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Conserved domains on  [gi|1207170594|ref|XP_021330440|]
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T-cell receptor beta chain V region A20.2.25 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
137-234 3.09e-35

Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) light chain constant (C) domain. 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 determine the type of immunoglobulin: 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: 409496  Cd Length: 99  Bit Score: 121.02  E-value: 3.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 137 PPVLTILRPSSrEELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRE 216
Cdd:cd07699     1 APSVTIFPPSS-EELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKV 79
                          90       100
                  ....*....|....*....|
gi 1207170594 217 LTCEATVAS--KTSRASIRK 234
Cdd:cd07699    80 YTCEVTHEGlsSTITKSFNR 99
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
21-130 2.31e-26

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: 98.56  E-value: 2.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQSPV-ITVSKGQTAQLDCNL--GTVTNYAAWYKQTPAEVPQYVLYNYhgwSSPEYGSGFSAPKFTSTCSSKSDCSLII 97
Cdd:cd00099     1 VTQSPRsLSVQEGESVTLSCEVssSFSSTYIYWYRQKPGQGPEFLIYLS---SSKGKTKGGVPGRFSGSRDGTSSFSLTI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207170594  98 SNVDVSDSAVYYCQTWDSS-VSEYVFGQGTKLIV 130
Cdd:cd00099    78 SNLQPEDSGTYYCAVSESGgTDKLTFGSGTRLTV 111
 
Name Accession Description Interval E-value
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
137-234 3.09e-35

Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) light chain constant (C) domain. 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 determine the type of immunoglobulin: 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: 409496  Cd Length: 99  Bit Score: 121.02  E-value: 3.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 137 PPVLTILRPSSrEELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRE 216
Cdd:cd07699     1 APSVTIFPPSS-EELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKV 79
                          90       100
                  ....*....|....*....|
gi 1207170594 217 LTCEATVAS--KTSRASIRK 234
Cdd:cd07699    80 YTCEVTHEGlsSTITKSFNR 99
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
21-130 2.31e-26

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: 98.56  E-value: 2.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQSPV-ITVSKGQTAQLDCNL--GTVTNYAAWYKQTPAEVPQYVLYNYhgwSSPEYGSGFSAPKFTSTCSSKSDCSLII 97
Cdd:cd00099     1 VTQSPRsLSVQEGESVTLSCEVssSFSSTYIYWYRQKPGQGPEFLIYLS---SSKGKTKGGVPGRFSGSRDGTSSFSLTI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207170594  98 SNVDVSDSAVYYCQTWDSS-VSEYVFGQGTKLIV 130
Cdd:cd00099    78 SNLQPEDSGTYYCAVSESGgTDKLTFGSGTRLTV 111
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
22-131 2.09e-15

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: 69.79  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  22 TQSPVITVSKGQTAQLDC----NLGTVTNYAAWYKQTPAEVPQYVLYNYhgwsSPEYGSGFSAPKFTSTCS-SKSDCSLI 96
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCtyssSMSEASTSVYWYRQPPGKGPTFLIAYY----SNGSEEGVKKGRFSGRGDpSNGDGSLT 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1207170594  97 ISNVDVSDSAVYYCQTWDSsvSEYVFGQGTKLIVT 131
Cdd:pfam07686  77 IQNLTLSDSGTYTCAVIPS--GEGVFGKGTRLTVL 109
C1-set pfam07654
Immunoglobulin C1-set domain;
145-222 6.88e-10

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 54.18  E-value: 6.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207170594 145 PSSREELSSsKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRELTCEAT 222
Cdd:pfam07654   5 PPSPEELGK-PNTLTCLVTGFYPPDITVTWLKNGQEVTEGVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTCRVE 81
IGc1 smart00407
Immunoglobulin C-Type;
155-222 1.49e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 53.09  E-value: 1.49e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207170594  155 KVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRELTCEAT 222
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVT 68
IGv smart00406
Immunoglobulin V-Type;
34-112 2.02e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 50.07  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594   34 TAQLDCNLGTVTN---YAAWYKQTPAEVPQYVLYnyHGWSSPEYGSGFSAPKFT-STCSSKSDCSLIISNVDVSDSAVYY 109
Cdd:smart00406   1 SVTLSCKFSGSTFssyYVSWVRQPPGKGLEWLGY--IGSNGSSYYQESYKGRFTiSKDTSKNDVSLTISNLRVEDTGTYY 78

