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Conserved domains on  [gi|82407640|pdb|1ZVO|C]
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Chain C, Immunoglobulin delta heavy chain

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgC1_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 134-229 4.85e-65

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: 205.84  E-value: 4.85e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      134 APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 213
Cdd:cd16092   1 APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 80

                        90
                ....*....|....*.
1ZVO_C      214 VVQHTASKSKKEIFRW 229
Cdd:cd16092  81 VVQHTASKSKKEIFRW 96
IgC1_CH3_IgD cd16094
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 403-502 9.15e-62

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily domains; The members here are composed of the third immunoglobulin constant domain (IgC) of delta 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. 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: 319343  Cd Length: 100  Bit Score: 197.38  E-value: 9.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      403 KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATY 482
Cdd:cd16094   1 KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATY 80

                        90       100
                ....*....|....*....|
1ZVO_C      483 TCVVSHEDSRTLLNASRSLE 502
Cdd:cd16094  81 TCVVSHEDSRTLLNASRSLE 100
IgC1_CH2_IgD cd16084
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; ...
 298-394 2.01e-61

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


:

Pssm-ID: 409506  Cd Length: 97  Bit Score: 196.50  E-value: 2.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      298 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 377
Cdd:cd16084   1 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 80

                        90
                ....*....|....*..
1ZVO_C      378 CTLNHPSLPPQRLMALR 394
Cdd:cd16084  81 CTLNHPSLPPQRLMALR 97
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 3-128 1.78e-59

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: 191.75  E-value: 1.78e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        3 QLQESGPGLVKPSETLSLTCIVSGGPIrrTGYYWGWIRQPPGKGLEWIGGVYY-TGSIYYNPSLRGRVTISVDTSRNQFS 81
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTF--TSYGMGWVRQAPGKGLEWIGLIYPgGGDTYYADSFKGRFTITRDTSKSTAY 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1ZVO_C       82 LNLRSMSAADTAMYYCARGNPPPYYdigtgsdDGIDVWGQGTTVHVS 128
Cdd:cd04981  79 LQLNSLTSEDTAVYYCARGLGGYGY-------SYFDYWGQGTTVTVS 118
 
Name Accession Description Interval E-value
IgC1_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 134-229 4.85e-65

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: 205.84  E-value: 4.85e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      134 APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 213
Cdd:cd16092   1 APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 80

                        90
                ....*....|....*.
1ZVO_C      214 VVQHTASKSKKEIFRW 229
Cdd:cd16092  81 VVQHTASKSKKEIFRW 96
IgC1_CH3_IgD cd16094
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 403-502 9.15e-62

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily domains; The members here are composed of the third immunoglobulin constant domain (IgC) of delta 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. 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: 319343  Cd Length: 100  Bit Score: 197.38  E-value: 9.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      403 KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATY 482
Cdd:cd16094   1 KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATY 80

                        90       100
                ....*....|....*....|
1ZVO_C      483 TCVVSHEDSRTLLNASRSLE 502
Cdd:cd16094  81 TCVVSHEDSRTLLNASRSLE 100
IgC1_CH2_IgD cd16084
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; ...
 298-394 2.01e-61

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


Pssm-ID: 409506  Cd Length: 97  Bit Score: 196.50  E-value: 2.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      298 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 377
Cdd:cd16084   1 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 80

                        90
                ....*....|....*..
1ZVO_C      378 CTLNHPSLPPQRLMALR 394
Cdd:cd16084  81 CTLNHPSLPPQRLMALR 97
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 3-128 1.78e-59

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: 191.75  E-value: 1.78e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        3 QLQESGPGLVKPSETLSLTCIVSGGPIrrTGYYWGWIRQPPGKGLEWIGGVYY-TGSIYYNPSLRGRVTISVDTSRNQFS 81
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTF--TSYGMGWVRQAPGKGLEWIGLIYPgGGDTYYADSFKGRFTITRDTSKSTAY 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1ZVO_C       82 LNLRSMSAADTAMYYCARGNPPPYYdigtgsdDGIDVWGQGTTVHVS 128
Cdd:cd04981  79 LQLNSLTSEDTAVYYCARGLGGYGY-------SYFDYWGQGTTVTVS 118
IGv smart00406
Immunoglobulin V-Type;
17-99 7.26e-29

