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Conserved domains on  [gi|1065171|pdb|1MLC|D]
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Chain D, IGG1-KAPPA D44.1 FAB (HEAVY CHAIN)

Protein Classification

Graphical summary

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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 ...
 3-115 9.21e-67

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: 201.00  E-value: 9.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        3 QLQESGAEVMKPGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEILPGSGSTYYNEKFKGKATFTADTSSNTAYMQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*...
1MLC_D       83 LSSLTSEDSAVYYCARGDGNYG-----YWGQGTTLTVS 115
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYGysyfdYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 121-213 1.45e-43

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: 141.43  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      121 PPSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ-SDLYTLSSSVTVPSSPRPSETVTCN 199
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
1MLC_D      200 VAHPASSTKVDKKI 213
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 ...
 3-115 9.21e-67

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: 201.00  E-value: 9.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        3 QLQESGAEVMKPGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEILPGSGSTYYNEKFKGKATFTADTSSNTAYMQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*...
1MLC_D       83 LSSLTSEDSAVYYCARGDGNYG-----YWGQGTTLTVS 115
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYGysyfdYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 121-213 1.45e-43

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: 141.43  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      121 PPSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ-SDLYTLSSSVTVPSSPRPSETVTCN 199
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
1MLC_D      200 VAHPASSTKVDKKI 213
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
IGv smart00406
Immunoglobulin V-Type;
17-98 7.00e-31

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 108.62  E-value: 7.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D          17 SVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEIlPGSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAVYYC 96
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYI-GSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   ..
1MLC_D          97 AR 98
Cdd:smart00406  80 AV 81
C1-set pfam07654
Immunoglobulin C1-set domain;
124-205 8.21e-15

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 66.89  E-value: 8.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        124 VFPLAPgSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSS-VTVPSSPRPSETVTCN 199
Cdd:pfam07654   1 VYVFPP-SPEELGKPNTLTCLVTGFYPPDITVTWlkNGQEVTEGVKTTPPSPNSDwTYQLSSYlTVTPSDWESGDEYTCR 79


                  ....*.
1MLC_D        200 VAHPAS 205
Cdd:pfam07654  80 VEHEGL 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 15-114 2.95e-12

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 60.93  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D         15 GASVKISCKATGYTFS-TYWIEWVKQRPGHGLEWigEILpGSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAV 93
Cdd:pfam07686  11 GGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTF--LIA-YYSNGSEEGVKKGRFSGRGDPSNGDGSLTIQNLTLSDSGT 87

                          90       100
                  ....*....|....*....|.
1MLC_D         94 YYCARGDGNYGYWGQGTTLTV 114
Cdd:pfam07686  88 YTCAVIPSGEGVFGKGTRLTV 108
IGc1 smart00407
Immunoglobulin C-Type;
139-206 1.29e-08

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 50.00  E-value: 1.29e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MLC_D         139 VTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSDL--YTLSSSVTVPSSPRPSETVTCNVAHPASS 206
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 ...
 3-115 9.21e-67

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: 201.00  E-value: 9.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        3 QLQESGAEVMKPGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEILPGSGSTYYNEKFKGKATFTADTSSNTAYMQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*...
1MLC_D       83 LSSLTSEDSAVYYCARGDGNYG-----YWGQGTTLTVS 115
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYGysyfdYWGQGTTVTVS 118
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 121-213 1.45e-43

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: 141.43  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      121 PPSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ-SDLYTLSSSVTVPSSPRPSETVTCN 199
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQsSGLYTTSSQVTVPSSSWGSQTFTCN 80

                        90
                ....*....|....
1MLC_D      200 VAHPASSTKVDKKI 213
Cdd:cd21817  81 VEHKPSSTKVDKKI 94
IGv smart00406
Immunoglobulin V-Type;
17-98 7.00e-31

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 108.62  E-value: 7.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D          17 SVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEIlPGSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAVYYC 96
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYI-GSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   ..
1MLC_D          97 AR 98
Cdd:smart00406  80 AV 81
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 5-114 3.82e-23