                   ...
gi 1207170594  110 CQT 112
Cdd:smart00406  79 CAV 81
 
Name Accession Description Interval E-value
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
137-234 3.09e-35

Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) light chain constant (C) domain. 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 determine the type of immunoglobulin: 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: 409496  Cd Length: 99  Bit Score: 121.02  E-value: 3.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 137 PPVLTILRPSSrEELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRE 216
Cdd:cd07699     1 APSVTIFPPSS-EELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKV 79
                          90       100
                  ....*....|....*....|
gi 1207170594 217 LTCEATVAS--KTSRASIRK 234
Cdd:cd07699    80 YTCEVTHEGlsSTITKSFNR 99
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
21-130 2.31e-26

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: 98.56  E-value: 2.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQSPV-ITVSKGQTAQLDCNL--GTVTNYAAWYKQTPAEVPQYVLYNYhgwSSPEYGSGFSAPKFTSTCSSKSDCSLII 97
Cdd:cd00099     1 VTQSPRsLSVQEGESVTLSCEVssSFSSTYIYWYRQKPGQGPEFLIYLS---SSKGKTKGGVPGRFSGSRDGTSSFSLTI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207170594  98 SNVDVSDSAVYYCQTWDSS-VSEYVFGQGTKLIV 130
Cdd:cd00099    78 SNLQPEDSGTYYCAVSESGgTDKLTFGSGTRLTV 111
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
20-130 2.92e-21

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: 85.21  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  20 VVTQSPVITVSKGQTAQLDC---NLGTVTNYAAWYKQTPAEVPQYVLYNYHGwsspeYGSGfsAPKFTSTCSSKSDCSLI 96
Cdd:cd04984     1 VLTQPSSLSVSPGETVTITCtgsSGNISGNYVNWYQQKPGSAPRYLIYEDKH-----RPSG--IPDRFSGSKSGNTASLT 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207170594  97 ISNVDVSDSAVYYCQTWDSSVseYVFGQGTKLIV 130
Cdd:cd04984    74 ISGAQTEDEADYYCQVWDSNS--YVFGGGTKLTV 105
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
21-131 1.50e-20

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: 83.09  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQSP-VITVSKGQTAQLDCNLGTVTNYAA-WYKQTPAEVPQYVLYNYhGWSSPEYGSGFSApkfTSTCSSKSdCSLIIS 98
Cdd:cd04983     1 VTQSPqSLSVQEGENVTLNCNYSTSTFYYLfWYRQYPGQGPQFLIYIS-SDSGNKKKGRFSA---TLDKSRKS-SSLHIS 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207170594  99 NVDVSDSAVYYCQTWDSSVSE-YVFGQGTKLIVT 131
Cdd:cd04983    76 AAQLSDSAVYFCALSESGGTGkLTFGKGTRLTVE 109
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
21-131 1.51e-20

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: 83.57  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQSPV-ITVSKGQTAQLDCNLGTVTNYAA---WYKQTPAEVPQYVLY-NYHGWSSPEygSGFSAPKF-TSTCSSKSDCS 94
Cdd:cd04982     1 LEQPQLsITREESKSVTISCKVSGIDFSTTyihWYRQKPGQALERLLYvSSTSAVRKD--SGKTKNKFeARKDVGKSTST 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207170594  95 LIISNVDVSDSAVYYCQTWDSSVSEY--VFGQGTKLIVT 131
Cdd:cd04982    79 LTITNLEKEDSATYYCAYWESGSGYYikVFGSGTKLIVT 117
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
21-130 5.17e-20

