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Conserved domains on  [gi|22219245|pdb|1LK3|I]
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Chain I, 9D7 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 ...
 4-118 2.51e-57

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: 177.12  E-value: 2.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQSGAALVKPGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGYTNYNEKFKNKATLTVDKSTSTGYMEL 83
Cdd:cd04981   2 LQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQL 81

                        90       100       110
                ....*....|....*....|....*....|....*..
1LK3_I       84 SRLTSEDSANYSCTRG--VPGNNWFPYWGQGTLVTVS 118
Cdd:cd04981  82 NSLTSEDTAVYYCARGlgGYGYSYFDYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 124-216 3.72e-49

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: 155.68  E-value: 3.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQ-SGLYTLTSSVTVPSSTWPSQTVTCN 202
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
1LK3_I      203 VAHPASSTKVDKKI 216
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 ...
 4-118 2.51e-57

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: 177.12  E-value: 2.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQSGAALVKPGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGYTNYNEKFKNKATLTVDKSTSTGYMEL 83
Cdd:cd04981   2 LQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQL 81

                        90       100       110
                ....*....|....*....|....*....|....*..
1LK3_I       84 SRLTSEDSANYSCTRG--VPGNNWFPYWGQGTLVTVS 118
Cdd:cd04981  82 NSLTSEDTAVYYCARGlgGYGYSYFDYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 124-216 3.72e-49

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: 155.68  E-value: 3.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQ-SGLYTLTSSVTVPSSTWPSQTVTCN 202
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
1LK3_I      203 VAHPASSTKVDKKI 216
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
IGv smart00406
Immunoglobulin V-Type;
17-98 6.78e-26

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 95.91  E-value: 6.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I          17 SVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNsGYTNYNEKFKNKATLTVDKSTSTGYMELSRLTSEDSANYSC 96
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSN-GSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   ..
1LK3_I          97 TR 98
Cdd:smart00406  80 AV 81
C1-set pfam07654
Immunoglobulin C1-set domain;
127-208 9.96e-19

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 77.29  E-value: 9.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        127 VYPLAPGTALKSNSmVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQS-GLYTLTSSVTVPSSTWPS-QTVTCN 202
Cdd:pfam07654   1 VYVFPPSPEELGKP-NTLTCLVTGFYPPDITVTWlkNGQEVTEGVKTTPPSPNSdWTYQLSSYLTVTPSDWESgDEYTCR 79


                  ....*.
1LK3_I        203 VAHPAS 208
Cdd:pfam07654  80 VEHEGL 85
IGc1 smart00407
Immunoglobulin C-Type;
142-209 7.01e-14

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 64.26  E-value: 7.01e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1LK3_I         142 VTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQS-GLYTLTSSVTVPSSTW-PSQTVTCNVAHPASS 209
Cdd:smart00407   2 ATLVCLVSGFYPPDITVTWlrNGQEVTEGVSTTDPLKNSdGTYFLSSYLTVPASTWeSGDVYTCQVTHEGLK 73
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 11-117 9.07e-08

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: 48.99  E-value: 9.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I         11 LVKPGASVKLSCKASGYTFTD-FYIHWVKQSHGKSLEWIGYInpnsgYTNYNEKFKNKA--TLTVDKSTSTGYMELSRLT 87
Cdd:pfam07686   7 TVALGGSVTLPCTYSSSMSEAsTSVYWYRQPPGKGPTFLIAY-----YSNGSEEGVKKGrfSGRGDPSNGDGSLTIQNLT 81

                          90       100       110
                  ....*....|....*....|....*....|
1LK3_I         88 SEDSANYSCTRGVPGNNwfpYWGQGTLVTV 117
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEG---VFGKGTRLTV 108
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 4-118 2.51e-57

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: 177.12  E-value: 2.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQSGAALVKPGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGYTNYNEKFKNKATLTVDKSTSTGYMEL 83
Cdd:cd04981   2 LQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQL 81

                        90       100       110
                ....*....|....*....|....*....|....*..
1LK3_I       84 SRLTSEDSANYSCTRG--VPGNNWFPYWGQGTLVTVS 118
Cdd:cd04981  82 NSLTSEDTAVYYCARGlgGYGYSYFDYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 124-216 3.72e-49