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 89.70  E-value: 3.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        5 QESGAEVMKPGASVKISCKATGyTFSTYWIEWVKQRPGHGLEWIGEIlpGSGSTYYNEKFKGKATFTADtSSNTAYMQLS 84
Cdd:cd00099   3 QSPRSLSVQEGESVTLSCEVSS-SFSSTYIYWYRQKPGQGPEFLIYL--SSSKGKTKGGVPGRFSGSRD-GTSSFSLTIS 78

                        90       100       110
                ....*....|....*....|....*....|...
1MLC_D       85 SLTSEDSAVYYCARGDGNYG---YWGQGTTLTV 114
Cdd:cd00099  79 NLQPEDSGTYYCAVSESGGTdklTFGSGTRLTV 111
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 122-213 8.80e-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: 88.42  E-value: 8.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      122 PSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW---NSGSLSSGVHTFPAVLQSD-LYTLSSSVTVPSSPRPS-ETV 196
Cdd:cd04985   2 PTVFPLQSATKSQSNGPVALGCLISDYFPESITVSWqknTNSITSGFTRTFPVVLRSGgDYSCSSQLTVPLQEWNSgEVY 81

                        90
                ....*....|....*..
1MLC_D      197 TCNVAHPASSTKVDKKI 213
Cdd:cd04985  82 KCQVQHSASNSKQEKDV 98
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 14-115 3.49e-17

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: 74.32  E-value: 3.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D       14 PGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEILPGSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAV 93
Cdd:cd04982  12 ESKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYVSSTSAVRKDSGKTKNKFEARKDVGKSTSTLTITNLEKEDSAT 91

                        90       100
                ....*....|....*....|....*.
1MLC_D       94 YYCARGDGNYGYW----GQGTTLTVS 115
Cdd:cd04982  92 YYCAYWESGSGYYikvfGSGTKLIVT 117
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 5-114 6.10e-16

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: 70.57  E-value: 6.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        5 QESGAEVmKPGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEILPGSGSTYynekfkgKATFTADTSSNTAYMQLS 84
Cdd:cd04984   4 QPSSLSV-SPGETVTITCTGSSGNISGNYVNWYQQKPGSAPRYLIYEDKHRPSGI-------PDRFSGSKSGNTASLTIS 75

                        90       100       110
                ....*....|....*....|....*....|
1MLC_D       85 SLTSEDSAVYYCARGDGNYGYWGQGTTLTV 114
Cdd:cd04984  76 GAQTEDEADYYCQVWDSNSYVFGGGTKLTV 105
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 11-114 6.75e-15

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: 68.08  E-value: 6.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D       11 VMKPGASVKISCKAT-GYtfstYWIEWVKQRPGHGLEWIGEiLPGSGSTYYNEKFKGKatFTADTSSNTAY-MQLSSLTS 88
Cdd:cd05899   9 IKRRGQSVTLRCSQKsGH----DNMYWYRQDPGKGLQLLFY-SYGGGLNEEGDLPGDR--FSASRPSLTRSsLTIKSAEP 81

                        90       100
                ....*....|....*....|....*....
1MLC_D       89 EDSAVYYCA---RGDGNYGYWGQGTTLTV 114
Cdd:cd05899  82 EDSAVYLCAsslGGGADEAYFGPGTRLTV 110
C1-set pfam07654
Immunoglobulin C1-set domain;
124-205 8.21e-15

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 66.89  E-value: 8.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        124 VFPLAPgSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSS-VTVPSSPRPSETVTCN 199
Cdd:pfam07654   1 VYVFPP-SPEELGKPNTLTCLVTGFYPPDITVTWlkNGQEVTEGVKTTPPSPNSDwTYQLSSYlTVTPSDWESGDEYTCR 79


                  ....*.
1MLC_D        200 VAHPAS 205
Cdd:pfam07654  80 VEHEGL 85
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 15-114 2.10e-14

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 66.53  E-value: 2.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D       15 GASVKISCKATgyTFSTYWIEWVKQRPGHGLEWIGeilpgSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAVY 94
Cdd:cd04983  13 GENVTLNCNYS--TSTFYYLFWYRQYPGQGPQFLI-----YISSDSGNKKKGRFSATLDKSRKSSSLHISAAQLSDSAVY 85

