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Conserved domains on  [gi|153792387|ref|NP_001093393|]
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myeloid differentiation primary response protein MyD88 [Sus scrofa]

Protein Classification

toll-like receptor( domain architecture ID 10169774)

toll-like receptor (TLR) is involved in the recognition of microbial pathogens by the innate immune system, which recognize different pathogen-associated molecular patterns

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.25e-33

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: 117.70  E-value: 1.25e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792387  29 VRHRLSLFLNVRTQVAADWTGLAEEMNFEYLEIRRLETHPDPTRSLLDDWQGRP-GASVGRLLELLAKLGRDDVLVELG 106
Cdd:cd08312    1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
TIR smart00255
Toll - interleukin 1 - resistance;
158-293 1.87e-33

Toll - interleukin 1 - resistance;


:

Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 119.35  E-value: 1.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387   158 FDAFICYcPSDTQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKrCRRMVVVVSDDYLQSKECDFQTKFA 237
Cdd:smart00255   2 YDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVAA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792387   238 LSLSPGAHQKRLIPVKYKSMKKEFPSILRFITVCDYTN----PCTKS-WFWTRLARALSLP 293
Cdd:smart00255  80 LENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKNylkwPEDEKeQFWKKALYAVPSK 140
 
Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.25e-33

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: 117.70  E-value: 1.25e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792387  29 VRHRLSLFLNVRTQVAADWTGLAEEMNFEYLEIRRLETHPDPTRSLLDDWQGRP-GASVGRLLELLAKLGRDDVLVELG 106
Cdd:cd08312    1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
TIR smart00255
Toll - interleukin 1 - resistance;
158-293 1.87e-33

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 119.35  E-value: 1.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387   158 FDAFICYcPSDTQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKrCRRMVVVVSDDYLQSKECDFQTKFA 237
Cdd:smart00255   2 YDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVAA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792387   238 LSLSPGAHQKRLIPVKYKSMKKEFPSILRFITVCDYTN----PCTKS-WFWTRLARALSLP 293
Cdd:smart00255  80 LENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKNylkwPEDEKeQFWKKALYAVPSK 140
Death pfam00531
Death domain;
30-105 1.47e-14

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 67.78  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387   30 RHRLSLFLNVRTQVAADWTGLAEEMNFEYLEIRRLETHP----DPTRSLLDDW--QGRPGASVGRLLELLAKLGRDDVLV 103
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESENprlrSQTYELLRLWeqREGKNATVGTLLEALRKLGRRDAAE 80


                  ..
gi 153792387  104 EL 105
Cdd:pfam00531  81 KI 82
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 158-291 8.90e-13

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 65.08  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387  158 FDAFICYCPSDTQ--FVQEMIRQLEQTNYrlKLCVSDRDVLPGTcvwSIASELIE--KRCRRMVVVVSDDYLQSKECDFQ 233
Cdd:pfam01582   1 YDVFLSFRGSDTRewFVSHLLKELKQKGI--KLFIDDRDLEPGE---AIAPELLSaiEKSRRSVVVLSPNYASSGWCLDE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387  234 TKFALSLspgAHQKR--LIPVKYK-----------SMKKEFPSILRFITVC----------------DYTNPCTKSWFWT 284
Cdd:pfam01582  76 LVKILEC---ALDLGqkVIPIFYEvdpsdvrkqtgSFGKAFKKHKKVLTEEkvlkwrgalnevaniwHSKSVSDESKFWK 152


                  ....*..
gi 153792387  285 RLARALS 291
Cdd:pfam01582 153 KIAYDIS 159
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 43-105 1.68e-10

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 56.65  E-value: 1.68e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387    43 VAADWTGLAEEMNFEYLEIRRLET-----HPDPTRSLLDDWQGRPG--ASVGRLLELLAKLGRDDVLVEL 105
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTeaprdLAEQSVQLLRLWEQREGknATLGTLLEALRKMGRDDAVELL 85
 
Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.25e-33

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: 117.70  E-value: 1.25e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792387  29 VRHRLSLFLNVRTQVAADWTGLAEEMNFEYLEIRRLETHPDPTRSLLDDWQGRP-GASVGRLLELLAKLGRDDVLVELG 106
Cdd:cd08312    1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
TIR smart00255
Toll - interleukin 1 - resistance;
158-293 1.87e-33

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 119.35  E-value: 1.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387   158 FDAFICYcPSDTQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKrCRRMVVVVSDDYLQSKECDFQTKFA 237
Cdd:smart00255   2 YDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVAA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792387   238 LSLSPGAHQKRLIPVKYKSMKKEFPSILRFITVCDYTN----PCTKS-WFWTRLARALSLP 293
Cdd:smart00255  80 LENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKNylkwPEDEKeQFWKKALYAVPSK 140
Death pfam00531
Death domain;
30-105 1.47e-14

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 67.78  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387   30 RHRLSLFLNVRTQVAADWTGLAEEMNFEYLEIRRLETHP----DPTRSLLDDW--QGRPGASVGRLLELLAKLGRDDVLV 103
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESENprlrSQTYELLRLWeqREGKNATVGTLLEALRKLGRRDAAE 80


                  ..
gi 153792387  104 EL 105
Cdd:pfam00531  81 KI 82
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 158-291 8.90e-13

