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Conserved domains on  [gi|268607708|ref|NP_001161312|]
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interleukin-1 receptor accessory protein isoform b precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
243-349 6.93e-78

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: 243.78  E-value: 6.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 243 PHIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEIWWTIDGKKPDDVPVDITINESVSYSSTEDETRTQILSIKKVT 322
Cdd:cd20931    1 PQIYSPNDRVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTEDETRTQILSIKKVT 80
                         90       100
                 ....*....|....*....|....*..
gi 268607708 323 PEDLKRNYVCHARNAEGEAEQAAKVKQ 349
Cdd:cd20931   81 PEDLKRNYVCHARNAKGEVEKAAKVKQ 107
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
25-132 3.06e-73

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first 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.


:

Pssm-ID: 409584  Cd Length: 108  Bit Score: 231.74  E-value: 3.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  25 DDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPT 104
Cdd:cd20992    1 DDWGLDTMRQIQVFEGEPARIKCPLFEHFLKYNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPDNRISKEKDVLWFRPT 80
                         90       100
                 ....*....|....*....|....*...
gi 268607708 105 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 132
Cdd:cd20992   81 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 108
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
143-235 1.45e-41

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 cd20993:

Pssm-ID: 472250  Cd Length: 93  Bit Score: 146.20  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 143 RLPVHRLYIEQGIHNITCPNVDGYFPSSVKPSVTWYKGCTEIVNFHNVQPKGMNLSFFIPLVSNNGNYTCVVTYLENGRL 222
Cdd:cd20993    1 KPTPVIAYIEYGGRTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYETKGRT 80
                         90
                 ....*....|...
gi 268607708 223 FHLTRTMTVKVVG 235
Cdd:cd20993   81 IKLTRTVNVKVVG 93
TIR smart00255
Toll - interleukin 1 - resistance;
404-547 7.70e-22

Toll - interleukin 1 - resistance;


:

Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 92.00  E-value: 7.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   404 EYDIYVSYARNaeeEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVtEKSISMLEF 483
Cdd:smart00255   1 EYDVFISYSGK---EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYA-ESEWCLDEL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607708   484 KLGVMCQNSI-ATKLIVVEYRPLEQPhpgIMQLKESVSFVS------WKGEKSKhsgsKFWKALRLALPLR 547
Cdd:smart00255  77 VAALENALEEgGLRVIPIFYEVIPSD---VRKQPGKFRKVFkknylkWPEDEKE----QFWKKALYAVPSK 140
 
Name Accession Description Interval E-value
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
243-349 6.93e-78

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: 243.78  E-value: 6.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 243 PHIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEIWWTIDGKKPDDVPVDITINESVSYSSTEDETRTQILSIKKVT 322
Cdd:cd20931    1 PQIYSPNDRVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTEDETRTQILSIKKVT 80
                         90       100
                 ....*....|....*....|....*..
gi 268607708 323 PEDLKRNYVCHARNAEGEAEQAAKVKQ 349
Cdd:cd20931   81 PEDLKRNYVCHARNAKGEVEKAAKVKQ 107
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
25-132 3.06e-73

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first 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.


Pssm-ID: 409584  Cd Length: 108  Bit Score: 231.74  E-value: 3.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  25 DDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPT 104
Cdd:cd20992    1 DDWGLDTMRQIQVFEGEPARIKCPLFEHFLKYNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPDNRISKEKDVLWFRPT 80
                         90       100
                 ....*....|....*....|....*...
gi 268607708 105 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 132
Cdd:cd20992   81 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 108
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
143-235 1.45e-41

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: 409585  Cd Length: 93  Bit Score: 146.20  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 143 RLPVHRLYIEQGIHNITCPNVDGYFPSSVKPSVTWYKGCTEIVNFHNVQPKGMNLSFFIPLVSNNGNYTCVVTYLENGRL 222
Cdd:cd20993    1 KPTPVIAYIEYGGRTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYETKGRT 80
                         90
                 ....*....|...
gi 268607708 223 FHLTRTMTVKVVG 235
Cdd:cd20993   81 IKLTRTVNVKVVG 93
TIR smart00255
Toll - interleukin 1 - resistance;
404-547 7.70e-22

