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Conserved domains on  [gi|538918830|ref|NP_001269328|]
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interleukin-18 receptor 1 isoform 2 [Homo sapiens]

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 13093141)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and pattern recognition; similar to Drosophila melanogaster DIP/Dpr cell recognition proteins, which are members of the Wirin family of IgSF proteins with neuronal wiring functions, and human IgLON proteins, a family of cell adhesion molecules

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 ...
 222-364 1.89e-36

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: 130.18  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  222 FVSYLkeCRPENGEEHTFAVEILPRVleKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSN-EVRYEL 300
Cdd:pfam01582   1 YDVFL--SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSgWCLDEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  301 ESGLHEALvERKIKIILIEFTPVTDFT-----FLPQSLKLLKSH----RVLKWKAD----------KSLSYNSRFWKNLL 361
Cdd:pfam01582  77 VKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVlteeKVLKWRGAlnevaniwhsKSVSDESKFWKKIA 155


                  ...
gi 538918830  362 YLM 364
Cdd:pfam01582 156 YDI 158
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 2-53 1.70e-05

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: 43.22  E-value: 1.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 538918830   2 NCKKLLLENN-----KNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVE 53
Cdd:cd20994   38 DCKPLLLDDKrfaglESDLLIFNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVLE 94
PHA02785 super family cl31505
IL-beta-binding protein; Provisional
 16-157 8.38e-04

IL-beta-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02785:

Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 41.15  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  16 IKKNaefeDQGYYSCVHFLHHNGKLFNITKtfnITIVEDRSNIVPvllgPKL---NHVAVELGKNVRLNCSALLNEEDV- 91
Cdd:PHA02785 184 VRKN----DAGYYTCVLKYIYGDKTYNVTR---IVKLEVRDRIIP----PTMqlpEGVVTSIGSNLTIACRVSLRPPTTd 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918830  92 --IYW----MFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVlYNC---TVASTGGTDTKSFI 157
Cdd:PHA02785 253 adVFWisngMYYEEDDEDGDGRISVANKIYTTDKRRVITSRLNINPVKEEDATT-FTCmafTIPSISKTVTISIT 326
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 222-364 1.89e-36

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: 130.18  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  222 FVSYLkeCRPENGEEHTFAVEILPRVleKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSN-EVRYEL 300
Cdd:pfam01582   1 YDVFL--SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSgWCLDEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  301 ESGLHEALvERKIKIILIEFTPVTDFT-----FLPQSLKLLKSH----RVLKWKAD----------KSLSYNSRFWKNLL 361
Cdd:pfam01582  77 VKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVlteeKVLKWRGAlnevaniwhsKSVSDESKFWKKIA 155


                  ...
gi 538918830  362 YLM 364
Cdd:pfam01582 156 YDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
218-367 2.16e-34

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 123.97  E-value: 2.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830   218 TYDAFVSYlkecrpenGEEHTFAVEILPRVLEKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNE-V 296
Cdd:smart00255   1 EYDVFISY--------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEwC 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 538918830   297 RYELESGLHEALVERKIKIILIEFTPVT-DFTFLPQSLKLLKSHRVLKWKADKSLsynsRFWKNLLYLMPAK 367
Cdd:smart00255  73 LDELVAALENALEEGGLRVIPIFYEVIPsDVRKQPGKFRKVFKKNYLKWPEDEKE----QFWKKALYAVPSK 140
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 2-53 1.70e-05

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: 43.22  E-value: 1.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 538918830   2 NCKKLLLENN-----KNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVE 53
Cdd:cd20994   38 DCKPLLLDDKrfaglESDLLIFNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVLE 94
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 16-157 8.38e-04

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 41.15  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  16 IKKNaefeDQGYYSCVHFLHHNGKLFNITKtfnITIVEDRSNIVPvllgPKL---NHVAVELGKNVRLNCSALLNEEDV- 91
Cdd:PHA02785 184 VRKN----DAGYYTCVLKYIYGDKTYNVTR---IVKLEVRDRIIP----PTMqlpEGVVTSIGSNLTIACRVSLRPPTTd 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918830  92 --IYW----MFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVlYNC---TVASTGGTDTKSFI 157
Cdd:PHA02785 253 adVFWisngMYYEEDDEDGDGRISVANKIYTTDKRRVITSRLNINPVKEEDATT-FTCmafTIPSISKTVTISIT 326
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 69-158 3.13e-03

