single Ig IL-1-related receptor [Homo sapiens]
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 ... |
168-311 | 3.07e-15 | ||||
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: 72.78 E-value: 3.07e-15
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Ig super family | cl11960 | Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ... |
9-66 | 1.32e-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 pfam07679: Pssm-ID: 472250 [Multi-domain] Cd Length: 90 Bit Score: 43.40 E-value: 1.32e-05
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Name | Accession | Description | Interval | E-value | ||||
TIR | pfam01582 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
168-311 | 3.07e-15 | ||||
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: 72.78 E-value: 3.07e-15
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TIR | smart00255 | Toll - interleukin 1 - resistance; |
165-310 | 1.03e-13 | ||||
Toll - interleukin 1 - resistance; Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 67.73 E-value: 1.03e-13
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I-set | pfam07679 | Immunoglobulin I-set domain; |
9-66 | 1.32e-05 | ||||
Immunoglobulin I-set domain; Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 43.40 E-value: 1.32e-05
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IgI_4_Dscam | cd20956 | Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ... |
8-102 | 1.45e-05 | ||||
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig 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: 409548 [Multi-domain] Cd Length: 96 Bit Score: 43.32 E-value: 1.45e-05
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Name | Accession | Description | Interval | E-value | ||||
TIR | pfam01582 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
168-311 | 3.07e-15 | ||||
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: 72.78 E-value: 3.07e-15
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TIR | smart00255 | Toll - interleukin 1 - resistance; |
165-310 | 1.03e-13 | ||||
Toll - interleukin 1 - resistance; Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 67.73 E-value: 1.03e-13
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TIR_2 | pfam13676 | TIR domain; This is a family of Toll-like receptors. |
168-269 | 2.71e-07 | ||||
TIR domain; This is a family of Toll-like receptors. Pssm-ID: 463954 [Multi-domain] Cd Length: 118 Bit Score: 48.85 E-value: 2.71e-07
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I-set | pfam07679 | Immunoglobulin I-set domain; |
9-66 | 1.32e-05 | ||||
Immunoglobulin I-set domain; Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 43.40 E-value: 1.32e-05
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IgI_4_Dscam | cd20956 | Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ... |
8-102 | 1.45e-05 | ||||
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig 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: 409548 [Multi-domain] Cd Length: 96 Bit Score: 43.32 E-value: 1.45e-05
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IgC1_hNephrin_like | cd05773 | Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ... |
8-111 | 6.85e-04 | ||||
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes. Pssm-ID: 143250 Cd Length: 109 Bit Score: 39.14 E-value: 6.85e-04
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Ig_3 | pfam13927 | Immunoglobulin domain; This family contains immunoglobulin-like domains. |
9-102 | 3.80e-03 | ||||
Immunoglobulin domain; This family contains immunoglobulin-like domains. Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 36.00 E-value: 3.80e-03
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Blast search parameters | ||||
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