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 92.00  E-value: 7.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   404 EYDIYVSYARNaeeEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVtEKSISMLEF 483
Cdd:smart00255   1 EYDVFISYSGK---EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYA-ESEWCLDEL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607708   484 KLGVMCQNSI-ATKLIVVEYRPLEQPhpgIMQLKESVSFVS------WKGEKSKhsgsKFWKALRLALPLR 547
Cdd:smart00255  77 VAALENALEEgGLRVIPIFYEVIPSD---VRKQPGKFRKVFkknylkWPEDEKE----QFWKKALYAVPSK 140
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
405-541 1.60e-21

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: 92.04  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  405 YDIYVSYARNAEEEEFVLLTLRGVleNEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVTEKSiSMLEFK 484
Cdd:pfam01582   1 YDVFLSFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGW-CLDELV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607708  485 LGVMCQNSIATKLIVVEYRPLEQPHPGI-----MQLKESVSF------VSWKGE----------KSKHSGSKFWKALR 541
Cdd:pfam01582  78 KILECALDLGQKVIPIFYEVDPSDVRKQtgsfgKAFKKHKKVlteekvLKWRGAlnevaniwhsKSVSDESKFWKKIA 155
PHA02785 PHA02785
IL-beta-binding protein; Provisional
3-334 2.20e-13

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 71.59  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   3 LPWCLMSLFF-CGILQSHASERCDDWGLdTMRQIQVFEDEPARIKCPlfehflKYNYSTAHSSGLTLIWYWTRQDRDLEE 81
Cdd:PHA02785   4 LPVIFLPIFFySSFVQTFNAPECIDKGQ-YFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRII 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  82 PINfrlpenrisKEKDVLWFRPTLlNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMRLPvhRLYIEQGIHNITCP 161
Cdd:PHA02785  77 PID---------NGSNMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYP--QIVNERSTGEMVCP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 162 NVDGYFPSSVKPSVTWyKGCTEIVNFHNVQ-PKGMnlsFFIPLVSNN--GNYTCVVTYLENGRLFHLTRTMTVKVvgspK 238
Cdd:PHA02785 145 NINAFIASNVNADIIW-SGHRRLRNKRLKQrTPGI---ITIEDVRKNdaGYYTCVLKYIYGDKTYNVTRIVKLEV----R 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 239 D-AVPPHIYSPNDRVVyekEPGEELVIPCKVYFSfIMDSHNEIWWTIDGK--KPDDVPVD--ITINESVsYSSTEDETRT 313
Cdd:PHA02785 217 DrIIPPTMQLPEGVVT---SIGSNLTIACRVSLR-PPTTDADVFWISNGMyyEEDDEDGDgrISVANKI-YTTDKRRVIT 291
                        330       340
                 ....*....|....*....|.
gi 268607708 314 QILSIKKVTPEDlKRNYVCHA 334
Cdd:PHA02785 292 SRLNINPVKEED-ATTFTCMA 311
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
157-233 1.35e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 49.32  E-value: 1.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607708  157 NITCPnvdgyFPSSVKPSVTWYKGCTEIvnfhnvqPKGMNLSFFIPLVSNNGNYTCVVTyleNGRLFHLTRTMTVKV 233
Cdd:pfam13895  18 TLTCS-----APGNPPPSYTWYKDGSAI-------SSSPNFFTLSVSAEDSGTYTCVAR---NGRGGKVSNPVELTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
253-348 4.89e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 4.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   253 VYEKEPGEELVIPCKVYFSfimdSHNEIWWTIDGKKPDDVPVDITINESvsysstedeTRTQILSIKKVTPEDlKRNYVC 332
Cdd:smart00410   3 SVTVKEGESVTLSCEASGS----PPPEVTWYKQGGKLLAESGRFSVSRS---------GSTSTLTISNVTPED-SGTYTC 68
                           90
                   ....*....|....*.
gi 268607708   333 HARNAEGEAEQAAKVK 348
Cdd:smart00410  69 AATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
242-336 1.91e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  242 PPHIYSPNDRVVYEkePGEELVIPCKVYFSfimdSHNEIWWTIDGKKPDDVPvditinesvsYSSTEDETRTQILSIKKV 321
Cdd:pfam13927   1 KPVITVSPSSVTVR--EGETVTLTCEATGS----PPPTITWYKNGEPISSGS----------TRSRSLSGSNSTLTISNV 64
                          90
                  ....*....|....*
gi 268607708  322 TPEDlKRNYVCHARN 336
Cdd:pfam13927  65 TRSD-AGTYTCVASN 78
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
70-140 5.40e-06

