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Conserved domains on  [gi|1127249]
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Chain H, OPG2 FAB (HEAVY CHAIN)

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 3-124 7.52e-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: 194.07  E-value: 7.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    3 QLVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 1127249   83 MSSLRSEDTALYYCTRHPFYRYdggnYYAMDHWGQGTSVTVS 124
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYG----YSYFDYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 130-222 5.22e-46

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: 147.98  E-value: 5.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  130 PPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ-SDLYTLSSSVTVPSSPRPSETVTCN 208
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
gi 1127249  209 VAHPASSTKVDKKI 222
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 3-124 7.52e-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: 194.07  E-value: 7.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    3 QLVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 1127249   83 MSSLRSEDTALYYCTRHPFYRYdggnYYAMDHWGQGTSVTVS 124
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYG----YSYFDYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 130-222 5.22e-46

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: 147.98  E-value: 5.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  130 PPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ-SDLYTLSSSVTVPSSPRPSETVTCN 208
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
gi 1127249  209 VAHPASSTKVDKKI 222
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
IGv smart00406
Immunoglobulin V-Type;
17-98 6.54e-32

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 111.32  E-value: 6.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249      17 SLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIhYPDSVKGRFTISRDNAKNNLYLQMSSLRSEDTALYYC 96
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSY-YQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   ..
gi 1127249      97 TR 98
Cdd:smart00406  80 AV 81
C1-set pfam07654
Immunoglobulin C1-set domain;
133-214 1.63e-15

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 69.20  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    133 VYPLAPgSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSS-VTVPSSPRPSETVTCN 208
Cdd:pfam07654   1 VYVFPP-SPEELGKPNTLTCLVTGFYPPDITVTWlkNGQEVTEGVKTTPPSPNSDwTYQLSSYlTVTPSDWESGDEYTCR 79


                  ....*.
gi 1127249    209 VAHPAS 214
Cdd:pfam07654  80 VEHEGL 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 11-123 2.42e-09

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: 53.23  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249     11 LVNPGRSLKLSCAASGFTFS-SYGMSWVRQTPEKRLEWVAAISGGGTYihyPDSVKGRFTISRDNAKNNLYLQMSSLRSE 89
Cdd:pfam07686   7 TVALGGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTFLIAYYSNGSE---EGVKKGRFSGRGDPSNGDGSLTIQNLTLS 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1127249     90 DTALYYCTRHPFYrydggnyyaMDHWGQGTSVTV 123
Cdd:pfam07686  84 DSGTYTCAVIPSG---------EGVFGKGTRLTV 108
IGc1 smart00407
Immunoglobulin C-Type;
148-215 5.33e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 51.16  E-value: 5.33e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1127249     148 VTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSDL--YTLSSSVTVPSSPRPSETVTCNVAHPASS 215
Cdd:smart00407   2 ATLVCLVSGFYPPDITVTWlrNGQEVTEGVSTTDPLKNSDGtyFLSSYLTVPASTWESGDVYTCQVTHEGLK 73
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 3-124 7.52e-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: 194.07  E-value: 7.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    3 QLVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 1127249   83 MSSLRSEDTALYYCTRHPFYRYdggnYYAMDHWGQGTSVTVS 124
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYG----YSYFDYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 130-222 5.22e-46

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: 147.98  E-value: 5.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  130 PPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ-SDLYTLSSSVTVPSSPRPSETVTCN 208
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
gi 1127249  209 VAHPASSTKVDKKI 222
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
IGv smart00406
Immunoglobulin V-Type;
17-98 6.54e-32

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 111.32  E-value: 6.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249      17 SLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIhYPDSVKGRFTISRDNAKNNLYLQMSSLRSEDTALYYC 96
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSY-YQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   ..
gi 1127249      97 TR 98
Cdd:smart00406  80 AV 81
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 131-222 1.49e-23

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, epsilon, gamma, and mu chains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are 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: 409374  Cd Length: 98  Bit Score: 90.34  E-value: 1.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  131 PSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW---NSGSLSSGVHTFPAVLQSD-LYTLSSSVTVPSSPRPS-ETV 205
Cdd:cd04985   2 PTVFPLQSATKSQSNGPVALGCLISDYFPESITVSWqknTNSITSGFTRTFPVVLRSGgDYSCSSQLTVPLQEWNSgEVY 81

                        90
                ....*....|....*..
gi 1127249  206 TCNVAHPASSTKVDKKI 222
Cdd:cd04985  82 KCQVQHSASNSKQEKDV 98
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 4-123 1.33e-19