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: 155.68  E-value: 3.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQ-SGLYTLTSSVTVPSSTWPSQTVTCN 202
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
1LK3_I      203 VAHPASSTKVDKKI 216
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 124-216 2.06e-29

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: 105.36  E-value: 2.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTW---NSGALSSGVHTFPAVLQS-GLYTLTSSVTVPSSTWPS-QT 198
Cdd:cd04985   1 APTVFPLQSATKSQSNGPVALGCLISDYFPESITVSWqknTNSITSGFTRTFPVVLRSgGDYSCSSQLTVPLQEWNSgEV 80

                        90
                ....*....|....*...
1LK3_I      199 VTCNVAHPASSTKVDKKI 216
Cdd:cd04985  81 YKCQVQHSASNSKQEKDV 98
IGv smart00406
Immunoglobulin V-Type;
17-98 6.78e-26

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 95.91  E-value: 6.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I          17 SVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNsGYTNYNEKFKNKATLTVDKSTSTGYMELSRLTSEDSANYSC 96
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSN-GSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   ..
1LK3_I          97 TR 98
Cdd:smart00406  80 AV 81
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 124-213 4.46e-20

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: 81.22  E-value: 4.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTAlKSNSMVTLGCLVKGYFPEPVTVTWNSG--ALSSGVHTFPAVLQSGLYTLTSSVTVPSSTWPSQT-VT 200
Cdd:cd21819   1 APTLFPLVSCGS-STSDPVTVGCLATDFLPDSITFSWTDDnnSLTTGVKTYPSVLTGGTYTASSQLQVPESEWKSKEnFY 79

                        90
                ....*....|...
1LK3_I      201 CNVAHPASSTKVD 213
Cdd:cd21819  80 CKVEHPGGNKEVP 92
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 4-117 4.62e-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: 78.92  E-value: 4.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQSGAAL-VKPGASVKLSCKASGyTFTDFYIHWVKQSHGKSLEWIGYINpnSGYTNYNEKFKNKATLTVDKSTStGYME 82
Cdd:cd00099   1 VTQSPRSLsVQEGESVTLSCEVSS-SFSSTYIYWYRQKPGQGPEFLIYLS--SSKGKTKGGVPGRFSGSRDGTSS-FSLT 76

                        90       100       110
                ....*....|....*....|....*....|....*
1LK3_I       83 LSRLTSEDSANYSCTRGVPGNNWFPYWGQGTLVTV 117
Cdd:cd00099  77 ISNLQPEDSGTYYCAVSESGGTDKLTFGSGTRLTV 111
C1-set pfam07654
Immunoglobulin C1-set domain;
127-208 9.96e-19

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 77.29  E-value: 9.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        127 VYPLAPGTALKSNSmVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQS-GLYTLTSSVTVPSSTWPS-QTVTCN 202
Cdd:pfam07654   1 VYVFPPSPEELGKP-NTLTCLVTGFYPPDITVTWlkNGQEVTEGVKTTPPSPNSdWTYQLSSYLTVTPSDWESgDEYTCR 79


                  ....*.
1LK3_I        203 VAHPAS 208
Cdd:pfam07654  80 VEHEGL 85
IgC1_CH1_IgA cd21818
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 125-213 2.11e-17

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: 74.08  E-value: 2.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      125 PSVYPLAPGTALKSNSmVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSG-LYTLTSSVTVPSSTWP-SQTVTCN 202
Cdd:cd21818   2 PTVFPLSLCPSLSSDP-VVIGCLVQGFFPEPVNVTWNYSGKGGTARNFPAMLASGgRYTQSSQLTLPADQCPeGEAYKCS 80

                        90
                ....*....|.
1LK3_I      203 VAHPASSTKVD 213
Cdd:cd21818  81 VQHYSPSQDLN 91
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 126-216 9.10e-17

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: 72.49  E-value: 9.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      126 SVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQS-GLYTLTSSVTVPSSTWPSQ-TVTC 201
Cdd:cd00098   1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWlkNGVPLTSGVSTSSPVEPNdGTYSVTSSLTVPPSDWDEGaTYTC 80