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: 81.94  E-value: 5.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQSPVITVSK-GQTAQLDCNLGTVTNYAAWYKQTPAEVPQYVLYNYHGwSSPEYGsGFSAPKFTSTCSSKSDCSLIISN 99
Cdd:cd05899     1 VTQSPRYLIKRrGQSVTLRCSQKSGHDNMYWYRQDPGKGLQLLFYSYGG-GLNEEG-DLPGDRFSASRPSLTRSSLTIKS 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207170594 100 VDVSDSAVYYC-QTWDSSVSEYVFGQGTKLIV 130
Cdd:cd05899    79 AEPEDSAVYLCaSSLGGGADEAYFGPGTRLTV 110
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
22-131 2.09e-15

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: 69.79  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  22 TQSPVITVSKGQTAQLDC----NLGTVTNYAAWYKQTPAEVPQYVLYNYhgwsSPEYGSGFSAPKFTSTCS-SKSDCSLI 96
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCtyssSMSEASTSVYWYRQPPGKGPTFLIAYY----SNGSEEGVKKGRFSGRGDpSNGDGSLT 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1207170594  97 ISNVDVSDSAVYYCQTWDSsvSEYVFGQGTKLIVT 131
Cdd:pfam07686  77 IQNLTLSDSGTYTCAVIPS--GEGVFGKGTRLTVL 109
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
19-128 5.53e-14

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: 65.87  E-value: 5.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  19 TVVTQSPV-ITVSKGQTAQLDC--NLGTVTNYAAWYKQTPAEVPQYVLYnyhgWSSPEYgSGFSApKFTSTcSSKSDCSL 95
Cdd:cd04980     1 IVMTQSPAsLSVSPGERVTISCkaSQSISSNYLAWYQQKPGQAPKLLIY----YASTLH-SGVPS-RFSGS-GSGTDFTL 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207170594  96 IISNVDVSDSAVYYCQTWDSSVseYVFGQGTKL 128
Cdd:cd04980    74 TISSVEPEDAAVYYCQQGYTFP--YTFGGGTKL 104
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
143-222 6.29e-13

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. 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 strands by G, F, C, and C'.


Pssm-ID: 409354  Cd Length: 95  Bit Score: 62.86  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 143 LRPSSREELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRELTCEAT 222
Cdd:cd00098     4 LLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVT 83
IgC1_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig ...
137-236 2.80e-11

T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the T cell receptor (TCR) beta chain constant immunoglobulin domain. 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 beta chain. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The antigen binding site is formed by the variable domains of the alpha and beta chains, located at the N-terminus of each chain. Alpha/beta TCRs recognize antigens differently from gamma/delta TCRs.


Pssm-ID: 409426 [Multi-domain]  Cd Length: 116  Bit Score: 58.93  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 137 PPVLTILRPSSREELSSSKVTLLCLinhMSVAFAD---VRWLVNGNSVTEGVFTGSAEQQPDHKFKS-SSSLTIQRSEWD 212
Cdd:cd05769     2 PPTVALFPPSEAEIRNKRKATLVCL---ATGFYPDhvsLSWKVNGKEVKDGVATDPQALRENTSTYSlSSRLRVSATEWF 78
                          90       100
                  ....*....|....*....|....*
gi 1207170594 213 K-DRELTCEATVASKTSRASIRKSE 236
Cdd:cd05769    79 NpRNTFTCIVKFYGGTDTDTWTQGI 103
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
21-130 4.98e-11

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: 57.91  E-value: 4.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  21 VTQS-PVITVSKGQTAQLDCNLGTVTN--YAAWYKQTPAEVPQYVLYNYHGWSSPeyGSGFSAPKFTSTCSSksdCSLII 97
Cdd:cd07706     2 VTQAqPDVSVQVGEEVTLNCRYETSWTnyYLFWYKQLPSGEMTFLIRQDSSEQNA--KSGRYSVNFQKAQKS---ISLTI 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207170594  98 SNVDVSDSAVYYCQTWDS-SVSEYVFGQGTKLIV 130
Cdd:cd07706    77 SALQLEDSAKYFCALSLPyDTDKLIFGKGTRLTV 110
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
137-220 2.81e-10

