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Conserved domains on  [gi|589911169]
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Chain A, Probable ATP-dependent RNA helicase DDX58

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARD_RIG-I_r2 cd08817
Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation ...
 103-192 1.19e-43

Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. 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. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates 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: 260076  Cd Length: 91  Bit Score: 141.05  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169 103 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKE- 181
Cdd:cd08817    1 LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPKTLKLALEKCg 80

                         90
                 ....*....|.
gi 589911169 182 RNKFSELWIVE 192
Cdd:cd08817   81 YDAASELWPDE 91
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 5-95 4.81e-39

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 cd08816:

Pssm-ID: 472698  Cd Length: 90  Bit Score: 129.10  E-value: 4.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169   5 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNnKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 84
Cdd:cd08816    1 TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEE-KGVTEAAQLFLDAVLQLEEEGWFQGFLDALLAAG 79

                         90
                 ....*....|.
gi 589911169  85 YSGLYEAIESW 95
Cdd:cd08816   80 YTGLCEAIENW 90
 
Name Accession Description Interval E-value
CARD_RIG-I_r2 cd08817
Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation ...
 103-192 1.19e-43

Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. 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. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates 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: 260076  Cd Length: 91  Bit Score: 141.05  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169 103 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKE- 181
Cdd:cd08817    1 LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPKTLKLALEKCg 80

                         90
                 ....*....|.
gi 589911169 182 RNKFSELWIVE 192
Cdd:cd08817   81 YDAASELWPDE 91
CARD_RIG-I_r1 cd08816
Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and ...
 5-95 4.81e-39

Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), first repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. 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. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates 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: 260075  Cd Length: 90  Bit Score: 129.10  E-value: 4.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169   5 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNnKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 84
Cdd:cd08816    1 TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEE-KGVTEAAQLFLDAVLQLEEEGWFQGFLDALLAAG 79

                         90
                 ....*....|.
gi 589911169  85 YSGLYEAIESW 95
Cdd:cd08816   80 YTGLCEAIENW 90
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 4-96 5.24e-37

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: 123.86  E-value: 5.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169    4 MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHA 83
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKT 80

                          90
                  ....*....|...
gi 589911169   84 GYSGLYEAIESWD 96
Cdd:pfam16739  81 GHDGLAEELEGEY 93
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 102-193 1.93e-28

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: 102.29  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169  102 KLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEK- 180
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKt 80

                          90
                  ....*....|...
gi 589911169  181 ERNKFSELWIVEK 193
Cdd:pfam16739  81 GHDGLAEELEGEY 93
 
Name Accession Description Interval E-value
CARD_RIG-I_r2 cd08817
Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation ...
 103-192 1.19e-43

Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. 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. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates 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: 260076  Cd Length: 91  Bit Score: 141.05  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169 103 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKE- 181
Cdd:cd08817    1 LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPKTLKLALEKCg 80

                         90
                 ....*....|.
gi 589911169 182 RNKFSELWIVE 192
Cdd:cd08817   81 YDAASELWPDE 91
CARD_RIG-I_r1 cd08816
Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and ...
 5-95 4.81e-39

Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), first repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. 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. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates 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: 260075  Cd Length: 90  Bit Score: 129.10  E-value: 4.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169   5 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNnKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 84
Cdd:cd08816    1 TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEE-KGVTEAAQLFLDAVLQLEEEGWFQGFLDALLAAG 79

                         90
                 ....*....|.
gi 589911169  85 YSGLYEAIESW 95
Cdd:cd08816   80 YTGLCEAIENW 90
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 4-96 5.24e-37

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: 123.86  E-value: 5.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169    4 MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHA 83
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKT 80

                          90
                  ....*....|...
gi 589911169   84 GYSGLYEAIESWD 96
Cdd:pfam16739  81 GHDGLAEELEGEY 93
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 102-193 1.93e-28

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: 102.29  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169  102 KLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEK- 180
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKt 80

                          90
                  ....*....|...
gi 589911169  181 ERNKFSELWIVEK 193
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; ...
 5-95 1.43e-19

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: 79.43  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169   5 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 84
Cdd:cd08789    1 TDDEKQLLQCYRATVERSLDVVYVLPYLTDCLPDEDRERIRAAEENRGNSGAAALLLNTLLQLEKEGWFRGFLDALRATG 80

                         90
                 ....*....|.
gi 589911169  85 YSGLYEAIESW 95
Cdd:cd08789   81 YTGARELIDNW 91
CARD_IPS-1_RIG-I cd08789
Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; ...
 103-189 6.40e-17

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: 72.49  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911169 103 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLAL-EKE 181
Cdd:cd08789    1 TDDEKQLLQCYRATVERSLDVVYVLPYLTDCLPDEDRERIRAAEENRGNSGAAALLLNTLLQLEKEGWFRGFLDALrATG 80


                 ....*...
gi 589911169 182 RNKFSELW 189
Cdd:cd08789   81 YTGARELI 88
CARD_IPS1 cd08811
Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and ...
 104-180 7.47e-06

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: 42.73  E-value: 7.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589911169 104 EEYRLLLKRLQPEFKTRIIPTDIISDLSeCLINQECEEILQICSTKGMMAGAEKLVECLLRsdKENWPKTLKLALEK 180
Cdd:cd08811    4 DKEYKYLRRNMGVFCHDIKVSEIIPYLP-CLTRSDRDEILAKKDMSGNRDTAWTLLDHLQR--RPGWVEDFIKALRN 77
CARD_MDA5_r2 cd08819
Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and ...
 36-90 3.88e-04

Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), second repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays 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. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates 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: 260078  Cd Length: 92  Bit Score: 38.08  E-value: 3.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 589911169  36 FREEEVQYIQAEKNNKGPMEAATLFLKFLLElQEEGWFRGFLDALDHAGYSGLYE 90
Cdd:cd08819   33 LTAEDRERILAATENHGNRSGARELLSRIVR-QKEGWFSKFLQALRETEHNNLAE 86
CARD_MDA5_r1 cd08818
Caspase activation and recruitment domain found in MDA5, first repeat; Caspase activation and ...
 39-84 8.69e-03

Caspase activation and recruitment domain found in MDA5, first repeat; Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), first repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays 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. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates 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: 260077  Cd Length: 92  Bit Score: 34.20  E-value: 8.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 589911169  39 EEVQYIQAEKNNKGPMEAATLFLKFLLE-LQEEGWFRGFLDALDHAG 84
Cdd:cd08818   34 EQKERIRQKARTEGNLAAADLLIDAVEKgPHPPGWFREFVDALEQGG 80
 
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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