                        90
                ....*....|....*
1LK3_I      202 NVAHPASSTKVDKKI 216
Cdd:cd00098  81 VVTHESLKSPLSKTW 95
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 125-219 1.69e-14

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: 66.98  E-value: 1.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      125 PSVYPLAPGT-ALKSNSMVTLGCLVKGYFPEPVTVTW--NSGALSSGVH--TFPAVLQSGLYTLTSSVTVPSSTWPS-QT 198
Cdd:cd05768   1 PSVYLLPPPEeELSLNETVTLTCLVKGFYPEDIFVSWlqNGEPLPSADYktTAPVPESDGSFFVYSKLNVSTADWNSgDV 80

                        90       100
                ....*....|....*....|.
1LK3_I      199 VTCNVAHPASSTKVDKKIVPR 219
Cdd:cd05768  81 FSCVVGHEALPLQFTQKSIDK 101
IGc1 smart00407
Immunoglobulin C-Type;
142-209 7.01e-14

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 64.26  E-value: 7.01e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1LK3_I         142 VTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQS-GLYTLTSSVTVPSSTW-PSQTVTCNVAHPASS 209
Cdd:smart00407   2 ATLVCLVSGFYPPDITVTWlrNGQEVTEGVSTTDPLKNSdGTYFLSSYLTVPASTWeSGDVYTCQVTHEGLK 73
IgC1_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 124-211 9.67e-14

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: 64.48  E-value: 9.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTAL-KSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSGLYTLTSS-VTVPSSTWPSQTVTC 201
Cdd:cd16092   1 APDVFPIISGCRHpKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSqLSTPLQQWRQGEYKC 80

                        90
                ....*....|
1LK3_I      202 NVAHPASSTK 211
Cdd:cd16092  81 VVQHTASKSK 90
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 14-118 5.41e-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: 57.76  E-value: 5.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I       14 PGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGYTNYNEKFKNK--ATLTVDKSTSTgyMELSRLTSEDS 91
Cdd:cd04982  12 ESKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYVSSTSAVRKDSGKTKNKfeARKDVGKSTST--LTITNLEKEDS 89

                        90       100
                ....*....|....*....|....*...
1LK3_I       92 ANYSCTRGVPGNN-WFPYWGQGTLVTVS 118
Cdd:cd04982  90 ATYYCAYWESGSGyYIKVFGSGTKLIVT 117
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 15-117 3.43e-10

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: 55.35  E-value: 3.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I       15 GASVKLSCKASGYTFTdfYIHWVKQSHGKSLEWIGYInpnsgYTNYNEKFKNKATLTVDKSTSTGYMELSRLTSEDSANY 94
Cdd:cd04983  13 GENVTLNCNYSTSTFY--YLFWYRQYPGQGPQFLIYI-----SSDSGNKKKGRFSATLDKSRKSSSLHISAAQLSDSAVY 85

                        90       100
                ....*....|....*....|...
1LK3_I       95 SCTRGVPGNNWFPYWGQGTLVTV 117
Cdd:cd04983  86 FCALSESGGTGKLTFGKGTRLTV 108
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 4-117 1.06e-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: 54.00  E-value: 1.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQSGAALVKPGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGyTNYNEKFKNKatltvdKSTSTGYMEL 83
Cdd:cd04984   2 LTQPSSLSVSPGETVTITCTGSSGNISGNYVNWYQQKPGSAPRYLIYEDKHRP-SGIPDRFSGS------KSGNTASLTI 74

                        90       100       110
                ....*....|....*....|....*....|....
1LK3_I       84 SRLTSEDSANYSCTRGVPGNNWFpywGQGTLVTV 117
Cdd:cd04984  75 SGAQTEDEADYYCQVWDSNSYVF---GGGTKLTV 105
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 11-117 1.11e-09

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: 53.28  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I          11 LVKPGASVKLSCKASGytFTDFYIHWVKQShgksLEWIGYinpnsgytnynekfknKATLTVDKSTSTGYMELSRLTSED 90
Cdd:smart00410   5 TVKEGESVTLSCEASG--SPPPEVTWYKQG----GKLLAE----------------SGRFSVSRSGSTSTLTISNVTPED 62

