IC9-Luc90-CD828Z [synthetic construct]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
136-398 | 1.20e-103 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. : Pssm-ID: 237997 Cd Length: 243 Bit Score: 321.86 E-value: 1.20e-103
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IgV_H | cd04981 | Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ... |
571-687 | 1.79e-64 | |||||
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. 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. : Pssm-ID: 409370 [Multi-domain] Cd Length: 118 Bit Score: 212.17 E-value: 1.79e-64
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IgV_L_kappa | cd04980 | Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ... |
445-549 | 2.77e-60 | |||||
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). 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 seem to be functionally identical, and can associate with any of the heavy chains. : Pssm-ID: 409369 Cd Length: 106 Bit Score: 200.31 E-value: 2.77e-60
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FkpA | COG0545 | FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
5-108 | 5.05e-43 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 151.49 E-value: 5.05e-43
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ITAM | smart00077 | Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on ... |
830-850 | 1.69e-04 | |||||
Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery. : Pssm-ID: 128390 Cd Length: 21 Bit Score: 39.29 E-value: 1.69e-04
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ITAM | smart00077 | Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on ... |
899-919 | 7.20e-04 | |||||
Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery. : Pssm-ID: 128390 Cd Length: 21 Bit Score: 37.36 E-value: 7.20e-04
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Name | Accession | Description | Interval | E-value | |||||
CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
136-398 | 1.20e-103 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. Pssm-ID: 237997 Cd Length: 243 Bit Score: 321.86 E-value: 1.20e-103
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CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
137-397 | 7.50e-98 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. Pssm-ID: 214521 Cd Length: 241 Bit Score: 306.47 E-value: 7.50e-98
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IgV_H | cd04981 | Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ... |
571-687 | 1.79e-64 | |||||
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. 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. Pssm-ID: 409370 [Multi-domain] Cd Length: 118 Bit Score: 212.17 E-value: 1.79e-64
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Peptidase_C14 | pfam00656 | Caspase domain; |
145-396 | 5.63e-63 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 211.80 E-value: 5.63e-63
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IgV_L_kappa | cd04980 | Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ... |
445-549 | 2.77e-60 | |||||
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). 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 seem to be functionally identical, and can associate with any of the heavy chains. Pssm-ID: 409369 Cd Length: 106 Bit Score: 200.31 E-value: 2.77e-60
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FkpA | COG0545 | FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
5-108 | 5.05e-43 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 151.49 E-value: 5.05e-43
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FKBP_C | pfam00254 | FKBP-type peptidyl-prolyl cis-trans isomerase; |
15-107 | 6.51e-42 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase; Pssm-ID: 459735 Cd Length: 94 Bit Score: 148.11 E-value: 6.51e-42
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IGv | smart00406 | Immunoglobulin V-Type; |
585-666 | 2.31e-27 | |||||
Immunoglobulin V-Type; Pssm-ID: 214650 Cd Length: 81 Bit Score: 105.93 E-value: 2.31e-27
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PRK10902 | PRK10902 | FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
6-110 | 5.50e-24 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 102.53 E-value: 5.50e-24
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IGv | smart00406 | Immunoglobulin V-Type; |
462-533 | 3.69e-18 | |||||
Immunoglobulin V-Type; Pssm-ID: 214650 Cd Length: 81 Bit Score: 79.73 E-value: 3.69e-18
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V-set | pfam07686 | Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ... |
449-547 | 5.15e-17 | |||||
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: 77.50 E-value: 5.15e-17
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V-set | pfam07686 | Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ... |
573-686 | 4.54e-10 | |||||
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: 57.85 E-value: 4.54e-10
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ITAM | smart00077 | Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on ... |
830-850 | 1.69e-04 | |||||
Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery. Pssm-ID: 128390 Cd Length: 21 Bit Score: 39.29 E-value: 1.69e-04
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ITAM | smart00077 | Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on ... |
899-919 | 7.20e-04 | |||||
Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery. Pssm-ID: 128390 Cd Length: 21 Bit Score: 37.36 E-value: 7.20e-04