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: 80.46  E-value: 1.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    4 LVQSGGGL-VNPGRSLKLSCAASGFtFSSYGMSWVRQTPEKRLEWVaaISGGGTYIHYPDSVKGRFTISRDNAKnNLYLQ 82
Cdd:cd00099   1 VTQSPRSLsVQEGESVTLSCEVSSS-FSSTYIYWYRQKPGQGPEFL--IYLSSSKGKTKGGVPGRFSGSRDGTS-SFSLT 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 1127249   83 MSSLRSEDTALYYCTrhpfyRYDGGNYYaMDHWGQGTSVTV 123
Cdd:cd00099  77 ISNLQPEDSGTYYCA-----VSESGGTD-KLTFGSGTRLTV 111
C1-set pfam07654
Immunoglobulin C1-set domain;
133-214 1.63e-15

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 69.20  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    133 VYPLAPgSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSS-VTVPSSPRPSETVTCN 208
Cdd:pfam07654   1 VYVFPP-SPEELGKPNTLTCLVTGFYPPDITVTWlkNGQEVTEGVKTTPPSPNSDwTYQLSSYlTVTPSDWESGDEYTCR 79


                  ....*.
gi 1127249    209 VAHPAS 214
Cdd:pfam07654  80 VEHEGL 85
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 1-123 8.99e-15

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: 67.97  E-value: 8.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    1 EVQLVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTyihypDSVKGRFTISRDNAKNNLY 80
Cdd:cd16095   1 ETQLEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSLDHIST-----KVSEDRITSSREDTNSQIF 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 1127249   81 LQMSSLRSEDTALYYCTRhpfyRYDGGNYYAMDHWGQGTSVTV 123
Cdd:cd16095  76 LQIKGLGLRDSGQYHCAR----RVGYGDDTDKLIFGPGTDVIV 114
IgC1_CH1_IgA cd21818
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 131-219 7.06e-14

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha 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 alpha chains. It belongs to a family composed of the first immunoglobulin constant-1 set domain of alpha, 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: 409623  Cd Length: 94  Bit Score: 64.83  E-value: 7.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  131 PSVYPLAPGSAaQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQS-DLYTLSSSVTVPSSPRP-SETVTCN 208
Cdd:cd21818   2 PTVFPLSLCPS-LSSDPVVIGCLVQGFFPEPVNVTWNYSGKGGTARNFPAMLASgGRYTQSSQLTLPADQCPeGEAYKCS 80

                        90
                ....*....|.
gi 1127249  209 VAHPASSTKVD 219
Cdd:cd21818  81 VQHYSPSQDLN 91
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 130-219 8.98e-14

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu 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 mu 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: 409624  Cd Length: 95  Bit Score: 64.66  E-value: 8.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  130 PPSVYPLAPGSAAqTNSMVTLGCLVKGYFPEPVTVTWNSG--SLSSGVHTFPAVLQSDLYTLSSSVT-VPSSPRPSETVT 206
Cdd:cd21819   1 APTLFPLVSCGSS-TSDPVTVGCLATDFLPDSITFSWTDDnnSLTTGVKTYPSVLTGGTYTASSQLQvPESEWKSKENFY 79

                        90
                ....*....|...
gi 1127249  207 CNVAHPASSTKVD 219
Cdd:cd21819  80 CKVEHPGGNKEVP 92
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 132-222 1.18e-11

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: 59.01  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  132 SVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSS-VTVPSSPRPSETVTC 207
Cdd:cd00098   1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWlkNGVPLTSGVSTSSPVEPNDgTYSVTSSlTVPPSDWDEGATYTC 80

                        90
                ....*....|....*
gi 1127249  208 NVAHPASSTKVDKKI 222
Cdd:cd00098  81 VVTHESLKSPLSKTW 95
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 14-124 1.49e-11

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: 59.30  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   14 PGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQMSSLRSEDTAL 93
Cdd:cd04982  12 ESKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYVSSTSAVRKDSGKTKNKFEARKDVGKSTSTLTITNLEKEDSAT 91

                        90       100       110
                ....*....|....*....|....*....|.
gi 1127249   94 YYCTRhpfYRYDGGNYYAMdhWGQGTSVTVS 124
Cdd:cd04982  92 YYCAY---WESGSGYYIKV--FGSGTKLIVT 117
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 7-123 2.15e-11

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: 58.29  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249       7 SGGGLVNPGRSLKLSCAASGFtfSSYGMSWVRQtpekRLEWVAAisgggtyihypdsvKGRFTISRDNakNNLYLQMSSL 86
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGS--PPPEVTWYKQ----GGKLLAE--------------SGRFSVSRSG--STSTLTISNV 58