                           90       100
                   ....*....|....*....|....*..
1LK3_I          91 SANYSCTRgvpGNNWFPYWGqGTLVTV 117
Cdd:smart00410  63 SGTYTCAA---TNSSGSASS-GTTLTV 85
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 11-117 1.27e-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: 51.13  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I       11 LVKPGASVKLSC-KASGYTftdfYIHWVKQSHGKSLEWIGYINpnSGYTNYNEKFKNKATLTVDKSTSTGYMELSRLTSE 89
Cdd:cd05899   9 IKRRGQSVTLRCsQKSGHD----NMYWYRQDPGKGLQLLFYSY--GGGLNEEGDLPGDRFSASRPSLTRSSLTIKSAEPE 82

                        90       100
                ....*....|....*....|....*...
1LK3_I       90 DSANYSCTRGVPGNNWFPYWGQGTLVTV 117
Cdd:cd05899  83 DSAVYLCASSLGGGADEAYFGPGTRLTV 110
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 125-210 1.30e-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: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      125 PSVYPLAPGTA-LKSNSMVTLGCLVKGYFPEPVTVTW---NSGALSSGVHTFPAVLQSGLYTLTSSVTVPSSTWPSQ-TV 199
Cdd:cd05847   1 PTVQILHSSCAsTLTSETIQLLCLISGYTPSTIEVEWlvdGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGkTY 80

                        90
                ....*....|.
1LK3_I      200 TCNVAHPASST 210
Cdd:cd05847  81 TCKVTHQGTTF 91
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 124-216 3.43e-08

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: 49.76  E-value: 3.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQSG-LYTLTSSVTVPSSTWPS-QTV 199
Cdd:cd07699   1 APSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWkvDGSTVSSGVTTSKTEQQSDnTYSMSSYLTLSSSDWNKhKVY 80

                        90
                ....*....|....*..
1LK3_I      200 TCNVAHPASSTKVDKKI 216
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 ...
 123-205 3.51e-08

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: 50.07  E-value: 3.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      123 TAPSVYPLAPGTA-LKSNSMVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQSG--LYTLTSSVTVPSSTW--P 195
Cdd:cd05769   1 TPPTVALFPPSEAeIRNKRKATLVCLATGFYPDHVSLSWkvNGKEVKDGVATDPQALRENtsTYSLSSRLRVSATEWfnP 80

                        90
                ....*....|
1LK3_I      196 SQTVTCNVAH 205
Cdd:cd05769  81 RNTFTCIVKF 90
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 11-117 9.07e-08

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: 48.99  E-value: 9.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I         11 LVKPGASVKLSCKASGYTFTD-FYIHWVKQSHGKSLEWIGYInpnsgYTNYNEKFKNKA--TLTVDKSTSTGYMELSRLT 87
Cdd:pfam07686   7 TVALGGSVTLPCTYSSSMSEAsTSVYWYRQPPGKGPTFLIAY-----YSNGSEEGVKKGrfSGRGDPSNGDGSLTIQNLT 81

                          90       100       110
                  ....*....|....*....|....*....|
1LK3_I         88 SEDSANYSCTRGVPGNNwfpYWGQGTLVTV 117
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEG---VFGKGTRLTV 108
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 125-210 3.97e-07

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: 46.62  E-value: 3.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      125 PSVYPLAPG-TALKSNSMVTLGCLVKGYFPEPVTVTW--NSGALSS--GVHTFPAVLQSG-LYTLTSSVTVPSSTWPSQT 198
Cdd:cd16093   2 PTVSLHAPSrEEFLGNRTATFVCLATGFSPKTISFKWlrNGKEVTSstGAVVEEPKEDGKtLYSATSFLTITESEWKSQT 81

                        90
                ....*....|...
1LK3_I      199 -VTCNVAHPASST 210
Cdd:cd16093  82 eFTCEFKHKGEIV 94
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 130-212 6.57e-06

Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain on Tapasin-R. Tapasin is a V-C1 (variable-constant) immunoglobulin superfamily molecule present in the endoplasmic reticulum (ER), where it links MHC class I molecules to the transporter associated with antigen processing (TAP). Tapasin-R is a tapasin-related protein that contains similar structural motifs to Tapasin, with some marked differences, especially in the V domain, transmembrane and cytoplasmic regions. The majority of Tapasin-R is located within the ER; however, there may be some expression of Tapasin-R at the cell surface. Tapasin-R lacks an obvious ER retention signal.


