind viral DNA in the cytoplasm during the initial stage of intracellular antiviral response, leading to the induction of type I interferons. 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: 260073  Cd Length: 92  Bit Score: 156.75  E-value: 1.44e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679   3 FAEDKTYKYIRDNHSKFCC-VDVLEILPYLSCLTASDQDRLRASYRQIGNRDTLWGLFNNLQRRPGWVEVFIRALQICEL 81
Cdd:cd08811   1 FAEDKEYKYLRRNMGVFCHdIKVSEIIPYLPCLTRSDRDEILAKKDMSGNRDTAWTLLDHLQRRPGWVEDFIKALRNCEL 80

                        90
                ....*....|..
gi 81170679  82 PGLADQVTRVYQ 93
Cdd:cd08811  81 GHLADELERVYD 92
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 5-92 8.07e-21

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: 86.88  E-value: 8.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679     5 EDKTYK-YIRDNHSKF-CCVDVLEILPYLS-CLTASDQDRLRASYRQIGNRDTLWGLFNNLQR--RPGWVEVFIRALQIC 79
Cdd:pfam16739   1 EDDEYRrLLRLFRPRLkDTIKPTEILPHLPeCLTEDDKERIRAETNNKGNTAAAELLLDRLVRsdREGWFRAFLDALRKT 80

                          90
                  ....*....|...
gi 81170679    80 ELPGLADQVTRVY 92
Cdd:pfam16739  81 GHDGLAEELEGEY 93
 
Name Accession Description Interval E-value
CARD_IPS1 cd08811
Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and ...
 3-93 1.44e-46

Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and recruitment domain (CARD) found in IPS-1 (Interferon beta promoter stimulator protein 1), also known as CARDIF, VISA or MAVS. IPS-1 is an adaptor protein that plays an important role in interferon induction in response to viral infection. It is crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. The CARD of IPS-1 associates with the CARDs of two RNA helicases, RIG-I and MDA5, which bind viral DNA in the cytoplasm during the initial stage of intracellular antiviral response, leading to the induction of type I interferons. 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: 260073  Cd Length: 92  Bit Score: 156.75  E-value: 1.44e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679   3 FAEDKTYKYIRDNHSKFCC-VDVLEILPYLSCLTASDQDRLRASYRQIGNRDTLWGLFNNLQRRPGWVEVFIRALQICEL 81
Cdd:cd08811   1 FAEDKEYKYLRRNMGVFCHdIKVSEIIPYLPCLTRSDRDEILAKKDMSGNRDTAWTLLDHLQRRPGWVEDFIKALRNCEL 80

                        90
                ....*....|..
gi 81170679  82 PGLADQVTRVYQ 93
Cdd:cd08811  81 GHLADELERVYD 92
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 5-92 8.07e-21

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: 86.88  E-value: 8.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679     5 EDKTYK-YIRDNHSKF-CCVDVLEILPYLS-CLTASDQDRLRASYRQIGNRDTLWGLFNNLQR--RPGWVEVFIRALQIC 79
Cdd:pfam16739   1 EDDEYRrLLRLFRPRLkDTIKPTEILPHLPeCLTEDDKERIRAETNNKGNTAAAELLLDRLVRsdREGWFRAFLDALRKT 80

                          90
                  ....*....|...
gi 81170679    80 ELPGLADQVTRVY 92
Cdd:pfam16739  81 GHDGLAEELEGEY 93
CARD_IPS-1_RIG-I cd08789
Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; ...
 5-86 2.17e-16

Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; Caspase activation and recruitment domains (CARDs) found in IPS-1 (Interferon beta promoter stimulator protein 1) and Retinoic acid Inducible Gene I (RIG-I)-like DEAD box helicases. RIG-I-like helicases and IPS-1 play important roles in the induction of interferons in response to viral infection. They are crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. RIG-I-like helicases, including MDA5 and RIG-I, contain two N-terminal CARD domains and a C-terminal DEAD box RNA helicase domain. They are cytoplasmic RNA helicases that play 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. MDA5 and RIG-I associate 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: 260057  Cd Length: 91  Bit Score: 74.42  E-value: 2.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679   5 EDKTYKYIRDNHSKFC-CVDVLEILPYLS-CLTASDQDRLRASYRQIGNRDTLWGLFNNLQR--RPGWVEVFIRALQICE 80
Cdd:cd08789   1 TDDEKQLLQCYRATVErSLDVVYVLPYLTdCLPDEDRERIRAAEENRGNSGAAALLLNTLLQleKEGWFRGFLDALRATG 80


                ....*.
gi 81170679  81 LPGLAD 86
Cdd:cd08789  81 YTGARE 86
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 12-86 5.30e-06

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: 44.43  E-value: 5.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81170679  12 IRDNHSKFC-CVDVLEILPYL---SCLTASDQDRLRAsyrQIGNRDTLWGLFNNLQRR-PGWVEVFIRALQICELPGLAD 86
Cdd:cd01671   1 LRKNRVELVeDLDVEDILDHLiqkGVLTEEDKEEILS---EKTRQDKARKLLDILPRRgPKAFEVFCEALRETGQPHLAE 77
 
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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