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ITAM | pfam02189 | Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex ... |
899-918 | 2.72e-03 | |||||
Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex multi-protein cell surface receptor composed of the ligand-sensing TCR heterodimer and three signaling subunits. These signaling subunits contain cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) with a consensus sequence of YxxL/Ix6-12YxxL/I. The two tyrosines are phosphorylated by a Src kinase, Lck or Fyn. Binding of the dually phosphorylated ITAM peptide reorients the two SH2 domains relative to each other, destabilizing inhibitory interactions made by the linker connecting the SH2 and kinase domains. Pssm-ID: 426646 Cd Length: 20 Bit Score: 35.82 E-value: 2.72e-03
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ITAM | pfam02189 | Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex ... |
830-849 | 3.16e-03 | |||||
Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex multi-protein cell surface receptor composed of the ligand-sensing TCR heterodimer and three signaling subunits. These signaling subunits contain cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) with a consensus sequence of YxxL/Ix6-12YxxL/I. The two tyrosines are phosphorylated by a Src kinase, Lck or Fyn. Binding of the dually phosphorylated ITAM peptide reorients the two SH2 domains relative to each other, destabilizing inhibitory interactions made by the linker connecting the SH2 and kinase domains. Pssm-ID: 426646 Cd Length: 20 Bit Score: 35.82 E-value: 3.16e-03
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Name | Accession | Description | Interval | E-value | |||||
CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
136-398 | 1.20e-103 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. Pssm-ID: 237997 Cd Length: 243 Bit Score: 321.86 E-value: 1.20e-103
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CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
137-397 | 7.50e-98 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. Pssm-ID: 214521 Cd Length: 241 Bit Score: 306.47 E-value: 7.50e-98
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IgV_H | cd04981 | Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ... |
571-687 | 1.79e-64 | |||||
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. 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. Pssm-ID: 409370 [Multi-domain] Cd Length: 118 Bit Score: 212.17 E-value: 1.79e-64
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Peptidase_C14 | pfam00656 | Caspase domain; |
145-396 | 5.63e-63 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 211.80 E-value: 5.63e-63
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IgV_L_kappa | cd04980 | Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ... |
445-549 | 2.77e-60 | |||||
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). 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 seem to be functionally identical, and can associate with any of the heavy chains. Pssm-ID: 409369 Cd Length: 106 Bit Score: 200.31 E-value: 2.77e-60
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FkpA | COG0545 | FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ... |
5-108 | 5.05e-43 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440311 [Multi-domain] Cd Length: 104 Bit Score: 151.49 E-value: 5.05e-43
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FKBP_C | pfam00254 | FKBP-type peptidyl-prolyl cis-trans isomerase; |
15-107 | 6.51e-42 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase; Pssm-ID: 459735 Cd Length: 94 Bit Score: 148.11 E-value: 6.51e-42
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IgV_L_lambda | cd04984 | Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ... |
446-547 | 2.36e-34 | |||||
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). 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 seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409373 Cd Length: 105 Bit Score: 126.81 E-value: 2.36e-34
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IgV | cd00099 | Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ... |
447-548 | 1.19e-31 | |||||
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: 119.36 E-value: 1.19e-31
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IGv | smart00406 | Immunoglobulin V-Type; |
585-666 | 2.31e-27 | |||||
Immunoglobulin V-Type; Pssm-ID: 214650 Cd Length: 81 Bit Score: 105.93 E-value: 2.31e-27
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PRK10902 | PRK10902 | FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
6-110 | 5.50e-24 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional Pssm-ID: 236791 [Multi-domain] Cd Length: 269 Bit Score: 102.53 E-value: 5.50e-24
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IgV | cd00099 | Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ... |
573-686 | 1.40e-23 | |||||
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: 96.25 E-value: 1.40e-23
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PRK11570 | PRK11570 | peptidyl-prolyl cis-trans isomerase; Provisional |
4-109 | 1.31e-19 | |||||
peptidyl-prolyl cis-trans isomerase; Provisional Pssm-ID: 183207 [Multi-domain] Cd Length: 206 Bit Score: 87.93 E-value: 1.31e-19
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IgV_TCR_alpha | cd04983 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ... |