Pssm-ID: 409428  Cd Length: 100  Bit Score: 43.64  E-value: 6.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      130 LAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFP---AVLQS------GLYTLTSSVTVPSSTWPS-QTV 199
Cdd:cd05771   5 LSPKNLVKPDLPQTLSCHIAGYYPLDVDVEWLREEPGGSESQVSrdgVSLSShrqsvdGTYSISSYLTLEPGTENRgATY 84

                        90
                ....*....|...
1LK3_I      200 TCNVAHPASSTKV 212
Cdd:cd05771  85 TCRVTHVSLEEPL 97
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 4-96 2.81e-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: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQS-GAALVKPGASVKLSCKASGYTfTDFYIHWVKQSHGKS----LEWIGYINPNSGYTNYNEKFKNKATLTVDKSTST 78
Cdd:cd07700   1 LLQTpGSLLVQTNQTVKMSCEAKTSP-KNTRIYWLRQRQAPSkdshFEFLASWDPSKGIVYGEGVDQEKLIILSDSDSSR 79

                        90
                ....*....|....*...
1LK3_I       79 GYMELSRLTSEDSANYSC 96
Cdd:cd07700  80 YILSLMSVKPEDSGTYFC 97
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 2-113 3.17e-05

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: 41.61  E-value: 3.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        2 VNLLQSGAAL-VKPGASVKLSCKASGyTFTDFYIHWVKQSHGKSLEWIGYinpnsgYTNynekfkNKATLTVDKSTSTGY 80
Cdd:cd04980   1 IVMTQSPASLsVSPGERVTISCKASQ-SISSNYLAWYQQKPGQAPKLLIY------YAS------TLHSGVPSRFSGSGS 67

                        90       100       110
                ....*....|....*....|....*....|....*....
1LK3_I       81 -----MELSRLTSEDSANYSCTRGvpgnNWFPY-WGQGT 113
Cdd:cd04980  68 gtdftLTISSVEPEDAAVYYCQQG----YTFPYtFGGGT 102
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 4-100 3.33e-05

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: 41.78  E-value: 3.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I        4 LLQSGAALVKPGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGYTNynekfKNKATLTVDKSTSTGYMEL 83
Cdd:cd16095   4 LEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSLDHISTKVS-----EDRITSSREDTNSQIFLQI 78

                        90
                ....*....|....*..
1LK3_I       84 SRLTSEDSANYSCTRGV 100
Cdd:cd16095  79 KGLGLRDSGQYHCARRV 95
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 142-210 4.52e-04

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 38.17  E-value: 4.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1LK3_I        142 VTLGCLVKGYFPEPvTVTW--NSGALSSGVHTFPAVLQSGLYTLTSSVTV-PSSTWPSQTVTCNVAHPASST 210
Cdd:pfam08205  17 VVATCSSAGGKPAP-RITWylDGKPLEAAETSSEQDPESGLVTVTSELKLvPSRSDHGQSLTCQVSYGALRG 87
IgC1_MHC_II_beta_HLA-DM cd21002
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of ...
 122-209 6.02e-04

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: 37.98  E-value: 6.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      122 TTAPSVYpLAPGTALKSNSMVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTFPAVLQSGLYTLTSSVTVPSSTWPSQTV 199
Cdd:cd21002   1 RRPPSVR-VAPTTPFNTREPVMLACHVWGFYPADVTITWlkNGDPVAPHSSAPKTAQPNGDWTYQTQVTLAVTPSPGDTY 79

                        90
                ....*....|
1LK3_I      200 TCNVAHPASS 209
Cdd:cd21002  80 TCSVQHASLP 89
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 12-117 2.11e-03

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: 36.73  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I       12 VKPGASVKLSCKASgYTFTDFYIHWVKQSHGKSLEWIgyINPNSGYTN-----YNEKFKnkatltvdKSTSTGYMELSRL 86
Cdd:cd07706  11 VQVGEEVTLNCRYE-TSWTNYYLFWYKQLPSGEMTFL--IRQDSSEQNaksgrYSVNFQ--------KAQKSISLTISAL 79