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: 46.26  E-value: 5.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607708   70 WYWTRQDRDLEEPINFRLPEnrISKEKDVLWFRPTLLNDTGNYTCMLRNTTY-----CSKVAfpLEVVQKD--SCFNS 140
Cdd:pfam18452  48 WYWQPKNGDPLEAITESSPH--IIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKII--LEVQPKTnaSCSGS 121
 
Name Accession Description Interval E-value
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
243-349 6.93e-78

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: 243.78  E-value: 6.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 243 PHIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEIWWTIDGKKPDDVPVDITINESVSYSSTEDETRTQILSIKKVT 322
Cdd:cd20931    1 PQIYSPNDRVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTEDETRTQILSIKKVT 80
                         90       100
                 ....*....|....*....|....*..
gi 268607708 323 PEDLKRNYVCHARNAEGEAEQAAKVKQ 349
Cdd:cd20931   81 PEDLKRNYVCHARNAKGEVEKAAKVKQ 107
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
25-132 3.06e-73

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first 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.


Pssm-ID: 409584  Cd Length: 108  Bit Score: 231.74  E-value: 3.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  25 DDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPT 104
Cdd:cd20992    1 DDWGLDTMRQIQVFEGEPARIKCPLFEHFLKYNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPDNRISKEKDVLWFRPT 80
                         90       100
                 ....*....|....*....|....*...
gi 268607708 105 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 132
Cdd:cd20992   81 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 108
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
25-132 3.22e-44

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first 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.


Pssm-ID: 409414  Cd Length: 96  Bit Score: 153.35  E-value: 3.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  25 DDWGLDtMRQIQVFEDEPARIKCPLFEHFLkynystAHSSGLTLIWYWTrqdrDLEEPINFRlPENRISKEKDVLWFRPT 104
Cdd:cd05756    1 DEWGED-IKILVVLEGEPDVIKCPLFPNFL------AQSAGLNLTWYKN----DSETPISFE-PDSRIHQEKDKLWFVPA 68
                         90       100
                 ....*....|....*....|....*...
gi 268607708 105 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 132
Cdd:cd05756   69 LLEDSGNYYCVVRNSTYCSKVSISLEVV 96
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
143-235 1.45e-41

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: 409585  Cd Length: 93  Bit Score: 146.20  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 143 RLPVHRLYIEQGIHNITCPNVDGYFPSSVKPSVTWYKGCTEIVNFHNVQPKGMNLSFFIPLVSNNGNYTCVVTYLENGRL 222
Cdd:cd20993    1 KPTPVIAYIEYGGRTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYETKGRT 80
                         90
                 ....*....|...
gi 268607708 223 FHLTRTMTVKVVG 235
Cdd:cd20993   81 IKLTRTVNVKVVG 93
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
26-131 1.98e-32

First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1). 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. IL1RAPL is encoded by a gene on the X-chromosome, this gene is wholly or partially deleted in multiple cases of non-syndromic intellectual disability. This group also contains IL1RAPL-2 which is also encoded by a gene on the X-chromosome and is a candidate for another non-syndromic intellectual disability loci.


Pssm-ID: 409477  Cd Length: 105  Bit Score: 120.82  E-value: 1.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  26 DWGLDtMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFrlPENRISKEKDVLWFRPTL 105
Cdd:cd05896    2 DWSVD-LKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGPGDFEEPIIF--DGVRMSKEEDSIWFRPAE 78
                         90       100
                 ....*....|....*....|....*.
gi 268607708 106 LNDTGNYTCMLRNTTYCSKVAFPLEV 131
Cdd:cd05896   79 LQDSGLYTCVLRNSTYCMKVSMSLTV 104
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
158-235 1.30e-24

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: 98.17  E-value: 1.30e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607708 158 ITCPNVDGYFPSSVKPSVTWYKGCTEIVNFHNVQPKGMNLSFFIPLVSNNGNYTCVVTYLENGRLFHLTRTMTVKVVG 235
Cdd:cd05757   15 ITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYNVTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
404-547 7.70e-22