                        90       100
                ....*....|....*....|...
1MLC_D       95 YCA-RGDGNYG--YWGQGTTLTV 114
Cdd:cd04983  86 FCAlSESGGTGklTFGKGTRLTV 108
IgC1_CH1_IgA cd21818
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 122-210 8.61e-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: 64.45  E-value: 8.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      122 PSVFPLAPGSAaQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQS-DLYTLSSSVTVPSSPRP-SETVTCN 199
Cdd:cd21818   2 PTVFPLSLCPS-LSSDPVVIGCLVQGFFPEPVNVTWNYSGKGGTARNFPAMLASgGRYTQSSQLTLPADQCPeGEAYKCS 80

                        90
                ....*....|.
1MLC_D      200 VAHPASSTKVD 210
Cdd:cd21818  81 VQHYSPSQDLN 91
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 121-210 1.41e-13

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: 63.89  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      121 PPSVFPLAPGSAAqTNSMVTLGCLVKGYFPEPVTVTWNSG--SLSSGVHTFPAVLQSDLYTLSSSVT-VPSSPRPSETVT 197
Cdd:cd21819   1 APTLFPLVSCGSS-TSDPVTVGCLATDFLPDSITFSWTDDnnSLTTGVKTYPSVLTGGTYTASSQLQvPESEWKSKENFY 79

                        90
                ....*....|...
1MLC_D      198 CNVAHPASSTKVD 210
Cdd:cd21819  80 CKVEHPGGNKEVP 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 11-114 6.90e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 62.14  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D          11 VMKPGASVKISCKATGytFSTYWIEWVKQrpghGLEWIGEilpgsgstyynekfkgKATFTADTSSNTAYMQLSSLTSED 90
Cdd:smart00410   5 TVKEGESVTLSCEASG--SPPPEVTWYKQ----GGKLLAE----------------SGRFSVSRSGSTSTLTISNVTPED 62

                           90       100
                   ....*....|....*....|....
1MLC_D          91 SAVYYCARGDGNYGYWGqGTTLTV 114
Cdd:smart00410  63 SGTYTCAATNSSGSASS-GTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 15-114 2.95e-12

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 60.93  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D         15 GASVKISCKATGYTFS-TYWIEWVKQRPGHGLEWigEILpGSGSTYYNEKFKGKATFTADTSSNTAYMQLSSLTSEDSAV 93
Cdd:pfam07686  11 GGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTF--LIA-YYSNGSEEGVKKGRFSGRGDPSNGDGSLTIQNLTLSDSGT 87

                          90       100
                  ....*....|....*....|.
1MLC_D         94 YYCARGDGNYGYWGQGTTLTV 114
Cdd:pfam07686  88 YTCAVIPSGEGVFGKGTRLTV 108
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 123-213 4.29e-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: 57.47  E-value: 4.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      123 SVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSS-VTVPSSPRPSETVTC 198
Cdd:cd00098   1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWlkNGVPLTSGVSTSSPVEPNDgTYSVTSSlTVPPSDWDEGATYTC 80

                        90
                ....*....|....*
1MLC_D      199 NVAHPASSTKVDKKI 213
Cdd:cd00098  81 VVTHESLKSPLSKTW 95
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 1-114 9.06e-10

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: 54.49  E-value: 9.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        1 QVQLQESGAEVMKPGASVKISCKATGYTFSTYWIEWVKQRPGHGLEWIGEIlpGSGSTYYNEkfkGKATFTADTSSNTAY 80
Cdd:cd16095   1 ETQLEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSL--DHISTKVSE---DRITSSREDTNSQIF 75

                        90       100       110
                ....*....|....*....|....*....|....*....
1MLC_D       81 MQLSSLTSEDSAVYYCARGDGNYG-----YWGQGTTLTV 114
Cdd:cd16095  76 LQIKGLGLRDSGQYHCARRVGYGDdtdklIFGPGTDVIV 114
IgC1_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 122-208 1.05e-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: 53.69  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      122 PSVFPLAPGSA-AQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSE-TVTCN 199
Cdd:cd16092   2 PDVFPIISGCRhPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQgEYKCV 81