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1127249      87 RSEDTALYYCTRHPfyryDGGNYYAmdhwgqGTSVTV 123
Cdd:smart00410  59 TPEDSGTYTCAATN----SSGSASS------GTTLTV 85
IgC1_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 131-217 1.59e-09

CH1 domain (first 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 first immunoglobulin constant-1 set domain of delta 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: 319341  Cd Length: 96  Bit Score: 53.30  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  131 PSVYPLAPGSA-AQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSE-TVTCN 208
Cdd:cd16092   2 PDVFPIISGCRhPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQgEYKCV 81


                ....*....
gi 1127249  209 VAHPASSTK 217
Cdd:cd16092  82 VQHTASKSK 90
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 11-123 2.42e-09

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: 53.23  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249     11 LVNPGRSLKLSCAASGFTFS-SYGMSWVRQTPEKRLEWVAAISGGGTYihyPDSVKGRFTISRDNAKNNLYLQMSSLRSE 89
Cdd:pfam07686   7 TVALGGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTFLIAYYSNGSE---EGVKKGRFSGRGDPSNGDGSLTIQNLTLS 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1127249     90 DTALYYCTRHPFYrydggnyyaMDHWGQGTSVTV 123
Cdd:pfam07686  84 DSGTYTCAVIPSG---------EGVFGKGTRLTV 108
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 4-123 2.88e-09

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: 52.85  E-value: 2.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    4 LVQSGGGLVNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVAAISGggtyiHYPDSVKGRFTISRDNakNNLYLQM 83
Cdd:cd04984   2 LTQPSSLSVSPGETVTITCTGSSGNISGNYVNWYQQKPGSAPRYLIYEDK-----HRPSGIPDRFSGSKSG--NTASLTI 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 1127249   84 SSLRSEDTALYYCTrhpfyRYDGGNYYamdhWGQGTSVTV 123
Cdd:cd04984  75 SGAQTEDEADYYCQ-----VWDSNSYV----FGGGTKLTV 105
IGc1 smart00407
Immunoglobulin C-Type;
148-215 5.33e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 51.16  E-value: 5.33e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1127249     148 VTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSDL--YTLSSSVTVPSSPRPSETVTCNVAHPASS 215
Cdd:smart00407   2 ATLVCLVSGFYPPDITVTWlrNGQEVTEGVSTTDPLKNSDGtyFLSSYLTVPASTWESGDVYTCQVTHEGLK 73
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 11-123 8.69e-08

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: 48.82  E-value: 8.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   11 LVNPGRSLKLSCAAsgfTFSSYGMSWVRQTPEKRLEWVAAISGGGTYihYPDSVKG-RFTISRDNAKNnLYLQMSSLRSE 89
Cdd:cd05899   9 IKRRGQSVTLRCSQ---KSGHDNMYWYRQDPGKGLQLLFYSYGGGLN--EEGDLPGdRFSASRPSLTR-SSLTIKSAEPE 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 1127249   90 DTALYYCTRHPfyryDGGNYYAmdHWGQGTSVTV 123
Cdd:cd05899  83 DSAVYLCASSL----GGGADEA--YFGPGTRLTV 110
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 131-227 1.02e-07

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: 48.49  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  131 PSVYPLAPGSAAQT-NSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVH--TFPAVLQSDLYTLSSSVTVPSSPRPS-ET 204
Cdd:cd05768   1 PSVYLLPPPEEELSlNETVTLTCLVKGFYPEDIFVSWlqNGEPLPSADYktTAPVPESDGSFFVYSKLNVSTADWNSgDV 80

                        90       100
                ....*....|....*....|...
gi 1127249  205 VTCNVAHPASSTKVDKKIVPRDC 227
Cdd:cd05768  81 FSCVVGHEALPLQFTQKSIDKSP 103
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 12-123 9.89e-07

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: 46.11  E-value: 9.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   12 VNPGRSLKLSCAASgfTFSSYGMSWVRQTPEKRLEWVAAISGGGTyihypDSVKGRFTISRDNAKNNLYLQMSSLRSEDT 91
Cdd:cd04983  10 VQEGENVTLNCNYS--TSTFYYLFWYRQYPGQGPQFLIYISSDSG-----NKKKGRFSATLDKSRKSSSLHISAAQLSDS 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 1127249   92 ALYYCTRHPFYRYDggNYYamdhWGQGTSVTV 123
Cdd:cd04983  83 AVYFCALSESGGTG--KLT----FGKGTRLTV 108
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 130-222 1.56e-06