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 109.01  E-value: 7.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C          17 TLSLTCIVSGGPIrrTGYYWGWIRQPPGKGLEWIGGVYYTGSIYYNPSLRGRVTISVDTSRNQFSLNLRSMSAADTAMYY 96
Cdd:smart00406   1 SVTLSCKFSGSTF--SSYYVSWVRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYY 78


                   ...
1ZVO_C          97 CAR 99
Cdd:smart00406  79 CAV 81
C1-set pfam07654
Immunoglobulin C1-set domain;
137-220 3.97e-20

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 84.61  E-value: 3.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        137 VFPiisgcRHPKD-NSPVVLACLITGYHPTSVTVTWYMGTQSQPQ--RTFPEIQRRDSYYMTSSQLSTPLQQWRQGE-YK 212
Cdd:pfam07654   3 VFP-----PSPEElGKPNTLTCLVTGFYPPDITVTWLKNGQEVTEgvKTTPPSPNSDWTYQLSSYLTVTPSDWESGDeYT 77


                  ....*...
1ZVO_C        213 CVVQHTAS 220
Cdd:pfam07654  78 CRVEHEGL 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 5-127 9.02e-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: 61.71  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C          5 QESGPGLVKPSETLSLTCIVSGGPIRRTGYYWgWIRQPPGKGLEWIggVYYTGSIYYNPSLRGRVTISVDTSRNQFSLNL 84
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVY-WYRQPPGKGPTFL--IAYYSNGSEEGVKKGRFSGRGDPSNGDGSLTI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
1ZVO_C         85 RSMSAADTAMYYCARGNPPpyydigtgsddgIDVWGQGTTVHV 127
Cdd:pfam07686  78 QNLTLSDSGTYTCAVIPSG------------EGVFGKGTRLTV 108
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 302-393 2.28e-11

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 59.90  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        302 LTPAVQDLWLRDKATFTCFVVGSDlKDAHLTWEVAGKVPTggveEGLLERHSNGSQSQHSRLTLPRSLWNAGTsVTCTLN 381
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGS-PGPDVTWSKEGGTLI----ESLKVKHDNGRTTQSSLLISNVTKEDAGT-YTCVVN 74

                          90
                  ....*....|..
1ZVO_C        382 HPSLPPQRLMAL 393
Cdd:pfam00047  75 NPGGSATLSTSL 86
IGc1 smart00407
Immunoglobulin C-Type;
421-489 6.09e-10

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 55.40  E-value: 6.09e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZVO_C         421 LLCEVSGFSPPNILLMWLEDQREVnTSGFAPARPPPQpGSTTFWAWSVLRVPAPPSPQPATYTCVVSHE 489
Cdd:smart00407   4 LVCLVSGFYPPDITVTWLRNGQEV-TEGVSTTDPLKN-SDGTYFLSSYLTVPASTWESGDVYTCQVTHE 70
IGc1 smart00407
Immunoglobulin C-Type;
314-388 4.22e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 53.09  E-value: 4.22e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZVO_C         314 KATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPPQ 388
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75
IGc1 smart00407
Immunoglobulin C-Type;
152-222 4.43e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 53.09  E-value: 4.43e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZVO_C         152 PVVLACLITGYHPTSVTVTWYMGTQSQPQ--RTFPEIQRRDSYYMTSSQLSTPLQQWRQGE-YKCVVQHTASKS 222
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEgvSTTDPLKNSDGTYFLSSYLTVPASTWESGDvYTCQVTHEGLKE 74
C1-set pfam07654
Immunoglobulin C1-set domain;
421-489 1.18e-06