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. 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 is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


Pssm-ID: 409513  Cd Length: 99  Bit Score: 55.48  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 137 PPVLTILRPSSREELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHK--FKSSSSLTIQRSEWDKD 214
Cdd:cd16093     1 PPTVSLHAPSREEFLGNRTATFVCLATGFSPKTISFKWLRNGKEVTSSTGAVVEEPKEDGKtlYSATSFLTITESEWKSQ 80

                  ....*.
gi 1207170594 215 RELTCE 220
Cdd:cd16093    81 TEFTCE 86
C1-set pfam07654
Immunoglobulin C1-set domain;
145-222 6.88e-10

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 54.18  E-value: 6.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207170594 145 PSSREELSSsKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRELTCEAT 222
Cdd:pfam07654   5 PPSPEELGK-PNTLTCLVTGFYPPDITVTWLKNGQEVTEGVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTCRVE 81
IGc1 smart00407
Immunoglobulin C-Type;
155-222 1.49e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 53.09  E-value: 1.49e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207170594  155 KVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRELTCEAT 222
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVT 68
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
138-234 1.45e-08

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second constant domain of the heavy chain of immunoglobulin E (IgE). The basic structure of immunoglobulin (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 is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta, and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). The different classes of antibodies vary in their heavy chains; the IgE class has the epsilon type. This domain (Cepsilon2) of IgE is in place of the flexible hinge region found in IgG.


Pssm-ID: 409434  Cd Length: 97  Bit Score: 50.87  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 138 PVLTILRPSSREELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDREL 217
Cdd:cd05847     1 PTVQILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTY 80
                          90
                  ....*....|....*..
gi 1207170594 218 TCEATVASKTSRASIRK 234
Cdd:cd05847    81 TCKVTHQGTTFEAHTKK 97
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
138-235 1.92e-08

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, and delta chains, and CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, epsilon, and mu chains; member of the C1-set of I; The members here are composed of the third and fourth immunoglobulin constant domain (IgC) of alpha, delta, gamma and alpha, epsilon, and mu heavy chains, respectively. This domain is found on the Fc fragment. 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 is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


Pssm-ID: 409425  Cd Length: 105  Bit Score: 50.80  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 138 PVLTILRPSSREELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQ-PDHKFKSSSSLTIQRSEWDKDRE 216
Cdd:cd05768     1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVPeSDGSFFVYSKLNVSTADWNSGDV 80
                          90       100
                  ....*....|....*....|...
gi 1207170594 217 LTC----EATVASKTSRaSIRKS 235
Cdd:cd05768    81 FSCvvghEALPLQFTQK-SIDKS 102
IGv smart00406
Immunoglobulin V-Type;
34-112 2.02e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 50.07  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594   34 TAQLDCNLGTVTN---YAAWYKQTPAEVPQYVLYnyHGWSSPEYGSGFSAPKFT-STCSSKSDCSLIISNVDVSDSAVYY 109
Cdd:smart00406   1 SVTLSCKFSGSTFssyYVSWVRQPPGKGLEWLGY--IGSNGSSYYQESYKGRFTiSKDTSKNDVSLTISNLRVEDTGTYY 78

                   ...
gi 1207170594  110 CQT 112
Cdd:smart00406  79 CAV 81
IgC1_MHC_II_alpha_HLA_DO cd21004
HLA class II histocompatibility antigen DO alpha; member of the C1-set of Ig superfamily (IgSF) ...
137-199 2.31e-08

HLA class II histocompatibility antigen DO alpha; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the nonclassical MHC class II (MHCII) protein, HLA-DO, which binds HLA-DM and influences the repertoire of peptides presented by MHCII proteins. In complex with HLA-DM, HLA-DO adopts a classical MHCII structure, with alterations near the a subunit's 310 helix. HLA-DO binds to HLA-DM at the same sites implicated in MHCII interaction, and kinetic analysis showed that HLA-DO acts as a competitive inhibitor by acting as a substrate mimic. Though more remains to be elucidated about the function of HLA-DO, its unique distribution in the mammalian body namely, the exclusive expression of HLA-DO in B cells, thymic medullary epithelial cells, and dendritic cells indicate that it may be of physiological importance and has inspired further research. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta-2-microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells.