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 92.00  E-value: 7.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   404 EYDIYVSYARNaeeEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVtEKSISMLEF 483
Cdd:smart00255   1 EYDVFISYSGK---EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYA-ESEWCLDEL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268607708   484 KLGVMCQNSI-ATKLIVVEYRPLEQPhpgIMQLKESVSFVS------WKGEKSKhsgsKFWKALRLALPLR 547
Cdd:smart00255  77 VAALENALEEgGLRVIPIFYEVIPSD---VRKQPGKFRKVFkknylkWPEDEKE----QFWKKALYAVPSK 140
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
405-541 1.60e-21

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: 92.04  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  405 YDIYVSYARNAEEEEFVLLTLRGVleNEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVTEKSiSMLEFK 484
Cdd:pfam01582   1 YDVFLSFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGW-CLDELV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607708  485 LGVMCQNSIATKLIVVEYRPLEQPHPGI-----MQLKESVSF------VSWKGE----------KSKHSGSKFWKALR 541
Cdd:pfam01582  78 KILECALDLGQKVIPIFYEVDPSDVRKQtgsfgKAFKKHKKVlteekvLKWRGAlnevaniwhsKSVSDESKFWKKIA 155
PHA02785 PHA02785
IL-beta-binding protein; Provisional
3-334 2.20e-13

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 71.59  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   3 LPWCLMSLFF-CGILQSHASERCDDWGLdTMRQIQVFEDEPARIKCPlfehflKYNYSTAHSSGLTLIWYWTRQDRDLEE 81
Cdd:PHA02785   4 LPVIFLPIFFySSFVQTFNAPECIDKGQ-YFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRII 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  82 PINfrlpenrisKEKDVLWFRPTLlNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMRLPvhRLYIEQGIHNITCP 161
Cdd:PHA02785  77 PID---------NGSNMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYP--QIVNERSTGEMVCP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 162 NVDGYFPSSVKPSVTWyKGCTEIVNFHNVQ-PKGMnlsFFIPLVSNN--GNYTCVVTYLENGRLFHLTRTMTVKVvgspK 238
Cdd:PHA02785 145 NINAFIASNVNADIIW-SGHRRLRNKRLKQrTPGI---ITIEDVRKNdaGYYTCVLKYIYGDKTYNVTRIVKLEV----R 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 239 D-AVPPHIYSPNDRVVyekEPGEELVIPCKVYFSfIMDSHNEIWWTIDGK--KPDDVPVD--ITINESVsYSSTEDETRT 313
Cdd:PHA02785 217 DrIIPPTMQLPEGVVT---SIGSNLTIACRVSLR-PPTTDADVFWISNGMyyEEDDEDGDgrISVANKI-YTTDKRRVIT 291
                        330       340
                 ....*....|....*....|.
gi 268607708 314 QILSIKKVTPEDlKRNYVCHA 334
Cdd:PHA02785 292 SRLNINPVKEED-ATTFTCMA 311
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
37-132 2.36e-10

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first 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. IL-1 receptor antagonist (IL-1RA), a naturally occurring cytokine, is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409583  Cd Length: 91  Bit Score: 57.68  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  37 VFEDEPARIKCPLfehflkynysTAHSSGLTLIWYwtrqDRDLEEPINFRlPENRISKEKDVLWFRPTLLNDTGNYTCML 116
Cdd:cd20991   11 SSANEIDVRSCPL----------NPNESKGTITWY----KNDSKTPISME-QDSRIHQYKEKLWFVPAKVEDSGHYYCVV 75
                         90
                 ....*....|....*.
gi 268607708 117 RNTTYCSKVAFPLEVV 132
Cdd:cd20991   76 RNSTYCLKIKITAKFV 91
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
407-473 8.76e-09