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 46.47  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZVO_C        421 LLCEVSGFSPPNILLMWLEDQREVnTSGFAPARPPPQPGStTFWAWSVLRVPAPPSPQPATYTCVVSHE 489
Cdd:pfam07654  17 LTCLVTGFYPPDITVTWLKNGQEV-TEGVKTTPPSPNSDW-TYQLSSYLTVTPSDWESGDEYTCRVEHE 83
 
Name Accession Description Interval E-value
IgC1_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 134-229 4.85e-65

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: 205.84  E-value: 4.85e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      134 APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 213
Cdd:cd16092   1 APDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 80

                        90
                ....*....|....*.
1ZVO_C      214 VVQHTASKSKKEIFRW 229
Cdd:cd16092  81 VVQHTASKSKKEIFRW 96
IgC1_CH3_IgD cd16094
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member ...
 403-502 9.15e-62

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin delta chain; member of the C1-set of Ig superfamily domains; The members here are composed of the third immunoglobulin constant domain (IgC) of delta 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. 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: 319343  Cd Length: 100  Bit Score: 197.38  E-value: 9.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      403 KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATY 482
Cdd:cd16094   1 KLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATY 80

                        90       100
                ....*....|....*....|
1ZVO_C      483 TCVVSHEDSRTLLNASRSLE 502
Cdd:cd16094  81 TCVVSHEDSRTLLNASRSLE 100
IgC1_CH2_IgD cd16084
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; ...
 298-394 2.01e-61

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


Pssm-ID: 409506  Cd Length: 97  Bit Score: 196.50  E-value: 2.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      298 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 377
Cdd:cd16084   1 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 80

                        90
                ....*....|....*..
1ZVO_C      378 CTLNHPSLPPQRLMALR 394
Cdd:cd16084  81 CTLNHPSLPPQRLMALR 97
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 3-128 1.78e-59

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: 191.75  E-value: 1.78e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        3 QLQESGPGLVKPSETLSLTCIVSGGPIrrTGYYWGWIRQPPGKGLEWIGGVYY-TGSIYYNPSLRGRVTISVDTSRNQFS 81
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTF--TSYGMGWVRQAPGKGLEWIGLIYPgGGDTYYADSFKGRFTITRDTSKSTAY 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1ZVO_C       82 LNLRSMSAADTAMYYCARGNPPPYYdigtgsdDGIDVWGQGTTVHVS 128
Cdd:cd04981  79 LQLNSLTSEDTAVYYCARGLGGYGY-------SYFDYWGQGTTVTVS 118
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 134-228 5.19e-39

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: 137.34  E-value: 5.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      134 APDVFPIISGCRHPkDNSPVVLACLITGYHPTSVTVTWYMGTQSQP---QRTFPEIQRRDSYYMTSSQLSTPLQQW-RQG 209
Cdd:cd04985   1 APTVFPLQSATKSQ-SNGPVALGCLISDYFPESITVSWQKNTNSITsgfTRTFPVVLRSGGDYSCSSQLTVPLQEWnSGE 79

                        90
                ....*....|....*....
1ZVO_C      210 EYKCVVQHTASKSKKEIFR 228
Cdd:cd04985  80 VYKCQVQHSASNSKQEKDV 98
IGv smart00406
Immunoglobulin V-Type;
17-99 7.26e-29

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 109.01  E-value: 7.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C          17 TLSLTCIVSGGPIrrTGYYWGWIRQPPGKGLEWIGGVYYTGSIYYNPSLRGRVTISVDTSRNQFSLNLRSMSAADTAMYY 96
Cdd:smart00406   1 SVTLSCKFSGSTF--SSYYVSWVRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYY 78


                   ...
1ZVO_C          97 CAR 99
Cdd:smart00406  79 CAV 81
C1-set pfam07654
Immunoglobulin C1-set domain;
137-220 3.97e-20

