interleukin-18 receptor 1 isoform X1 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
TIR super family | cl23801 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
375-516 | 1.16e-29 | ||||
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. The actual alignment was detected with superfamily member pfam01582: Pssm-ID: 396246 [Multi-domain] Cd Length: 165 Bit Score: 114.38 E-value: 1.16e-29
|
||||||||
Ig super family | cl11960 | Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ... |
131-205 | 7.37e-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 cd05757: Pssm-ID: 472250 Cd Length: 92 Bit Score: 53.10 E-value: 7.37e-09
|
||||||||
Ig_6 super family | cl39786 | Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ... |
3-98 | 3.29e-05 | ||||
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. The actual alignment was detected with superfamily member pfam18452: Pssm-ID: 465773 Cd Length: 128 Bit Score: 43.56 E-value: 3.29e-05
|
||||||||
PHA02785 super family | cl31505 | IL-beta-binding protein; Provisional |
157-257 | 3.36e-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: 43.08 E-value: 3.36e-04
|
||||||||
Ig super family | cl11960 | Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ... |
212-312 | 2.09e-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. The actual alignment was detected with superfamily member cd20932: Pssm-ID: 472250 Cd Length: 104 Bit Score: 38.03 E-value: 2.09e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
TIR | pfam01582 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
375-516 | 1.16e-29 | ||||
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: 114.38 E-value: 1.16e-29
|
||||||||
TIR | smart00255 | Toll - interleukin 1 - resistance; |
371-519 | 1.83e-28 | ||||
Toll - interleukin 1 - resistance; Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 110.11 E-value: 1.83e-28
|
||||||||
Ig2_IL1R-like | cd05757 | Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ... |
131-205 | 7.37e-09 | ||||
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: 53.10 E-value: 7.37e-09
|
||||||||
Ig_6 | pfam18452 | Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ... |
3-98 | 3.29e-05 | ||||
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: 43.56 E-value: 3.29e-05
|
||||||||
PHA02785 | PHA02785 | IL-beta-binding protein; Provisional |
157-257 | 3.36e-04 | ||||
IL-beta-binding protein; Provisional Pssm-ID: 165149 [Multi-domain] Cd Length: 326 Bit Score: 43.08 E-value: 3.36e-04
|
||||||||
IG_like | smart00410 | Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG. |
26-112 | 1.03e-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: 38.26 E-value: 1.03e-03
|
||||||||
Ig3_IL1R_like | cd20932 | Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ... |
212-312 | 2.09e-03 | ||||
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: 38.03 E-value: 2.09e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
TIR | pfam01582 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
375-516 | 1.16e-29 | ||||
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: 114.38 E-value: 1.16e-29
|
||||||||
TIR | smart00255 | Toll - interleukin 1 - resistance; |
371-519 | 1.83e-28 | ||||
Toll - interleukin 1 - resistance; Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 110.11 E-value: 1.83e-28
|
||||||||
TIR_2 | pfam13676 | TIR domain; This is a family of Toll-like receptors. |
375-472 | 1.56e-09 | ||||
TIR domain; This is a family of Toll-like receptors. Pssm-ID: 463954 [Multi-domain] Cd Length: 118 Bit Score: 55.78 E-value: 1.56e-09
|
||||||||
Ig2_IL1R-like | cd05757 | Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ... |
131-205 | 7.37e-09 | ||||
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: 53.10 E-value: 7.37e-09
|
||||||||
Ig2_IL1R_like | cd20994 | Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ... |
142-205 | 2.87e-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: 42.84 E-value: 2.87e-05
|
||||||||
Ig_6 | pfam18452 | Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ... |
3-98 | 3.29e-05 | ||||
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: 43.56 E-value: 3.29e-05
|
||||||||
PHA02785 | PHA02785 | IL-beta-binding protein; Provisional |
157-257 | 3.36e-04 | ||||
IL-beta-binding protein; Provisional Pssm-ID: 165149 [Multi-domain] Cd Length: 326 Bit Score: 43.08 E-value: 3.36e-04
|
||||||||
IG_like | smart00410 | Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG. |
26-112 | 1.03e-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: 38.26 E-value: 1.03e-03
|
||||||||
Ig3_IL1R_like | cd20932 | Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ... |
212-312 | 2.09e-03 | ||||
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: 38.03 E-value: 2.09e-03
|
||||||||
Ig2_IL1R2_like | cd05897 | Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ... |
169-205 | 4.97e-03 | ||||
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). 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 the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and 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: 409478 Cd Length: 95 Bit Score: 36.66 E-value: 4.97e-03
|
||||||||
Blast search parameters | ||||
|