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 65.08  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387  158 FDAFICYCPSDTQ--FVQEMIRQLEQTNYrlKLCVSDRDVLPGTcvwSIASELIE--KRCRRMVVVVSDDYLQSKECDFQ 233
Cdd:pfam01582   1 YDVFLSFRGSDTRewFVSHLLKELKQKGI--KLFIDDRDLEPGE---AIAPELLSaiEKSRRSVVVLSPNYASSGWCLDE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387  234 TKFALSLspgAHQKR--LIPVKYK-----------SMKKEFPSILRFITVC----------------DYTNPCTKSWFWT 284
Cdd:pfam01582  76 LVKILEC---ALDLGqkVIPIFYEvdpsdvrkqtgSFGKAFKKHKKVLTEEkvlkwrgalnevaniwHSKSVSDESKFWK 152


                  ....*..
gi 153792387  285 RLARALS 291
Cdd:pfam01582 153 KIAYDIS 159
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 161-254 2.47e-11

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 59.64  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387  161 FICYCPSDTQFVQEMIRQLEQTNYRlklCVSDR-DVLPGTcvwSIASELIE--KRCRRMVVVVSDDYLQSKECDFQTKFA 237
Cdd:pfam13676   2 FISYAGEDRAWAEWLADALEAAGYR---VWLDRwDIRPGD---DWVEEIEEaiENSDRVLVVLSPNYLESPWCRAEWEAA 75

                          90
                  ....*....|....*..
gi 153792387  238 LSLSPGahQKRLIPVKY 254
Cdd:pfam13676  76 LADPEG--RKRLIPVRL 90
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 43-105 1.68e-10

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 56.65  E-value: 1.68e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387    43 VAADWTGLAEEMNFEYLEIRRLET-----HPDPTRSLLDDWQGRPG--ASVGRLLELLAKLGRDDVLVEL 105
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTeaprdLAEQSVQLLRLWEQREGknATLGTLLEALRKMGRDDAVELL 85
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 46-101 2.84e-09

Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. 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: 260025  Cd Length: 80  Bit Score: 53.06  E-value: 2.84e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792387  46 DWTGLAEEMNFEYLEIRRLETHPDPTRSLLDDWQGRPGASVGRLLELLAKLGRDDV 101
Cdd:cd08311   20 DWRALAGELGYSAEEIDSFAREADPCRALLTDWSAQDGATLGVLLTALRKIGRDDI 75
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 36-105 1.41e-07

Death Domain: a protein-protein interaction domain; Death Domains (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. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 48.05  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792387  36 FLNVRTQVAADWTGLAEEMNFEYLEIRRLET-HPDPTRS----LLDDWQGRPG--ASVGRLLELLAKLGRDDVLVEL 105
Cdd:cd01670    2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEdNRDDLKEqayqMLERWREREGdeATLGRLIQALREIGRRDLAEKL 78
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
 25-97 5.00e-05

Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. 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: 260023  Cd Length: 88  Bit Score: 41.18  E-value: 5.00e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792387  25 LNVRVRHRLSLFLNvrTQVAADWTGLAEEMNFEYLEIRRLETHPD----PTRSLLDDWQGRpGASVGRLLELLAKLG 97
Cdd:cd08309    6 LPPWVLKRLCKVLD--ALELAGWRQLASLIPYDQTDVRQIESMKQrgqsPTRELLWDWGTQ-NATVQDLVQLLTQLG 79
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 29-100 5.42e-05

Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. 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: 260024  Cd Length: 72  Bit Score: 40.69  E-value: 5.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792387  29 VRHRLSLFLNVrtqvAADWTGLAEEMNFEYLeIRRLETHPDPTRSLLDDWQGRPGaSVGRLLELLAKLGRDD 100
Cdd:cd08310    1 TRLRLCKLLDV----GKDWRELAELLGLGHL-VESIEQSSSPTKLLLDYYEAQGG-TLEKLREALRALGETD 66
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 25-103 2.59e-03

Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 260051  Cd Length: 83  Bit Score: 36.10  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792387  25 LNVRVRHRLSLFLNVRTQVAADWTGLAEEMNFE-YleIRRLETHPDPTRSLLDDW--QGRPGASVGRLLELLAKLGRDDV 101
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDrY--INYFATKPSPTEVILDLWeaRNRDDGALNSLAAILREMGRHDA 78


                 ..
gi 153792387 102 LV 103
Cdd:cd08781   79 AT 80
Death_IRAK-M cd08796
Death domain of Interleukin 1 Receptor Associated Kinase-M; Death Domain (DD) of Interleukin-1 ...
 47-97 4.57e-03

Death domain of Interleukin 1 Receptor Associated Kinase-M; Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase M (IRAK-M). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors(TLRs), nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK-M, also called IRAK-3, is an inactive kinase present only in macrophages in an inducible manner. It is a negative regulator of TLR signaling and it contributes to the attenuation of NF-kB activation. 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: 260062  Cd Length: 89  Bit Score: 35.61  E-value: 4.57e-03
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                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153792387  47 WTGLAEEMNFEYLEIRRLETHPD----PTRSLLDDWQGRpGASVGRLLELLAKLG 97
Cdd:cd08796   27 WRGLAERISSSWLEVRHIEKYVAqgksPTRELLWSWAQK-NKTVGDLLKVLEDMG 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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