448-547 | 3.86e-19 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409372 [Multi-domain] Cd Length: 109 Bit Score: 83.47 E-value: 3.86e-19
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IGv | smart00406 | Immunoglobulin V-Type; |
462-533 | 3.69e-18 | |||||
Immunoglobulin V-Type; Pssm-ID: 214650 Cd Length: 81 Bit Score: 79.73 E-value: 3.69e-18
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IgV_TCR_beta | cd05899 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ... |
448-547 | 1.38e-17 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409480 Cd Length: 110 Bit Score: 79.25 E-value: 1.38e-17
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V-set | pfam07686 | Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ... |
449-547 | 5.15e-17 | |||||
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: 77.50 E-value: 5.15e-17
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IG_like | smart00410 | Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG. |
451-548 | 1.49e-15 | |||||
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: 72.54 E-value: 1.49e-15
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IgV_TCR_gamma | cd04982 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ... |
447-547 | 3.41e-15 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409371 Cd Length: 117 Bit Score: 72.40 E-value: 3.41e-15
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IgV_TCR_alpha | cd04983 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ... |
573-686 | 5.72e-14 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409372 [Multi-domain] Cd Length: 109 Bit Score: 68.84 E-value: 5.72e-14
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IgV_TCR_beta | cd05899 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ... |
573-686 | 2.65e-13 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409480 Cd Length: 110 Bit Score: 66.92 E-value: 2.65e-13
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SlpA | COG1047 | Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ... |
20-106 | 1.78e-12 | |||||
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440668 [Multi-domain] Cd Length: 138 Bit Score: 65.51 E-value: 1.78e-12
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IG_like | smart00410 | Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG. |
575-686 | 7.45e-12 | |||||
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: 62.14 E-value: 7.45e-12
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IgV_TCR_gamma | cd04982 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ... |
572-666 | 8.87e-12 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409371 Cd Length: 117 Bit Score: 62.77 E-value: 8.87e-12
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IgV_L_lambda | cd04984 | Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ... |
572-686 | 1.33e-11 | |||||
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). 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 seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409373 Cd Length: 105 Bit Score: 62.09 E-value: 1.33e-11
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V-set | pfam07686 | Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ... |
573-686 | 4.54e-10 | |||||
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: 57.85 E-value: 4.54e-10
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IgV_TCR_delta | cd07706 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ... |
448-547 | 1.98e-09 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409503 Cd Length: 112 Bit Score: 55.99 E-value: 1.98e-09
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IgV_TCR_gammadelta | cd20988 | Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ... |
580-686 | 1.07e-07 | |||||
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409580 Cd Length: 114 Bit Score: 51.02 E-value: 1.07e-07
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IgV_H_TCR_mu | cd16095 | T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ... |
569-686 | 1.29e-07 | |||||
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: 51.02 E-value: 1.29e-07
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IgV_CD8_beta | cd07700 | Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ... |
572-686 | 1.32e-07 | |||||
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409497 Cd Length: 116 Bit Score: 50.91 E-value: 1.32e-07
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IgV_H | cd04981 | Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ... |
459-535 | 1.59e-07 | |||||
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. 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. Pssm-ID: 409370 [Multi-domain] Cd Length: 118 Bit Score: 50.77 E-value: 1.59e-07
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IgV_CD8_alpha | cd05720 | Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; ... |
450-531 | 2.63e-07 | |||||
Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; The members here are composed of the immunoglobulin (Ig)-like variable domain of the Cluster of Differentiation (CD) 8 alpha. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. The Ig domain of CD8 alpha binds to antibodies. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409385 Cd Length: 110 Bit Score: 49.79 E-value: 2.63e-07
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IgV_L_kappa | cd04980 | Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ... |