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: 45.14  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  130 PPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSSVTVPSSPRPS-ETV 205
Cdd:cd07699   1 APSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWkvDGSTVSSGVTTSKTEQQSDnTYSMSSYLTLSSSDWNKhKVY 80

                        90
                ....*....|....*..
gi 1127249  206 TCNVAHPASSTKVDKKI 222
Cdd:cd07699  81 TCEVTHEGLSSTITKSF 97
IgC1_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig ...
 129-211 1.50e-05

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: 42.75  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  129 TPPSVYPLAPGSAAQTNS-MVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD--LYTLSS--SVTVPSSPRP 201
Cdd:cd05769   1 TPPTVALFPPSEAEIRNKrKATLVCLATGFYPDHVSLSWkvNGKEVKDGVATDPQALRENtsTYSLSSrlRVSATEWFNP 80

                        90
                ....*....|
gi 1127249  202 SETVTCNVAH 211
Cdd:cd05769  81 RNTFTCIVKF 90
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 11-96 2.48e-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: 42.44  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   11 LVNPGRSLKLSCAASGFTfSSYGMSWVRQ----TPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQMSSL 86
Cdd:cd07700   9 LVQTNQTVKMSCEAKTSP-KNTRIYWLRQrqapSKDSHFEFLASWDPSKGIVYGEGVDQEKLIILSDSDSSRYILSLMSV 87

                        90
                ....*....|
gi 1127249   87 RSEDTALYYC 96
Cdd:cd07700  88 KPEDSGTYFC 97
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 2-96 1.60e-04

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: 39.68  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249    2 VQLVQSGGGL-VNPGRSLKLSCAASGfTFSSYGMSWVRQTP---EKRLewvaaISGGGTYIhypDSVKGRFTISrdNAKN 77
Cdd:cd04980   1 IVMTQSPASLsVSPGERVTISCKASQ-SISSNYLAWYQQKPgqaPKLL-----IYYASTLH---SGVPSRFSGS--GSGT 69

                        90
                ....*....|....*....
gi 1127249   78 NLYLQMSSLRSEDTALYYC 96
Cdd:cd04980  70 DFTLTISSVEPEDAAVYYC 88
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 12-123 1.86e-04

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: 39.85  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   12 VNPGRSLKLSCAASGFTFSSYGMSWVRQTPEKRLEWVaaISGGGTyihYPDSVKGRFTISRDNAKNNLYLQMSSLRSEDT 91
Cdd:cd20988  10 VSVGKPVTLKCSMKGEAISNYYINWYRKTQGNTMTFI--YREGGI---YGPGFKDNFRGDIDSSNNLAVLKILEASERDE 84

                        90       100       110
                ....*....|....*....|....*....|...
gi 1127249   92 ALYYC-TRHPFyrydGGNYYAMDHWGQGTSVTV 123
Cdd:cd20988  85 GSYYCaSDTPG----GGREYDPLIFGKGTYLTV 113
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 15-96 2.08e-04

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 39.74  E-value: 2.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   15 GRSLKLSCAasgFTFSSYG-----MSWVRQTPEKRLEWVAAISGGGTYIHYPDSVKGRFTISRDNAKNNLYLQMSSLRSE 89
Cdd:cd20960  15 GENVTLPCH---HQLGLEDqgtldIEWLLLPSDKVEKVVITYSGDRVYNHYYPALKGRVAFTSNDLSGDASLNISNLKLS 91


                ....*..
gi 1127249   90 DTALYYC 96
Cdd:cd20960  92 DTGTYQC 98
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 29-123 3.51e-04

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: 39.04  E-value: 3.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249   29 FSSYGMSWVRQTPEKRLEWVaaISGGGTYIhypDSVKGRFTISRDNAKNNLYLQMSSLRSEDTALYYCTRHPFYRYDGGN 108
Cdd:cd07706  27 WTNYYLFWYKQLPSGEMTFL--IRQDSSEQ---NAKSGRYSVNFQKAQKSISLTISALQLEDSAKYFCALSLPYDTDKLI 101

                        90
                ....*....|....*
gi 1127249  109 YyamdhwGQGTSVTV 123
Cdd:cd07706 102 F------GKGTRLTV 110
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 131-216 2.62e-03

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: 36.24  E-value: 2.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  131 PSVYPLAPGSA-AQTNSMVTLGCLVKGYFPEPVTVTW---NSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSE-TV 205
Cdd:cd05847   1 PTVQILHSSCAsTLTSETIQLLCLISGYTPSTIEVEWlvdGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGkTY 80