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 53.86  E-value: 8.76e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607708  407 IYVSYARnaEEEEFVLlTLRGVLENEfGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYV 473
Cdd:pfam13676   1 VFISYAG--EDRAWAE-WLADALEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNYL 63
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
157-233 1.35e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 49.32  E-value: 1.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268607708  157 NITCPnvdgyFPSSVKPSVTWYKGCTEIvnfhnvqPKGMNLSFFIPLVSNNGNYTCVVTyleNGRLFHLTRTMTVKV 233
Cdd:pfam13895  18 TLTCS-----APGNPPPSYTWYKDGSAI-------SSSPNFFTLSVSAEDSGTYTCVAR---NGRGGKVSNPVELTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
253-348 4.89e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 47.89  E-value: 4.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   253 VYEKEPGEELVIPCKVYFSfimdSHNEIWWTIDGKKPDDVPVDITINESvsysstedeTRTQILSIKKVTPEDlKRNYVC 332
Cdd:smart00410   3 SVTVKEGESVTLSCEASGS----PPPEVTWYKQGGKLLAESGRFSVSRS---------GSTSTLTISNVTPED-SGTYTC 68
                           90
                   ....*....|....*.
gi 268607708   333 HARNAEGEAEQAAKVK 348
Cdd:smart00410  69 AATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
242-336 1.91e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.02  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  242 PPHIYSPNDRVVYEkePGEELVIPCKVYFSfimdSHNEIWWTIDGKKPDDVPvditinesvsYSSTEDETRTQILSIKKV 321
Cdd:pfam13927   1 KPVITVSPSSVTVR--EGETVTLTCEATGS----PPPTITWYKNGEPISSGS----------TRSRSLSGSNSTLTISNV 64
                          90
                  ....*....|....*
gi 268607708  322 TPEDlKRNYVCHARN 336
Cdd:pfam13927  65 TRSD-AGTYTCVASN 78
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
70-140 5.40e-06

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: 46.26  E-value: 5.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268607708   70 WYWTRQDRDLEEPINFRLPEnrISKEKDVLWFRPTLLNDTGNYTCMLRNTTY-----CSKVAfpLEVVQKD--SCFNS 140
Cdd:pfam18452  48 WYWQPKNGDPLEAITESSPH--IIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKII--LEVQPKTnaSCSGS 121
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
6-234 3.09e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 42.98  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708   6 CLMSLFFCgilqshasERCDDWGLDTMRQIQVFEDePARIKCPLfEHFLK-----------YNYSTAHSSGLTLIwywtr 74
Cdd:PHA02826  12 QFISAFLC--------LYCKYRGGDLTPVYAKFGD-PMVLLCTG-KHYKKsiffdktfitsYNVTWSKTDSLAFV----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708  75 qdRDLEEPINFR-LPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVvqKDSCFNspmrlpvhrLYIEQ 153
Cdd:PHA02826  77 --RDSGARTKIKkITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTF--DSGTIN---------YQFNS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 154 GIH-NITCPNVDGYFPSSVKPSVTWYKGCTEIVNFHNVQPKGMNLSFFIPLVSNN--GNYTCVVTYLENGRLFHLTRTMT 230
Cdd:PHA02826 144 GKDsKLHCYGTDGISSTFKDYTLTWYKNGNIVLYTDRIQLRNNNSTLVIKSATHDdsGIYTCNLRFNKNSNNYNITKEYK 223

                 ....
gi 268607708 231 VKVV 234
Cdd:PHA02826 224 VTII 227
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
158-235 1.40e-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). 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: 38.21  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 158 ITCPNVDgYF--PSSVKPSVTWYKGCT--EIVNFHNVQPKGMNLSFFIPLVsNNGNYTCVVTYLENGRLFHLTRTMTVKV 233
Cdd:cd20994   15 IVCPHLD-FFkdENNNLPKVQWYKDCKplLLDDKRFAGLESDLLIFNVTVQ-DQGNYTCHTSYTYMGKQYNISRTISLIV 92

                 ..
gi 268607708 234 VG 235
Cdd:cd20994   93 LE 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
262-344 4.16e-03

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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 36.54  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607708 262 LVIPCKVYFsfimDSHNEIWWTIDGKKPDDVPVDITINESVSYSstedetrtqiLSIKKVTPEDlKRNYVCHARNAEGEA 341
Cdd:cd00096    1 VTLTCSASG----NPPPTITWYKNGKPLPPSSRDSRRSELGNGT----------LTISNVTLED-SGTYTCVASNSAGGS 65

                 ...
gi 268607708 342 EQA 344
Cdd:cd00096   66 ASA 68
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
157-221 8.12e-03

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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 35.77  E-value: 8.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268607708 157 NITCPnvdgyFPSSVKPSVTWYKGCTEIVN--FHNVQPKGMNLSFFIPLV--SNNGNYTCVVTYLENGR 221
Cdd:cd00096    2 TLTCS-----ASGNPPPTITWYKNGKPLPPssRDSRRSELGNGTLTISNVtlEDSGTYTCVASNSAGGS 65
 
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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