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Conserved domains on  [gi|1983575963|ref|NP_001380416|]
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interleukin-18 receptor accessory protein isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 36-165 5.16e-77

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


:

Pssm-ID: 465773  Cd Length: 128  Bit Score: 240.01  E-value: 5.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963  36 TRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPeHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLT 115
Cdd:pfam18452   1 ARSEEEFVLFCDLPEPQKTHFYHRSQLSPTQGP-HLPCSGSKDLSDVQWYWQPKNGDPLEAITESSPHIIQEGNALWFLP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1983575963 116 PGVNNSGSYICRPkMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDL 165
Cdd:pfam18452  80 VGVNDSGSYICRP-RIRSPQDEACCLKIILEVQPKTNASCSGSVTNELYL 128
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 419-559 8.07e-37

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: 134.80  E-value: 8.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 419 SFPSeATSSLSEEHLALSLFPDVleNKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGP-SIFELQAA 497
Cdd:pfam01582   3 VFLS-FRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGwCLDELVKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 498 VNLALdDQTLKLILIKFCYFQEPE-----SLPHLVKKALRVL---PTVTWRGL----------KSVPPNSRFWAKMRYHM 559
Cdd:pfam01582  80 LECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGAlnevaniwhsKSVSDESKFWKKIAYDI 158
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 251-354 7.63e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20931:

Pssm-ID: 472250  Cd Length: 107  Bit Score: 53.49  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 251 PDILDPVEDTL-EVELGKPLTISCKARFGFERVFNPVIKWYI---KDSDLEWEVSVPEAKSIKSTlKDEIIERNIILEKV 326
Cdd:cd20931     1 PQIYSPNDRVVyEKEPGEELLIPCTVYFSFLMDSRNEVWWTIdgkKPDDVTIDVTINESISYSST-EDETRTQILSIKKV 79

                          90       100
                  ....*....|....*....|....*...
gi 1983575963 327 TQRDLRRKFVCFVQNSIGNTTQSVQLKE 354
Cdd:cd20931    80 TPEDLKRNYVCHARNAKGEVEKAAKVKQ 107
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 162-221 1.11e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20994:

Pssm-ID: 472250  Cd Length: 94  Bit Score: 41.30  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575963 162 KQDLLLGSTGSISCPSLSC--QSDAQSPAVTWYKNGKLLSVERS------NRIVVDEVYDYHQGTYVC 221
Cdd:cd20994     4 KQKVPFTSGGRIVCPHLDFfkDENNNLPKVQWYKDCKPLLLDDKrfagleSDLLIFNVTVQDQGNYTC 71
 
Name Accession Description Interval E-value
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 36-165 5.16e-77

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 240.01  E-value: 5.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963  36 TRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPeHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLT 115
Cdd:pfam18452   1 ARSEEEFVLFCDLPEPQKTHFYHRSQLSPTQGP-HLPCSGSKDLSDVQWYWQPKNGDPLEAITESSPHIIQEGNALWFLP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1983575963 116 PGVNNSGSYICRPkMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDL 165
Cdd:pfam18452  80 VGVNDSGSYICRP-RIRSPQDEACCLKIILEVQPKTNASCSGSVTNELYL 128
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 419-559 8.07e-37

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: 134.80  E-value: 8.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 419 SFPSeATSSLSEEHLALSLFPDVleNKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGP-SIFELQAA 497
Cdd:pfam01582   3 VFLS-FRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGwCLDELVKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 498 VNLALdDQTLKLILIKFCYFQEPE-----SLPHLVKKALRVL---PTVTWRGL----------KSVPPNSRFWAKMRYHM 559
Cdd:pfam01582  80 LECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGAlnevaniwhsKSVSDESKFWKKIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
408-562 1.25e-23

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 97.01  E-value: 1.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963  408 FDAFVSYAKWssfpseatsslseEHLALSLFPDVLENKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVN 487
Cdd:smart00255   2 YDVFISYSGK-------------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAE 68