                        90
                ....*....|.
gi 1127249  206 TCNVAHPASST 216
Cdd:cd05847  81 TCKVTHQGTTF 91
IgC1_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of ...
 130-178 3.02e-03

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: 35.75  E-value: 3.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 1127249  130 PP--SVYPLAPGSAAQTNsmvTLGCLVKGYFPEPVTVTW--NSGSLSSGV-HTF 178
Cdd:cd05767   2 PPevTVFPKSPVELGEPN---TLICFVDNFFPPVINVTWlrNGQPVTDGVsETV 52
IgC1_MHC_II_beta_HLA-DM cd21002
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of ...
 128-166 4.27e-03

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of histocompatibility antigen (HLA) DM; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of histocompatibility antigen (HLA) DM. Human HLA-DM plays a critical role in antigen presentation to CD4 T cells by catalyzing the exchange of peptides bound to MHC class II molecules. Type 1 diabetes is correlated with DM activation and it is also implicated in viral infections such as herpes simplex virus, celiac disease, multiple sclerosis, other autoimmune diseases, and leukemia. 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: 409593  Cd Length: 97  Bit Score: 35.67  E-value: 4.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 1127249  128 TTPPSV--YPLAPGSaaqTNSMVTLGCLVKGYFPEPVTVTW 166
Cdd:cd21002   1 RRPPSVrvAPTTPFN---TREPVMLACHVWGFYPADVTITW 38
IgC1_MHC_II_beta_HLA-DR cd21000
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of ...
 120-218 4.63e-03

Class II major histocompatibility complex (MHC) beta 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 Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of histocompatibility antigen (HLA) DR. HLA-DR is an MHC class II cell surface receptor encoded by the human leukocyte antigen complex on chromosome 6 region 6p21.31. HLA-DR is also involved in several autoimmune conditions, disease susceptibility, and disease resistance including seronegative-rheumatoid arthritis, penicillamine-induced myasthenia, schizophrenia, Goodpasture syndrome, systemic lupus erythematosus, Alzheimers, tuberculoid leprosy, and Hashimoto's thyroiditis. HLA-DR molecules are upregulated in response to signaling. HLA-DR is an alphabeta heterodimer cell surface receptor, each subunit of which contains two extracellular domains, a membrane-spanning domain, and a cytoplasmic tail. Both alpha and beta chains are anchored in the membrane. The DR beta chain is encoded by 4 loci, however no more than 3 functional loci are present in a single individual, and no more than two on a single chromosome. Sometimes an individual may only possess 2 copies of the same locus, DRB1*. The HLA-DRB1 locus is ubiquitous and encodes a very large number of functionally variable gene products (HLA-DR1 to HLA-DR17). The HLA-DRB3 locus encodes the HLA-DR52 specificity, is moderately variable and is variably associated with certain HLA-DRB1 types. The HLA-DRB4 locus encodes the HLA-DR53 specificity, has some variation, and is associated with certain HLA-DRB1 types. The HLA-DRB5 locus encodes the HLA-DR51 specificity, which is typically invariable, and is linked to the HLA-DR2 types. Three genetically distinct isotypes of class II MHC molecules are found in humans (HLA-DR, HLA-DQ, and HLA-DP), and two in mice (I-E and I-A). 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: 409591  Cd Length: 96  Bit Score: 35.36  E-value: 4.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  120 SVTVSAAKTTPPSVYPLapgsaaqtnsmvtLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSDlYTLSSSVTVPS 197
Cdd:cd21000   5 KVTVYPAKTQPLQHHNL-------------LVCSVNGFYPGSIEVRWfrNGQEEKAGVVSTGLIQNGD-WTFQTLVMLET 70

                        90       100
                ....*....|....*....|.
gi 1127249  198 SPRPSETVTCNVAHPASSTKV 218
Cdd:cd21000  71 VPRSGEVYTCQVEHPSVTSPL 91
IgC1_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of ...
 120-212 8.22e-03

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; 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 beta 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 has 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: 409423  Cd Length: 96  Bit Score: 34.62  E-value: 8.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127249  120 SVTVSAAKTTPPSVYPLapgsaaqtnsmvtLGCLVKGYFPEPVTVTW--NSGSLSSGV-HTFpaVLQSDLYTLSSSVTVP 196
Cdd:cd05766   5 SVKVSPTKTGPLEHPNL-------------LVCSVTGFYPAEIEVKWfrNGQEETAGVvSTE--LIPNGDWTFQILVMLE 69

                        90
                ....*....|....*.
gi 1127249  197 SSPRPSETVTCNVAHP 212
Cdd:cd05766  70 TTPRRGDVYTCQVEHS 85
 
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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