triggering receptor expressed on myeloid cells 1 isoform X1 [Rattus norvegicus]
immunoglobulin domain-containing family protein( domain architecture ID 34076)
immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Ig super family | cl11960 | Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ... |
24-132 | 1.06e-15 | |||
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 cd05716: Pssm-ID: 472250 Cd Length: 100 Bit Score: 70.12 E-value: 1.06e-15
|
|||||||
Name | Accession | Description | Interval | E-value | |||
IgV_pIgR_like | cd05716 | Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ... |
24-132 | 1.06e-15 | |||
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others. Pssm-ID: 409381 Cd Length: 100 Bit Score: 70.12 E-value: 1.06e-15
|
|||||||
V-set | pfam07686 | Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ... |
32-134 | 8.95e-12 | |||
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others. Pssm-ID: 462230 Cd Length: 109 Bit Score: 59.78 E-value: 8.95e-12
|
|||||||
IGv | smart00406 | Immunoglobulin V-Type; |
36-113 | 1.33e-04 | |||
Immunoglobulin V-Type; Pssm-ID: 214650 Cd Length: 81 Bit Score: 39.29 E-value: 1.33e-04
|
|||||||
Name | Accession | Description | Interval | E-value | |||
IgV_pIgR_like | cd05716 | Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ... |
24-132 | 1.06e-15 | |||
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others. Pssm-ID: 409381 Cd Length: 100 Bit Score: 70.12 E-value: 1.06e-15
|
|||||||
V-set | pfam07686 | Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ... |
32-134 | 8.95e-12 | |||
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others. Pssm-ID: 462230 Cd Length: 109 Bit Score: 59.78 E-value: 8.95e-12
|
|||||||
IgV_H_TCR_mu | cd16095 | T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ... |
34-114 | 4.25e-06 | |||
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain of the T-cell receptor Mu. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409514 Cd Length: 115 Bit Score: 44.47 E-value: 4.25e-06
|
|||||||
IGv | smart00406 | Immunoglobulin V-Type; |
36-113 | 1.33e-04 | |||
Immunoglobulin V-Type; Pssm-ID: 214650 Cd Length: 81 Bit Score: 39.29 E-value: 1.33e-04
|
|||||||
Ig_Aggrecan | cd05900 | Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ... |
23-117 | 3.10e-04 | |||
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes. Pssm-ID: 409481 Cd Length: 123 Bit Score: 39.54 E-value: 3.10e-04
|
|||||||
IgV | cd00099 | Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ... |
33-126 | 9.76e-03 | |||
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other. Pssm-ID: 409355 [Multi-domain] Cd Length: 111 Bit Score: 34.62 E-value: 9.76e-03
|
|||||||
Blast search parameters | ||||
|