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Conserved domains on  [gi|19921906|ref|NP_610479|]
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Myd88, isoform A [Drosophila melanogaster]

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) ...
 90-172 1.74e-12

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 cd08312:

Pssm-ID: 472698  Cd Length: 79  Bit Score: 63.00  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906  90 TRTQLSRMLNRKKVlrseegYQRDWRGISELAkqkGF------VDENANNPMDLVLISWSQRSPQtAKVGHLEHFLGIID 163
Cdd:cd08312   1 VRKKLSLYLNPEKV------VANDWRGLAELM---GFdyleirNFERQSSPTERLLEDWETRPPG-ATVGNLLEILEELE 70


                ....*....
gi 19921906 164 RWDVCDDIQ 172
Cdd:cd08312  71 RKDVLEDLQ 79
SEFIR super family cl23749
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 242-375 2.53e-07

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


The actual alignment was detected with superfamily member smart00255:

Pssm-ID: 474043 [Multi-domain]  Cd Length: 140  Bit Score: 50.01  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906    242 RYNACVLYAEADiDHATEIMNNLES--ERYNLRLFlrHRDMLMGVPFEHVQLSHFMATRcnHLIVVLTEEFLRSPENTYL 319
Cdd:smart00255   1 EYDVFISYSGKE-DVRNEFLSHLLEklRGYGLCVF--IDDFEPGGGDLEEIDEAIEKSR--IAIVVLSPNYAESEWCLDE 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921906    320 VNFTQKIQIENHTRKIIPILYKTD----MHIPQTLGIYTHIKYAG--DSKLFNFWDKLARSL 375
Cdd:smart00255  76 LVAALENALEEGGLRVIPIFYEVIpsdvRKQPGKFRKVFKKNYLKwpEDEKEQFWKKALYAV 137
 
Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 90-172 1.74e-12

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260026  Cd Length: 79  Bit Score: 63.00  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906  90 TRTQLSRMLNRKKVlrseegYQRDWRGISELAkqkGF------VDENANNPMDLVLISWSQRSPQtAKVGHLEHFLGIID 163
Cdd:cd08312   1 VRKKLSLYLNPEKV------VANDWRGLAELM---GFdyleirNFERQSSPTERLLEDWETRPPG-ATVGNLLEILEELE 70


                ....*....
gi 19921906 164 RWDVCDDIQ 172
Cdd:cd08312  71 RKDVLEDLQ 79
TIR smart00255
Toll - interleukin 1 - resistance;
242-375 2.53e-07

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 50.01  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906    242 RYNACVLYAEADiDHATEIMNNLES--ERYNLRLFlrHRDMLMGVPFEHVQLSHFMATRcnHLIVVLTEEFLRSPENTYL 319
Cdd:smart00255   1 EYDVFISYSGKE-DVRNEFLSHLLEklRGYGLCVF--IDDFEPGGGDLEEIDEAIEKSR--IAIVVLSPNYAESEWCLDE 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921906    320 VNFTQKIQIENHTRKIIPILYKTD----MHIPQTLGIYTHIKYAG--DSKLFNFWDKLARSL 375
Cdd:smart00255  76 LVAALENALEEGGLRVIPIFYEVIpsdvRKQPGKFRKVFKKNYLKwpEDEKEQFWKKALYAV 137
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 249-367 8.71e-06

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 45.00  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906   249 YAEADIDHATEIMNNLEseRYNLRLFLRHRDMLMGVPFEHvqlshFMAT---RCNHLIVVLTEEFLRSPENTYLVNFTQK 325
Cdd:pfam13676   5 YAGEDRAWAEWLADALE--AAGYRVWLDRWDIRPGDDWVE-----EIEEaieNSDRVLVVLSPNYLESPWCRAEWEAALA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 19921906   326 IQIENhtRKIIPILYKTDMHIPQtLGIYTHIKYAGDSKLFNF 367
Cdd:pfam13676  78 DPEGR--KRLIPVRLECDLELPG-LAGLQYIDLRDGDEFDAF 116
 
Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 90-172 1.74e-12

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260026  Cd Length: 79  Bit Score: 63.00  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906  90 TRTQLSRMLNRKKVlrseegYQRDWRGISELAkqkGF------VDENANNPMDLVLISWSQRSPQtAKVGHLEHFLGIID 163
Cdd:cd08312   1 VRKKLSLYLNPEKV------VANDWRGLAELM---GFdyleirNFERQSSPTERLLEDWETRPPG-ATVGNLLEILEELE 70


                ....*....
gi 19921906 164 RWDVCDDIQ 172
Cdd:cd08312  71 RKDVLEDLQ 79
TIR smart00255
Toll - interleukin 1 - resistance;
242-375 2.53e-07

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 50.01  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906    242 RYNACVLYAEADiDHATEIMNNLES--ERYNLRLFlrHRDMLMGVPFEHVQLSHFMATRcnHLIVVLTEEFLRSPENTYL 319
Cdd:smart00255   1 EYDVFISYSGKE-DVRNEFLSHLLEklRGYGLCVF--IDDFEPGGGDLEEIDEAIEKSR--IAIVVLSPNYAESEWCLDE 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921906    320 VNFTQKIQIENHTRKIIPILYKTD----MHIPQTLGIYTHIKYAG--DSKLFNFWDKLARSL 375
Cdd:smart00255  76 LVAALENALEEGGLRVIPIFYEVIpsdvRKQPGKFRKVFKKNYLKwpEDEKEQFWKKALYAV 137
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 249-367 8.71e-06

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 45.00  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921906   249 YAEADIDHATEIMNNLEseRYNLRLFLRHRDMLMGVPFEHvqlshFMAT---RCNHLIVVLTEEFLRSPENTYLVNFTQK 325
Cdd:pfam13676   5 YAGEDRAWAEWLADALE--AAGYRVWLDRWDIRPGDDWVE-----EIEEaieNSDRVLVVLSPNYLESPWCRAEWEAALA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 19921906   326 IQIENhtRKIIPILYKTDMHIPQtLGIYTHIKYAGDSKLFNF 367
Cdd:pfam13676  78 DPEGR--KRLIPVRLECDLELPG-LAGLQYIDLRDGDEFDAF 116
 
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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