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 84.61  E-value: 3.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        137 VFPiisgcRHPKD-NSPVVLACLITGYHPTSVTVTWYMGTQSQPQ--RTFPEIQRRDSYYMTSSQLSTPLQQWRQGE-YK 212
Cdd:pfam07654   3 VFP-----PSPEElGKPNTLTCLVTGFYPPDITVTWLKNGQEVTEgvKTTPPSPNSDWTYQLSSYLTVTPSDWESGDeYT 77


                  ....*...
1ZVO_C        213 CVVQHTAS 220
Cdd:pfam07654  78 CRVEHEGL 85
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 299-387 3.07e-18

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: 79.81  E-value: 3.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      299 VYLLTPAVQDlWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 378
Cdd:cd00098   2 VTLLPPSPEE-KGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTC 80


                ....*....
1ZVO_C      379 TLNHPSLPP 387
Cdd:cd00098  81 VVTHESLKS 89
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 134-223 1.43e-17

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: 77.87  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      134 APDVFPIISGCRHpKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKC 213
Cdd:cd21817   1 APSVFPLAPCCKS-TNGSSVTLGCLVTGYFPEPVTVTWNSGSLTSGVKTFPAVLQSSGLYTTSSQVTVPSSSWGSQTFTC 79

                        90
                ....*....|
1ZVO_C      214 VVQHTASKSK 223
Cdd:cd21817  80 NVEHKPSSTK 89
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 405-493 9.24e-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: 75.57  E-value: 9.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      405 SLNLLASSDP--PEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAParPPPQPGSTTFWAWSVLRVPAPPSPQPATY 482
Cdd:cd00098   1 TVTLLPPSPEekGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTS--SPVEPNDGTYSVTSSLTVPPSDWDEGATY 78

                        90
                ....*....|.
1ZVO_C      483 TCVVSHEDSRT 493
Cdd:cd00098  79 TCVVTHESLKS 89
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 147-227 2.08e-16

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: 74.42  E-value: 2.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      147 PKDNSPVVLACLITGYHPTSVTVTWYMGTQSQP--QRTFPEIQRRDSYYMTSSQLSTPLQQWRQG-EYKCVVQHTASKSK 223
Cdd:cd00098  11 EKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTsgVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGaTYTCVVTHESLKSP 90


                ....
1ZVO_C      224 KEIF 227
Cdd:cd00098  91 LSKT 94
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 5-127 8.29e-16

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: 73.14  E-value: 8.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        5 QESGPGLVKPSETLSLTCIVSGGPirrTGYYWGWIRQPPGKGLEWIGGVYYTGSIYyNPSLRGRVTISVDTSrNQFSLNL 84
Cdd:cd00099   3 QSPRSLSVQEGESVTLSCEVSSSF---SSTYIYWYRQKPGQGPEFLIYLSSSKGKT-KGGVPGRFSGSRDGT-SSFSLTI 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1ZVO_C       85 RSMSAADTAMYYCARgnpppyydiGTGSDDGIDVWGQGTTVHV 127
Cdd:cd00099  78 SNLQPEDSGTYYCAV---------SESGGTDKLTFGSGTRLTV 111
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 299-386 3.54e-13

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: 65.82  E-value: 3.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      299 VYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGK-VPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 377
Cdd:cd05768   3 VYLLPPPEEELSLNETVTLTCLVKGFYPEDIFVSWLQNGEpLPSADYKTTAPVPESDGSFFVYSKLNVSTADWNSGDVFS 82


                ....*....
1ZVO_C      378 CTLNHPSLP 386
Cdd:cd05768  83 CVVGHEALP 91
IgC1_CH1_IgA cd21818
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 135-217 1.02e-12

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: 64.06  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      135 PDVFPIISGCRHPKDnsPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGE-YKC 213
Cdd:cd21818   2 PTVFPLSLCPSLSSD--PVVIGCLVQGFFPEPVNVTWNYSGKGGTARNFPAMLASGGRYTQSSQLTLPADQCPEGEaYKC 79


