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Conserved domains on  [gi|1498449209|gb|AYO88837|]
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MC160 [Molluscum contagiosum virus subtype 1]

Protein Classification

protein kinase family protein( domain architecture ID 10636843)

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
DED smart00031
Death effector domain;
92-167 5.71e-19

Death effector domain;


:

Pssm-ID: 214477  Cd Length: 79  Bit Score: 80.41  E-value: 5.71e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498449209   92 SQYRLQVAAINNMVGSEDLRVMCLCAGKLLPPSCT-PRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDLSVAL 167
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLeIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRL 77
DED smart00031
Death effector domain;
7-76 1.30e-09

Death effector domain;


:

Pssm-ID: 214477  Cd Length: 79  Bit Score: 54.21  E-value: 1.30e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498449209    7 PFSFLRNLLAE-LDASEHEVLRFLCRDVAP----ASKTAEDALRA---LQRRRLLTLSSMAELLCALRRFDVLKVRFG 76
Cdd:smart00031   2 PYRVLLLLISEeLDSEELEVLLFLCKDLIPkrklEIKTFLDLFSAleeQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
 
Name Accession Description Interval E-value
DED smart00031
Death effector domain;
92-167 5.71e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 80.41  E-value: 5.71e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498449209   92 SQYRLQVAAINNMVGSEDLRVMCLCAGKLLPPSCT-PRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDLSVAL 167
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLeIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRL 77
DED smart00031
Death effector domain;
7-76 1.30e-09

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 54.21  E-value: 1.30e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498449209    7 PFSFLRNLLAE-LDASEHEVLRFLCRDVAP----ASKTAEDALRA---LQRRRLLTLSSMAELLCALRRFDVLKVRFG 76
Cdd:smart00031   2 PYRVLLLLISEeLDSEELEVLLFLCKDLIPkrklEIKTFLDLFSAleeQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 6-80 1.95e-09

Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 1, similar to that found in FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260044  Cd Length: 80  Bit Score: 53.96  E-value: 1.95e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498449209   6 IPFSFLRNLLAELDASEHEVLRFLCRDVAPASKTAE--DALRALQRRRLLTLSSMAELLCALRRFDVLKVRFGMTRE 80
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQlrDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKE 77
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 92-163 1.28e-05

Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260046  Cd Length: 81  Bit Score: 43.11  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498449209  92 SQYRLQVAAINNMVGSEDLR--VMCLCAGKLLPPSCTPRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDL 163
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRslIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDL 74
DED pfam01335
Death effector domain;
94-163 4.59e-04

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 38.62  E-value: 4.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498449209  94 YRLQVAAINNMVGSEDLRVMCLCAGKLLPPS--CTPRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDL 163
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRklEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDL 72
 
Name Accession Description Interval E-value
DED smart00031
Death effector domain;
92-167 5.71e-19

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 80.41  E-value: 5.71e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498449209   92 SQYRLQVAAINNMVGSEDLRVMCLCAGKLLPPSCT-PRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDLSVAL 167
Cdd:smart00031   1 SPYRVLLLLISEELDSEELEVLLFLCKDLIPKRKLeIKTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRL 77
DED smart00031
Death effector domain;
7-76 1.30e-09

Death effector domain;


Pssm-ID: 214477  Cd Length: 79  Bit Score: 54.21  E-value: 1.30e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498449209    7 PFSFLRNLLAE-LDASEHEVLRFLCRDVAP----ASKTAEDALRA---LQRRRLLTLSSMAELLCALRRFDVLKVRFG 76
Cdd:smart00031   2 PYRVLLLLISEeLDSEELEVLLFLCKDLIPkrklEIKTFLDLFSAleeQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79
DED_c-FLIP_r1 cd08337
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 6-80 1.95e-09

Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 1, similar to that found in FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260044  Cd Length: 80  Bit Score: 53.96  E-value: 1.95e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498449209   6 IPFSFLRNLLAELDASEHEVLRFLCRDVAPASKTAE--DALRALQRRRLLTLSSMAELLCALRRFDVLKVRFGMTRE 80
Cdd:cd08337     1 VSAEVLHQVEEELDTDEDEMLLFLCRDAAPDCTTAQlrDALCALNERGKLTLAGLAELLYRVKRFDLLKRILHLSKE 77
DED_c-FLIP_r2 cd08340
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ...
 92-163 1.28e-05

Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260046  Cd Length: 81  Bit Score: 43.11  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498449209  92 SQYRLQVAAINNMVGSEDLR--VMCLCAGKLLPPSCTPRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDL 163
Cdd:cd08340     1 SDYRVLMVCVSEELDKSDLRslIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLLEDCLRNIRRIDL 74
DED_Caspase-like_r1 cd08776
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ...
 10-75 1.18e-04

Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED), first repeat, found in initator caspase-like proteins, like caspase-8 and -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176754  Cd Length: 71  Bit Score: 39.81  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498449209  10 FLRNLLAELDASEHEVLRFLCRDVAPASKTAEDALRALQRRR--LLTLSSMAELLCALRRFDVLKVRF 75
Cdd:cd08776     4 VLCEVAEKLGTDEREVLLFLLNVFIPQPTLAQLIGALRALKEegRLTLPLLAECLYRAGRRDLLRSLL 71
DED pfam01335
Death effector domain;
94-163 4.59e-04

Death effector domain;


Pssm-ID: 460163  Cd Length: 82  Bit Score: 38.62  E-value: 4.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498449209  94 YRLQVAAINNMVGSEDLRVMCLCAGKLLPPS--CTPRCLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDL 163
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRklEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDL 72
DED_Caspase-like_r2 cd08775
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ...
 92-163 2.37e-03

Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED), second repeat, found in initator caspase-like proteins like caspase-8, -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176753  Cd Length: 81  Bit Score: 36.76  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498449209  92 SQYRLQVAAINNMVGSEDLRVMCLCAGKLLPPSCTPR--CLVDLVSALEDVGAISPQDVSVLVTLLHAVCRYDL 163
Cdd:cd08775     1 SAYRVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDdmNFLDIVIEMENRVLLGPGKVDILKRMLRQLRRKDL 74
DED_Caspase_8_r1 cd08333
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ...
 10-80 9.56e-03

Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260041  Cd Length: 82  Bit Score: 35.06  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498449209  10 FLRNLLA---ELDASEHEVLRFLCRDVAPASK--TAEDALRALQR------RRLLTLSSMAELLCALRRFDVLKVRFGMT 78
Cdd:cd08333     1 FRKLLFAiseELDREDLAALKFLSLDHIPRRKqeNIKDALALFLAlqekgmLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80


                  ..
gi 1498449209  79 RE 80
Cdd:cd08333    81 RE 82
 
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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