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: 36.33  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830    69 HVAVELGKNVRLNCSALLNEEDVIYWMFGeengsDPNIHEEKEMRIMTPEGKWHaskVLRIENIGESNlNVLYNCTVAST 148
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQ-----GGKLLAESGRFSVSRSGSTS---TLTISNVTPED-SGTYTCAATNS 73

                           90
                   ....*....|
gi 538918830   149 GGTDTKSFIL 158
Cdd:smart00410  74 SGSASSGTTL 83
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 222-364 1.89e-36

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: 130.18  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  222 FVSYLkeCRPENGEEHTFAVEILPRVleKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSN-EVRYEL 300
Cdd:pfam01582   1 YDVFL--SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSgWCLDEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  301 ESGLHEALvERKIKIILIEFTPVTDFT-----FLPQSLKLLKSH----RVLKWKAD----------KSLSYNSRFWKNLL 361
Cdd:pfam01582  77 VKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVlteeKVLKWRGAlnevaniwhsKSVSDESKFWKKIA 155


                  ...
gi 538918830  362 YLM 364
Cdd:pfam01582 156 YDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
218-367 2.16e-34

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 123.97  E-value: 2.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830   218 TYDAFVSYlkecrpenGEEHTFAVEILPRVLEKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNE-V 296
Cdd:smart00255   1 EYDVFISY--------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEwC 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 538918830   297 RYELESGLHEALVERKIKIILIEFTPVT-DFTFLPQSLKLLKSHRVLKWKADKSLsynsRFWKNLLYLMPAK 367
Cdd:smart00255  73 LDELVAALENALEEGGLRVIPIFYEVIPsDVRKQPGKFRKVFKKNYLKWPEDEKE----QFWKKALYAVPSK 140
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 222-319 1.54e-11

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 60.79  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  222 FVSYlkecrpeNGEEHTFAVEILPRvLEKHfGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNE-VRYEL 300
Cdd:pfam13676   2 FISY-------AGEDRAWAEWLADA-LEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNYLESPwCRAEW 72

                          90
                  ....*....|....*....
gi 538918830  301 ESGLHEALVERKIKIILIE 319
Cdd:pfam13676  73 EAALADPEGRKRLIPVRLE 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 2-53 1.70e-05

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: 43.22  E-value: 1.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 538918830   2 NCKKLLLENN-----KNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVE 53
Cdd:cd20994   38 DCKPLLLDDKrfaglESDLLIFNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVLE 94
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 1-53 3.44e-05

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: 42.31  E-value: 3.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 538918830   1 MNCKKLLLENN----KNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVE 53
Cdd:cd05757   36 KDCKPLQGDKRfipkGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYNVTRTISLTVTE 92
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 16-157 8.38e-04

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 41.15  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830  16 IKKNaefeDQGYYSCVHFLHHNGKLFNITKtfnITIVEDRSNIVPvllgPKL---NHVAVELGKNVRLNCSALLNEEDV- 91
Cdd:PHA02785 184 VRKN----DAGYYTCVLKYIYGDKTYNVTR---IVKLEVRDRIIP----PTMqlpEGVVTSIGSNLTIACRVSLRPPTTd 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918830  92 --IYW----MFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVlYNC---TVASTGGTDTKSFI 157
Cdd:PHA02785 253 adVFWisngMYYEEDDEDGDGRISVANKIYTTDKRRVITSRLNINPVKEEDATT-FTCmafTIPSISKTVTISIT 326
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 69-158 3.13e-03

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: 36.33  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918830    69 HVAVELGKNVRLNCSALLNEEDVIYWMFGeengsDPNIHEEKEMRIMTPEGKWHaskVLRIENIGESNlNVLYNCTVAST 148
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQ-----GGKLLAESGRFSVSRSGSTS---TLTISNVTPED-SGTYTCAATNS 73

                           90
                   ....*....|
gi 538918830   149 GGTDTKSFIL 158
Cdd:smart00410  74 SGSASSGTTL 83
 
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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