                        90       100       110
                ....*....|....*....|....*....|.
1LK3_I       87 TSEDSANYSCTRGVPGNNWFPYWGQGTLVTV 117
Cdd:cd07706  80 QLEDSAKYFCALSLPYDTDKLIFGKGTRLTV 110
IgC1_CD1 cd21029
Immunoglobulin domain of Cluster of Differentiation (CD) 1; member of the C1-set of Ig ...
 124-218 3.05e-03

Immunoglobulin domain of Cluster of Differentiation (CD) 1; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin domain of Cluster of Differentiation (CD) 1. CD1 family of transmembrane glycoproteins, are structurally related to the major histocompatibility complex (MHC) proteins and form heterodimers with beta-2-microglobulin. They mediate the presentation of primarily lipid and glycolipid antigens of self or microbial origin to T cells. The human genome contains five CD1 family genes (CD1a, CD1b, CD1c, CD1d, and CD1e) organized in a cluster on chromosome 1. The CD1 family members are thought to differ in their cellular localization and specificity for particular lipid ligands. CD1a localizes to the plasma membrane and to recycling vesicles of the early endocytic system. Alternative splicing results in multiple transcript variants. Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. 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. C1-set Ig domains 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: 409620  Cd Length: 93  Bit Score: 35.76  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      124 APSVYPLAPGTALKSNsmVTLGCLVKGYFPEPVTVTW--NSGALSSGVHTfPAVLQS--GLYTLTSSVTVPSSTwpSQTV 199
Cdd:cd21029   2 KPRVRLSSRPSPGDGH--LQLSCHVTGFYPRPIEVTWlrDGQEQMDGTQS-GGILPNhdGTYQLRKTLDIAPGE--GAGY 76

                        90
                ....*....|....*....
1LK3_I      200 TCNVAHpasSTKVDKKIVP 218
Cdd:cd21029  77 SCRVDH---SSLKQDLIVY 92
IgC1_MHC_II_beta_HLA-DR cd21000
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of ...
 126-212 3.48e-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: 35.75  E-value: 3.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      126 SVYPLAPGTALKSNSMVtlgCLVKGYFPEPVTVTW--NSGALSSGVHTfPAVLQSGLYTLTSSV---TVPSStwpSQTVT 200
Cdd:cd21000   7 TVYPAKTQPLQHHNLLV---CSVNGFYPGSIEVRWfrNGQEEKAGVVS-TGLIQNGDWTFQTLVmleTVPRS---GEVYT 79

                        90
                ....*....|..
1LK3_I      201 CNVAHPASSTKV 212
Cdd:cd21000  80 CQVEHPSVTSPL 91
IgC1_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of ...
 127-205 5.34e-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: 34.98  E-value: 5.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LK3_I      127 VYPLAPGTALKSNsmvTLGCLVKGYFPEPVTVTW--NSGALSSGV-HTFPAVLQSGLYTLTSSVT-VPSstwPSQTVTCN 202
Cdd:cd05767   7 VFPKSPVELGEPN---TLICFVDNFFPPVINVTWlrNGQPVTDGVsETVFLPREDHSFRKFSYLPfTPS---EGDIYDCR 80


                ...
1LK3_I      203 VAH 205
Cdd:cd05767  81 VEH 83
IgC1_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain, alpha3 immunoglobulin domain; ...
 138-210 9.05e-03

Class I major histocompatibility complex (MHC) alpha chain, alpha3 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 I alpha chain. 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: 409495  Cd Length: 92  Bit Score: 34.51  E-value: 9.05e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1LK3_I      138 SNSMVTLGCLVKGYFPEPVTVTW-----NSGALSSGVHTFPAvlQSGLYTLTSSVTVPSSTWpsQTVTCNVAHPASST 210
Cdd:cd07698  13 SDGESTLRCWALGFYPAEITLTWqrdgeDQTQDMELVETRPN--GDGTFQKWAAVVVPSGEE--QRYTCHVQHEGLPE 86
 
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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