                ....
1ZVO_C      214 VVQH 217
Cdd:cd21818  80 SVQH 83
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 5-127 9.02e-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: 61.71  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C          5 QESGPGLVKPSETLSLTCIVSGGPIRRTGYYWgWIRQPPGKGLEWIggVYYTGSIYYNPSLRGRVTISVDTSRNQFSLNL 84
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVY-WYRQPPGKGPTFL--IAYYSNGSEEGVKKGRFSGRGDPSNGDGSLTI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
1ZVO_C         85 RSMSAADTAMYYCARGNPPpyydigtgsddgIDVWGQGTTVHV 127
Cdd:pfam07686  78 QNLTLSDSGTYTCAVIPSG------------EGVFGKGTRLTV 108
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 302-393 2.28e-11

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 59.90  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        302 LTPAVQDLWLRDKATFTCFVVGSDlKDAHLTWEVAGKVPTggveEGLLERHSNGSQSQHSRLTLPRSLWNAGTsVTCTLN 381
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGS-PGPDVTWSKEGGTLI----ESLKVKHDNGRTTQSSLLISNVTKEDAGT-YTCVVN 74

                          90
                  ....*....|..
1ZVO_C        382 HPSLPPQRLMAL 393
Cdd:pfam00047  75 NPGGSATLSTSL 86
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 135-221 3.87e-11

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: 59.73  E-value: 3.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      135 PDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQS---QPQRTFPeIQRRDSYYMTSSQLSTPLQQWRQGE- 210
Cdd:cd05847   1 PTVQILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGQVatlSAASTAP-QKEEGGTFSTTSKLNVTQEDWKSGKt 79

                        90
                ....*....|.
1ZVO_C      211 YKCVVQHTASK 221
Cdd:cd05847  80 YTCKVTHQGTT 90
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 134-226 8.41e-11

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: 58.49  E-value: 8.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      134 APDVFPIISgCRHPkDNSPVVLACLITGYHPTSVTVTW-YMGTQSQPQ-RTFPEIQRRDSYYMtSSQLSTPLQQWR-QGE 210
Cdd:cd21819   1 APTLFPLVS-CGSS-TSDPVTVGCLATDFLPDSITFSWtDDNNSLTTGvKTYPSVLTGGTYTA-SSQLQVPESEWKsKEN 77

                        90
                ....*....|....*.
1ZVO_C      211 YKCVVQHTASKSKKEI 226
Cdd:cd21819  78 FYCKVEHPGGNKEVPV 93
C1-set pfam07654
Immunoglobulin C1-set domain;
299-385 5.37e-10

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 56.10  E-value: 5.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        299 VYLLTPAVQDLwlRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 378
Cdd:pfam07654   1 VYVFPPSPEEL--GKPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTC 78


                  ....*..
1ZVO_C        379 TLNHPSL 385
Cdd:pfam07654  79 RVEHEGL 85
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 3-127 5.88e-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: 56.80  E-value: 5.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        3 QLQESGPGLVKPSETLSLTCIVSGGPIRRTGYywGWIRQPPGKGLEWIGGVyytGSIYYNPSlRGRVTISVDTSRNQFSL 82
Cdd:cd16095   3 QLEESGGGSHPAGKTLSLKCQTSGFQFNTSQL--SWYLWVPGHAPLWLTSL---DHISTKVS-EDRITSSREDTNSQIFL 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1ZVO_C       83 NLRSMSAADTAMYYCARgnpppyyDIGTGSDDGIDVWGQGTTVHV 127
Cdd:cd16095  77 QIKGLGLRDSGQYHCAR-------RVGYGDDTDKLIFGPGTDVIV 114
IGc1 smart00407
Immunoglobulin C-Type;
421-489 6.09e-10