                ....*....
1MLC_D      200 VAHPASSTK 208
Cdd:cd16092  82 VQHTASKSK 90
IGc1 smart00407
Immunoglobulin C-Type;
139-206 1.29e-08

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 50.00  E-value: 1.29e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MLC_D         139 VTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSDL--YTLSSSVTVPSSPRPSETVTCNVAHPASS 206
Cdd:smart00407   2 ATLVCLVSGFYPPDITVTWlrNGQEVTEGVSTTDPLKNSDGtyFLSSYLTVPASTWESGDVYTCQVTHEGLK 73
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 4-114 1.62e-07

Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409497  Cd Length: 116  Bit Score: 48.21  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        4 LQESGAEVMKPGASVKISCKATGYTFSTYwIEWVKQRPGHGLEWIGEIL----PGSGSTYYNEKFKGKATFTADTSSNTA 79
Cdd:cd07700   2 LQTPGSLLVQTNQTVKMSCEAKTSPKNTR-IYWLRQRQAPSKDSHFEFLaswdPSKGIVYGEGVDQEKLIILSDSDSSRY 80

                        90       100       110
                ....*....|....*....|....*....|....*
1MLC_D       80 YMQLSSLTSEDSAVYYCARGDGNYGYWGQGTTLTV 114
Cdd:cd07700  81 ILSLMSVKPEDSGTYFCMTVGSPELIFGTGTKLSV 115
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 122-218 1.05e-06

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: 45.79  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      122 PSVFPLAPGSAAQT-NSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVH--TFPAVLQSDLYTLSSSVTVPSSPRPS-ET 195
Cdd:cd05768   1 PSVYLLPPPEEELSlNETVTLTCLVKGFYPEDIFVSWlqNGEPLPSADYktTAPVPESDGSFFVYSKLNVSTADWNSgDV 80

                        90       100
                ....*....|....*....|...
1MLC_D      196 VTCNVAHPASSTKVDKKIVPRDC 218
Cdd:cd05768  81 FSCVVGHEALPLQFTQKSIDKSP 103
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 121-213 2.78e-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: 44.37  E-value: 2.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      121 PPSVFPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD-LYTLSSSVTVPSSPRPS-ETV 196
Cdd:cd07699   1 APSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWkvDGSTVSSGVTTSKTEQQSDnTYSMSSYLTLSSSDWNKhKVY 80

                        90
                ....*....|....*..
1MLC_D      197 TCNVAHPASSTKVDKKI 213
Cdd:cd07699  81 TCEVTHEGLSSTITKSF 97
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 2-114 1.21e-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: 42.76  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        2 VQLQESGAEVM-KPGASVKISCKATGyTFSTYWIEWVKQRPGHglewIGEILPGSGSTYYN---EKFKGKATFTADTssn 77
Cdd:cd04980   1 IVMTQSPASLSvSPGERVTISCKASQ-SISSNYLAWYQQKPGQ----APKLLIYYASTLHSgvpSRFSGSGSGTDFT--- 72

                        90       100       110
                ....*....|....*....|....*....|....*..
1MLC_D       78 tayMQLSSLTSEDSAVYYCARGDGNYGYWGQGTTLTV 114
Cdd:cd04980  73 ---LTISSVEPEDAAVYYCQQGYTFPYTFGGGTKLEI 106
IgC1_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig ...
 120-202 3.78e-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: 41.59  E-value: 3.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      120 TPPSVFPLAPGSAAQTNS-MVTLGCLVKGYFPEPVTVTW--NSGSLSSGVHTFPAVLQSD--LYTLSS--SVTVPSSPRP 192
Cdd:cd05769   1 TPPTVALFPPSEAEIRNKrKATLVCLATGFYPDHVSLSWkvNGKEVKDGVATDPQALRENtsTYSLSSrlRVSATEWFNP 80

                        90
                ....*....|
1MLC_D      193 SETVTCNVAH 202
Cdd:cd05769  81 RNTFTCIVKF 90
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 15-114 5.38e-05

Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409580  Cd Length: 114  Bit Score: 41.39  E-value: 5.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D       15 GASVKISCKATGYTFSTYWIEWVKQRPGHGLEWI----GEILPGsgstyYNEKFKGKatftADTSSNTAYMQLSSLTSED 90
Cdd:cd20988  13 GKPVTLKCSMKGEAISNYYINWYRKTQGNTMTFIyregGIYGPG-----FKDNFRGD----IDSSNNLAVLKILEASERD 83

                        90       100       110
                ....*....|....*....|....*....|
1MLC_D       91 SAVYYCAR----GDGNYG--YWGQGTTLTV 114
Cdd:cd20988  84 EGSYYCASdtpgGGREYDplIFGKGTYLTV 113
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 5-114 6.95e-05

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: 40.97  E-value: 6.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D        5 QESGAEVMKPGASVKISCK-ATGYTfsTYWIEWVKQRPGHGLEWigeiLPGSGSTYYNEKfKGKATFTADTSSNTAYMQL 83
Cdd:cd07706   4 QAQPDVSVQVGEEVTLNCRyETSWT--NYYLFWYKQLPSGEMTF----LIRQDSSEQNAK-SGRYSVNFQKAQKSISLTI 76

                        90       100       110
                ....*....|....*....|....*....|....
1MLC_D       84 SSLTSEDSAVYYCA---RGDGNYGYWGQGTTLTV 114
Cdd:cd07706  77 SALQLEDSAKYFCAlslPYDTDKLIFGKGTRLTV 110
IgC1_MHC_II_beta_HLA-DM cd21002
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of ...
 119-157 1.10e-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: 37.21  E-value: 1.10e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
1MLC_D      119 TTPPSV--FPLAPGSaaqTNSMVTLGCLVKGYFPEPVTVTW 157
Cdd:cd21002   1 RRPPSVrvAPTTPFN---TREPVMLACHVWGFYPADVTITW 38
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 15-96 2.18e-03

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: 36.66  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D       15 GASVKISCKatgYTFS-----TYWIEWVKQRPGHGLEWIgeILPGSGSTY--YNEKFKGKATFTADTSSNTAYMQLSSLT 87
Cdd:cd20960  15 GENVTLPCH---HQLGledqgTLDIEWLLLPSDKVEKVV--ITYSGDRVYnhYYPALKGRVAFTSNDLSGDASLNISNLK 89


                ....*....
1MLC_D       88 SEDSAVYYC 96
Cdd:cd20960  90 LSDTGTYQC 98
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 122-207 2.24e-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: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MLC_D      122 PSVFPLAPGSA-AQTNSMVTLGCLVKGYFPEPVTVTW---NSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSE-TV 196
Cdd:cd05847   1 PTVQILHSSCAsTLTSETIQLLCLISGYTPSTIEVEWlvdGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGkTY 80

                        90
                ....*....|.
1MLC_D      197 TCNVAHPASST 207
Cdd:cd05847  81 TCKVTHQGTTF 91
IgC1_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of ...
 124-169 2.32e-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: 36.13  E-value: 2.32e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
1MLC_D      124 VFPLAPGSAAQTNsmvTLGCLVKGYFPEPVTVTW--NSGSLSSGV-HTF 169
Cdd:cd05767   7 VFPKSPVELGEPN---TLICFVDNFFPPVINVTWlrNGQPVTDGVsETV 52
IgC1_MHC_II_alpha_HLA_DO cd21004
HLA class II histocompatibility antigen DO alpha; member of the C1-set of Ig superfamily (IgSF) ...
 120-179 9.48e-03

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


Pssm-ID: 409595  Cd Length: 95  Bit Score: 34.40  E-value: 9.48e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1MLC_D      120 TPPSV--FPLAPGSAAQTNSMVtlgCLVKGYFPEPVTVTWnsgsLSSGVHTFPAVLQSDLYT 179
Cdd:cd21004   1 VPPRVtvLPKSRVELGQPNILI---CIVDNIFPPVINITW----LRNGQTVTEGVAQTSFYS 55
 
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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