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1983575963  488 GP-SIFELQAAVNLALDDQTLKLILIKFCYF-QEPESLPHLVKKALRVlPTVTWRGLKSVppnsRFWAKMRYHMPVK 562
Cdd:smart00255  69 SEwCLDELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKK-NYLKWPEDEKE----QFWKKALYAVPSK 140
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
 251-354 7.63e-09

Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members here are composed of the third immunoglobulin Ig interleukin-1 receptor accessory protein (IL1RAP). The interleukin 1 receptor accessory protein (IL-1RAP), also known as IL-1R3, is a coreceptor of type 1 interleukin 1 receptor (IL-1R1) and is required for transmission of IL-1 signaling. The activated IL-1 receptor complex, which consists of IL-1R1 and IL-1RAP, induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective Toll/IL-1 receptor (TIR) domains of the receptor/coreceptor subunits. Moreover, IL1RAP is known to be the accessory co-receptor that activates signal transduction upon IL-36 binding to IL-36R. IL-36 cytokines, which are a subfamily of the IL-1 superfamily, bind to the IL-36 receptor (IL-36R) and use IL1RAP as a co-receptor.


Pssm-ID: 409525  Cd Length: 107  Bit Score: 53.49  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 251 PDILDPVEDTL-EVELGKPLTISCKARFGFERVFNPVIKWYI---KDSDLEWEVSVPEAKSIKSTlKDEIIERNIILEKV 326
Cdd:cd20931     1 PQIYSPNDRVVyEKEPGEELLIPCTVYFSFLMDSRNEVWWTIdgkKPDDVTIDVTINESISYSST-EDETRTQILSIKKV 79

                          90       100
                  ....*....|....*....|....*...
gi 1983575963 327 TQRDLRRKFVCFVQNSIGNTTQSVQLKE 354
Cdd:cd20931    80 TPEDLKRNYVCHARNAKGEVEKAAKVKQ 107
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 162-221 1.11e-04

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 41.30  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575963 162 KQDLLLGSTGSISCPSLSC--QSDAQSPAVTWYKNGKLLSVERS------NRIVVDEVYDYHQGTYVC 221
Cdd:cd20994     4 KQKVPFTSGGRIVCPHLDFfkDENNNLPKVQWYKDCKPLLLDDKrfagleSDLLIFNVTVQDQGNYTC 71
 
Name Accession Description Interval E-value
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 36-165 5.16e-77

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 240.01  E-value: 5.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963  36 TRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPeHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLT 115
Cdd:pfam18452   1 ARSEEEFVLFCDLPEPQKTHFYHRSQLSPTQGP-HLPCSGSKDLSDVQWYWQPKNGDPLEAITESSPHIIQEGNALWFLP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1983575963 116 PGVNNSGSYICRPkMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDL 165
Cdd:pfam18452  80 VGVNDSGSYICRP-RIRSPQDEACCLKIILEVQPKTNASCSGSVTNELYL 128
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 419-559 8.07e-37

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: 134.80  E-value: 8.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 419 SFPSeATSSLSEEHLALSLFPDVleNKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGP-SIFELQAA 497
Cdd:pfam01582   3 VFLS-FRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGwCLDELVKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 498 VNLALdDQTLKLILIKFCYFQEPE-----SLPHLVKKALRVL---PTVTWRGL----------KSVPPNSRFWAKMRYHM 559
Cdd:pfam01582  80 LECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGAlnevaniwhsKSVSDESKFWKKIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
408-562 1.25e-23

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 97.01  E-value: 1.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963  408 FDAFVSYAKWssfpseatsslseEHLALSLFPDVLENKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVN 487
Cdd:smart00255   2 YDVFISYSGK-------------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAE 68

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1983575963  488 GP-SIFELQAAVNLALDDQTLKLILIKFCYF-QEPESLPHLVKKALRVlPTVTWRGLKSVppnsRFWAKMRYHMPVK 562
Cdd:smart00255  69 SEwCLDELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKK-NYLKWPEDEKE----QFWKKALYAVPSK 140
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
 251-354 7.63e-09

Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members here are composed of the third immunoglobulin Ig interleukin-1 receptor accessory protein (IL1RAP). The interleukin 1 receptor accessory protein (IL-1RAP), also known as IL-1R3, is a coreceptor of type 1 interleukin 1 receptor (IL-1R1) and is required for transmission of IL-1 signaling. The activated IL-1 receptor complex, which consists of IL-1R1 and IL-1RAP, induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective Toll/IL-1 receptor (TIR) domains of the receptor/coreceptor subunits. Moreover, IL1RAP is known to be the accessory co-receptor that activates signal transduction upon IL-36 binding to IL-36R. IL-36 cytokines, which are a subfamily of the IL-1 superfamily, bind to the IL-36 receptor (IL-36R) and use IL1RAP as a co-receptor.


Pssm-ID: 409525  Cd Length: 107  Bit Score: 53.49  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 251 PDILDPVEDTL-EVELGKPLTISCKARFGFERVFNPVIKWYI---KDSDLEWEVSVPEAKSIKSTlKDEIIERNIILEKV 326
Cdd:cd20931     1 PQIYSPNDRVVyEKEPGEELLIPCTVYFSFLMDSRNEVWWTIdgkKPDDVTIDVTINESISYSST-EDETRTQILSIKKV 79

                          90       100
                  ....*....|....*....|....*...
gi 1983575963 327 TQRDLRRKFVCFVQNSIGNTTQSVQLKE 354
Cdd:cd20931    80 TPEDLKRNYVCHARNAKGEVEKAAKVKQ 107
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 440-507 1.29e-05

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 44.61  E-value: 1.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1983575963 440 DVLENKyGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGPS-IFELQAAVNLALDDQTL 507
Cdd:pfam13676  18 DALEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNYLESPWcRAEWEAALADPEGRKRL 85
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 162-221 1.11e-04

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 41.30  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575963 162 KQDLLLGSTGSISCPSLSC--QSDAQSPAVTWYKNGKLLSVERS------NRIVVDEVYDYHQGTYVC 221
Cdd:cd20994     4 KQKVPFTSGGRIVCPHLDFfkDENNNLPKVQWYKDCKPLLLDDKrfagleSDLLIFNVTVQDQGNYTC 71
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 251-352 8.58e-04

Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.


Pssm-ID: 409526  Cd Length: 104  Bit Score: 39.18  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575963 251 PDILDPVEDTLEVELGKPLTISCKArfgfERVFNPVIKWYIKDSDLEWE----------VSVPEAKSiKSTLkdeIIERN 320
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNV----TGQLSDLAYWKWNGSEIDEDdpvlgedyysVENPANKR-KSTL---ITVLN 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1983575963 321 IilEKVTQRDLRRKFVCFVQNSIGNTTQSVQL 352
Cdd:cd20932    73 I--SEIESRFYKHPFTCFAKNTHGLDAAYVQL 102
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 162-221 2.40e-03

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 37.30  E-value: 2.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575963 162 KQDLLLGSTGSISCPSLSCQSDA-QSPAVTWYKNGKLLSVE-----RSNRIVVDEVYDYHQGTYVC 221
Cdd:cd05757     4 KQKLPITKGGKITCPDLDDYKNEnVLPPIQWYKDCKPLQGDkrfipKGSKLLIQNVTEEDAGNYTC 69
IgI_VEGFR-3 cd05863
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); ...
 186-219 6.08e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-3 (Flt-4) binds two members of the VEGF family (VEGF-C and VEGF-D) and is involved in tumor angiogenesis and growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409449  Cd Length: 88  Bit Score: 36.45  E-value: 6.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1983575963 186 SPAVTWYKNGKLLSVERS-NRIVVDEVYDYHQGTY 219
Cdd:cd05863    33 PPEFQWYKDGKLISGKHSpHSLQIKDVTEASAGTY 67
 
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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