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Conserved domains on  [gi|2462578113|ref|XP_054200331|]
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interleukin-1 receptor-like 2 isoform X9 [Homo sapiens]

Protein Classification

toll/interleukin-1 receptor domain-containing protein( domain architecture ID 10481568)

toll/interleukin-1 receptor (TIR) domain-containing protein adopts a flavodoxin fold and may play a role in signal transduction as a phosphorylation-independent conformational switch protein

CATH:  3.40.50.10140
Gene Ontology:  GO:0007165|GO:0005515
PubMed:  34868065
SCOP:  4003648

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
80-230 1.07e-40

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: 138.65  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113  80 YVLYPKPHkesQRHAVDALVLNILPEVleRQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGllKNL 159
Cdd:pfam01582   1 YDVFLSFR---GSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113 160 SEEQIAVYSALiQDGMKVILIELEKIEDYT-----VMPESIQYIKQKH---GAIRWHGDFTE-------QSQCMKTKFWK 224
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152

                  ....*.
gi 2462578113 225 TVRYHM 230
Cdd:pfam01582 153 KIAYDI 158
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
80-230 1.07e-40

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: 138.65  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113  80 YVLYPKPHkesQRHAVDALVLNILPEVleRQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGllKNL 159
Cdd:pfam01582   1 YDVFLSFR---GSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113 160 SEEQIAVYSALiQDGMKVILIELEKIEDYT-----VMPESIQYIKQKH---GAIRWHGDFTE-------QSQCMKTKFWK 224
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152

                  ....*.
gi 2462578113 225 TVRYHM 230
Cdd:pfam01582 153 KIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
77-230 2.51e-28

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 105.87  E-value: 2.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113   77 YDAYVLYPKPhkesqrhavDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLL 156
Cdd:smart00255   2 YDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEWC 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578113  157 KNlsEEQIAVYSALIQDGMKVILIELEKI-EDYTVMPESIQYIKQKHgAIRWHGDFTEQsqcmktkFWKTVRYHM 230
Cdd:smart00255  73 LD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDEKEQ-------FWKKALYAV 137
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
80-230 1.07e-40

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: 138.65  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113  80 YVLYPKPHkesQRHAVDALVLNILPEVleRQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGllKNL 159
Cdd:pfam01582   1 YDVFLSFR---GSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113 160 SEEQIAVYSALiQDGMKVILIELEKIEDYT-----VMPESIQYIKQKH---GAIRWHGDFTE-------QSQCMKTKFWK 224
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152

                  ....*.
gi 2462578113 225 TVRYHM 230
Cdd:pfam01582 153 KIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
77-230 2.51e-28

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 105.87  E-value: 2.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578113   77 YDAYVLYPKPhkesqrhavDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLL 156
Cdd:smart00255   2 YDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEWC 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578113  157 KNlsEEQIAVYSALIQDGMKVILIELEKI-EDYTVMPESIQYIKQKHgAIRWHGDFTEQsqcmktkFWKTVRYHM 230
Cdd:smart00255  73 LD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDEKEQ-------FWKKALYAV 137
 
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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