Pssm-ID: 409595  Cd Length: 95  Bit Score: 50.19  E-value: 2.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207170594 137 PPVLTILrPSSREELSSSKVtLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFK 199
Cdd:cd21004     2 PPRVTVL-PKSRVELGQPNI-LICIVDNIFPPVINITWLRNGQTVTEGVAQTSFYSQPDHLFR 62
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
24-130 2.55e-08

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: 49.81  E-value: 2.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594   24 SPVITVSKGQTAQLDCNL-GTVTNYAAWYKQTPaevpQYVLYNyhgwsspeygsgfsaPKFTSTcSSKSDCSLIISNVDV 102
Cdd:smart00410   1 PPSVTVKEGESVTLSCEAsGSPPPEVTWYKQGG----KLLAES---------------GRFSVS-RSGSTSTLTISNVTP 60
                           90       100
                   ....*....|....*....|....*...
gi 1207170594  103 SDSAVYYCQTWDSSVSEYvfgQGTKLIV 130
Cdd:smart00410  61 EDSGTYTCAATNSSGSAS---SGTTLTV 85
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
23-131 3.41e-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: 47.69  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  23 QSPVITVSKGQTAQLDCNL--GTVTNYA-AWYKQTPAEVPQYVLYNYHGWSSPEYGSGFSApKFT-STCSSKSDCSLIIS 98
Cdd:cd04981     4 ESGPGLVKPGQSLKLSCKAsgFTFTSYGmGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKG-RFTiTRDTSKSTAYLQLN 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1207170594  99 NVDVSDSAVYYCQ---TWDSSVSEYVFGQGTKLIVT 131
Cdd:cd04981    83 SLTSEDTAVYYCArglGGYGYSYFDYWGQGTTVTVS 118
IgC1_MHC_II_alpha_HLA-DQ cd21008
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of ...
157-212 1.31e-05

Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of histocompatibility antigen (HLA) DQ and related proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II alpha chain of histocompatibility antigen (HLA) DQ. MHC class II molecules are encoded by three different loci, HLA-DR, -DQ, and -DP, which are about 70% similar to each other. HLA-DQ (DQ) is a cell surface receptor protein found on antigen presenting cells. It is an alphabeta heterodimer of type MHC class II. The alpha and beta chains are encoded by two loci, HLA-DQA1 and HLA-DQB1, that are adjacent to each other on chromosome band 6p21.3. A person often produces two alpha-chain and two beta chain variants and thus 4 isoforms of DQ. Two autoimmune diseases in which HLA-DQ is involved are celiac disease and diabetes mellitus type 1. DQ is one of several antigens involved in rejection of organ transplants. DQ8 is a split antigen of the DQ3 broad antigen. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409599  Cd Length: 95  Bit Score: 42.63  E-value: 1.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207170594 157 TLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWD 212
Cdd:cd21008    20 TLICLVDNIFPPVINITWLSNGHSVTEGVSETSFLSKSDHSFLKISYLTFLPSADD 75
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
20-130 2.65e-05

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: 42.16  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  20 VVTQSPVITVSKGQTAQLDCNL--GTVTN-YAAWYKQTPAEVPQYVlYNYHGwsspEYGSGFSAPKFTSTCSSKSDCSLI 96
Cdd:cd20988     1 LVPEHQTVTVSVGKPVTLKCSMkgEAISNyYINWYRKTQGNTMTFI-YREGG----IYGPGFKDNFRGDIDSSNNLAVLK 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1207170594  97 ISNVDVSDSAVYYCQTWDSSVSEY----VFGQGTKLIV 130
Cdd:cd20988    76 ILEASERDEGSYYCASDTPGGGREydplIFGKGTYLTV 113
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
23-130 3.02e-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: 42.05  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594  23 QSP-VITVSKGQTAQLDCNLGTVTNYAA--WYKQTPAEVP----QYVLYnyhgWSS---PEYGSGFSAPKFTSTCSSKSD 92
Cdd:cd07700     3 QTPgSLLVQTNQTVKMSCEAKTSPKNTRiyWLRQRQAPSKdshfEFLAS----WDPskgIVYGEGVDQEKLIILSDSDSS 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207170594  93 CS-LIISNVDVSDSAVYYCQTWDSsvSEYVFGQGTKLIV 130
Cdd:cd07700    79 RYiLSLMSVKPEDSGTYFCMTVGS--PELIFGTGTKLSV 115
IgC1_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of ...
137-222 8.53e-04

Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of the major histocompatibility complex (MHC) class II alpha chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are also expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409424  Cd Length: 95  Bit Score: 37.67  E-value: 8.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207170594 137 PPVLTILrPSSREELSSSKvTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDkdrE 216
Cdd:cd05767     2 PPEVTVF-PKSPVELGEPN-TLICFVDNFFPPVINVTWLRNGQPVTDGVSETVFLPREDHSFRKFSYLPFTPSEGD---I 76

                  ....*.
gi 1207170594 217 LTCEAT 222
Cdd:cd05767    77 YDCRVE 82
IgC1_CH2_IgD cd16084
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; ...
142-219 1.57e-03

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin constant domain (IgC) in delta heavy chains. The IgC family includes immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 409506  Cd Length: 97  Bit Score: 37.03  E-value: 1.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207170594 142 ILRPSSREELSSSKVTLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWDKDRELTC 219
Cdd:cd16084     4 LLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81
IgC1_MHC_II_alpha_I-EK cd21005
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of ...
158-212 2.03e-03

Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of histocompatibility antigen (HLA) I-E; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II alpha chain of histocompatibility antigen (HLA) I-E. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409596  Cd Length: 95  Bit Score: 36.57  E-value: 2.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207170594 158 LLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEWD 212
Cdd:cd21005    21 LICFIDKFSPPVVNVTWLRNGRPVTEGVSETVFLPRDDHLFRKFHYLTFLPSTDD 75
IgC1_MHC_II_alpha_HLA-DR cd21007
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of ...
137-199 3.50e-03

Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of histocompatibility antigen (HLA) DR; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II alpha chain of histocompatibility antigen (HLA) DR. MHC class II molecules are encoded by three different loci, HLA-DR, -DQ, and -DP, which are about 70% similar to each other. HLA-DR is a cell surface receptor protein found on antigen presenting cells. It is an alphabeta heterodimer of type MHC class II. The alpha and beta chains are encoded by two loci, HLA-DRA1 and HLA-DRB1, that are adjacent to each other on chromosome band 6p21.31. Susceptibility to multiple sclerosis and rheumatoid arthritis are associated with the human histocompatibility leukocyte antigen HLA-DR2 and HLA-DR4, respectively. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409598  Cd Length: 95  Bit Score: 35.80  E-value: 3.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207170594 137 PPVLTILrPSSREELSSSKVtLLCLINHMSVAFADVRWLVNGNSVTEGVFTGSAEQQPDHKFK 199
Cdd:cd21007     2 PPEVTVL-TNSPVELREPNV-LICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFR 62
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
137-211 7.97e-03

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and gamma chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin constant-1 set domain of epsilon and gamma chains. It belongs to a family composed of the first immunoglobulin constant-1 set domain of alpha, delta, epsilon, gamma, and mu heavy chains. This domain is found on the Fab antigen-binding fragment. 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 is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors.


Pssm-ID: 409622  Cd Length: 94  Bit Score: 34.73  E-value: 7.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207170594 137 PPVLTILRPSSREElSSSKVTLLCLINHMSVAFADVRWlvNGNSVTEGVFTGSAEQQPDHKFKSSSSLTIQRSEW 211
Cdd:cd21817     1 APSVFPLAPCCKST-NGSSVTLGCLVTGYFPEPVTVTW--NSGSLTSGVKTFPAVLQSSGLYTTSSQVTVPSSSW 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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