573-664 | 7.51e-07 | |||||
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). 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 seem to be functionally identical, and can associate with any of the heavy chains. Pssm-ID: 409369 Cd Length: 106 Bit Score: 48.54 E-value: 7.51e-07
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PRK15095 | PRK15095 | FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional |
27-86 | 1.58e-06 | |||||
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional Pssm-ID: 237908 [Multi-domain] Cd Length: 156 Bit Score: 48.94 E-value: 1.58e-06
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IgV_SIRP | cd16097 | Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The ... |
447-550 | 2.94e-06 | |||||
Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409516 Cd Length: 111 Bit Score: 46.78 E-value: 2.94e-06
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IgV_TCR_delta | cd07706 | Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ... |
583-686 | 3.40e-06 | |||||
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409503 Cd Length: 112 Bit Score: 46.74 E-value: 3.40e-06
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IgV_CD8_beta | cd07700 | Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ... |
449-547 | 5.40e-05 | |||||
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409497 Cd Length: 116 Bit Score: 43.59 E-value: 5.40e-05
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IgV_CD79b_beta | cd16096 | Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are ... |
476-547 | 1.03e-04 | |||||
Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are composed of the immunoglobulin variable domain (IgV) of the Cluster of Differentiation (CD) 79B (also known as CD79b molecule, immunoglobulin-associated beta (Ig-beta), and B29). The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-beta protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. Members of the IgV family 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. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409515 Cd Length: 96 Bit Score: 42.25 E-value: 1.03e-04
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ITAM | smart00077 | Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on ... |
830-850 | 1.69e-04 | |||||
Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery. Pssm-ID: 128390 Cd Length: 21 Bit Score: 39.29 E-value: 1.69e-04
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I-set | pfam07679 | Immunoglobulin I-set domain; |
446-532 | 3.20e-04 | |||||
Immunoglobulin I-set domain; Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 40.32 E-value: 3.20e-04
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Ig_3 | pfam13927 | Immunoglobulin domain; This family contains immunoglobulin-like domains. |
446-532 | 3.24e-04 | |||||
Immunoglobulin domain; This family contains immunoglobulin-like domains. Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 40.24 E-value: 3.24e-04
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Ig_3 | pfam13927 | Immunoglobulin domain; This family contains immunoglobulin-like domains. |
574-664 | 4.06e-04 | |||||
Immunoglobulin domain; This family contains immunoglobulin-like domains. Pssm-ID: 464046 [Multi-domain] Cd Length: 78 Bit Score: 39.86 E-value: 4.06e-04
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ITAM | smart00077 | Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on ... |
899-919 | 7.20e-04 | |||||
Immunoreceptor tyrosine-based activation motif; Motif that may be dually phosphorylated on tyrosine that links antigen receptors to downstream signalling machinery. Pssm-ID: 128390 Cd Length: 21 Bit Score: 37.36 E-value: 7.20e-04
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ITAM | pfam02189 | Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex ... |
899-918 | 2.72e-03 | |||||
Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex multi-protein cell surface receptor composed of the ligand-sensing TCR heterodimer and three signaling subunits. These signaling subunits contain cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) with a consensus sequence of YxxL/Ix6-12YxxL/I. The two tyrosines are phosphorylated by a Src kinase, Lck or Fyn. Binding of the dually phosphorylated ITAM peptide reorients the two SH2 domains relative to each other, destabilizing inhibitory interactions made by the linker connecting the SH2 and kinase domains. Pssm-ID: 426646 Cd Length: 20 Bit Score: 35.82 E-value: 2.72e-03
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ITAM | pfam02189 | Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex ... |
830-849 | 3.16e-03 | |||||
Immunoreceptor tyrosine-based activation motif; T cell receptor (TCR) is a complex multi-protein cell surface receptor composed of the ligand-sensing TCR heterodimer and three signaling subunits. These signaling subunits contain cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) with a consensus sequence of YxxL/Ix6-12YxxL/I. The two tyrosines are phosphorylated by a Src kinase, Lck or Fyn. Binding of the dually phosphorylated ITAM peptide reorients the two SH2 domains relative to each other, destabilizing inhibitory interactions made by the linker connecting the SH2 and kinase domains. Pssm-ID: 426646 Cd Length: 20 Bit Score: 35.82 E-value: 3.16e-03
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Blast search parameters | ||||
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