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 55.40  E-value: 6.09e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZVO_C         421 LLCEVSGFSPPNILLMWLEDQREVnTSGFAPARPPPQpGSTTFWAWSVLRVPAPPSPQPATYTCVVSHE 489
Cdd:smart00407   4 LVCLVSGFYPPDITVTWLRNGQEV-TEGVSTTDPLKN-SDGTYFLSSYLTVPASTWESGDVYTCQVTHE 70
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 421-490 9.01e-10

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: 55.80  E-value: 9.01e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      421 LLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGStTFWAWSVLRVPAPPSPQPATYTCVVSHED 490
Cdd:cd05768  21 LTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVPESDG-SFFVYSKLNVSTADWNSGDVFSCVVGHEA 89
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 150-219 1.09e-09

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: 55.80  E-value: 1.09e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZVO_C      150 NSPVVLACLITGYHPTSVTVTWYMGTQSQPQ---RTFPEIQRRDSYYMTSSQLSTPLQQWRQG-EYKCVVQHTA 219
Cdd:cd05768  16 NETVTLTCLVKGFYPEDIFVSWLQNGEPLPSadyKTTAPVPESDGSFFVYSKLNVSTADWNSGdVFSCVVGHEA 89
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 4-128 1.78e-09

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: 55.45  E-value: 1.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        4 LQESGPGLVKP-SETLSLTCIVSGGPIRRTGYYWgwIRQPPGKGLEWIggVYYTgsiyYNPSLR-------GRVTISVDT 75
Cdd:cd04982   1 LEQPQLSITREeSKSVTISCKVSGIDFSTTYIHW--YRQKPGQALERL--LYVS----STSAVRkdsgktkNKFEARKDV 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
1ZVO_C       76 SRNQFSLNLRSMSAADTAMYYCArgnpppYYDIGTGSDdgIDVWGQGTTVHVS 128
Cdd:cd04982  73 GKSTSTLTITNLEKEDSATYYCA------YWESGSGYY--IKVFGSGTKLIVT 117
IGc1 smart00407
Immunoglobulin C-Type;
314-388 4.22e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 53.09  E-value: 4.22e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZVO_C         314 KATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPPQ 388
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75
IGc1 smart00407
Immunoglobulin C-Type;
152-222 4.43e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 53.09  E-value: 4.43e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZVO_C         152 PVVLACLITGYHPTSVTVTWYMGTQSQPQ--RTFPEIQRRDSYYMTSSQLSTPLQQWRQGE-YKCVVQHTASKS 222
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEgvSTTDPLKNSDGTYFLSSYLTVPASTWESGDvYTCQVTHEGLKE 74
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 12-127 9.43e-09

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: 53.33  E-value: 9.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C       12 VKPSETLSLTCIVSGGPIRrtGYYWGWIRQPPGKGLEWIggvYYTGSIYyNPSLRGRVTISVDTSRNQFSLNLRSMSAAD 91
Cdd:cd20988  10 VSVGKPVTLKCSMKGEAIS--NYYINWYRKTQGNTMTFI---YREGGIY-GPGFKDNFRGDIDSSNNLAVLKILEASERD 83

                        90       100       110
                ....*....|....*....|....*....|....*.
1ZVO_C       92 TAMYYCARGnpppyyDIGTGSDDGIDVWGQGTTVHV 127
Cdd:cd20988  84 EGSYYCASD------TPGGGREYDPLIFGKGTYLTV 113
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 31-126 3.55e-08

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: 51.50  E-value: 3.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C       31 RTGYYWGWIRQPPGKGLEWIggvyYTGSIYYNPSLRGRVTISVDTSRNQFSLNLRSMSAADTAMYYCARGNPPPYYDIgt 110
Cdd:cd04983  25 STFYYLFWYRQYPGQGPQFL----IYISSDSGNKKKGRFSATLDKSRKSSSLHISAAQLSDSAVYFCALSESGGTGKL-- 98

                        90
                ....*....|....*...
1ZVO_C      111 gsddgidVWGQGT--TVH 126
Cdd:cd04983  99 -------TFGKGTrlTVE 109
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 299-389 7.65e-08

CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, and mu chains, and CH2 domain (second constant Ig domain of the gheavy chain) in immunoglobulin heavy gamma chain; member of the C1-set of Ig superfamily (IgSF) ; The members here are composed of the third immunoglobulin constant domain (IgC) of the gamma heavy chains and the second immunoglobulin constant domain (IgC) of alpha, epsilon, and 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: 409493  Cd Length: 98  Bit Score: 50.14  E-value: 7.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      299 VYLLTPAVQDLWLRDKATFTCFVVG-SDLKDAHLTWEVAGKVPTGgVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 377
Cdd:cd07696   3 VFLIPPSPKDLFLTKSAKVTCLVVDlTSIEEVNVTWSREDGNEVL-ASTTNPEKHYNATLSVVSTLTVCADDWDNGKTFK 81

                        90
                ....*....|..
1ZVO_C      378 CTLNHPSLPPQR 389
Cdd:cd07696  82 CKVTHPDLPSPI 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 7-127 1.42e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C           7 SGPGLVKPSETLSLTCIVSGGPirrTGYYWgWIRQppgkGLEWIGGvyytgsiyynpslRGRvtISVDTSRNQFSLNLRS 86
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSP---PPEVT-WYKQ----GGKLLAE-------------SGR--FSVSRSGSTSTLTISN 57

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
1ZVO_C          87 MSAADTAMYYCARGNpppyydigtgsdDGIDVWGqGTTVHV 127
Cdd:smart00410  58 VTPEDSGTYTCAATN------------SSGSASS-GTTLTV 85
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 313-387 2.09e-07

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: 48.99  E-value: 2.09e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1ZVO_C      313 DKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPP 387
Cdd:cd07699  17 GKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSS 91
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 11-106 2.49e-07

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: 49.20  E-value: 2.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C       11 LVKPSETLSLTCIVSggpirrTGYYW-GWIRQPPGKGLEWIGgVYYTGSIYYNPSLRG-RVTIS-VDTSRnqFSLNLRSM 87
Cdd:cd05899   9 IKRRGQSVTLRCSQK------SGHDNmYWYRQDPGKGLQLLF-YSYGGGLNEEGDLPGdRFSASrPSLTR--SSLTIKSA 79

                        90       100
                ....*....|....*....|..
1ZVO_C       88 SAADTAMYYCA---RGNPPPYY 106
Cdd:cd05899  80 EPEDSAVYLCAsslGGGADEAY 101
IgC1_CH2_IgA cd04986
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 304-387 7.50e-07

CH2 domain (second 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 second immunoglobulin constant-1 set domain (IgC) of alpha 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. 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: 409375  Cd Length: 96  Bit Score: 47.37  E-value: 7.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      304 PAVQDLWLRDKATFTCFVVG-SDLKDAHLTWEvagkvPTGGVE--EGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTL 380
Cdd:cd04986   9 PALEDLLLGSNASLTCTLSGlKDPEGATFTWE-----PSGGKEaiQGPPERDSCGCYSVSSVLPGCAEPWNSGDTFSCTV 83


                ....*..
1ZVO_C      381 NHPSLPP 387
Cdd:cd04986  84 THPESKG 90
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 421-498 9.78e-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: 47.00  E-value: 9.78e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1ZVO_C      421 LLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATYTCVVSHEDSRTLLNAS 498
Cdd:cd16093  22 FVCLATGFSPKTISFKWLRNGKEVTSSTGAVVEEPKEDGKTLYSATSFLTITESEWKSQTEFTCEFKHKGEIVEKNAS 99
C1-set pfam07654
Immunoglobulin C1-set domain;
421-489 1.18e-06

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 46.47  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZVO_C        421 LLCEVSGFSPPNILLMWLEDQREVnTSGFAPARPPPQPGStTFWAWSVLRVPAPPSPQPATYTCVVSHE 489
Cdd:pfam07654  17 LTCLVTGFYPPDITVTWLKNGQEV-TEGVKTTPPSPNSDW-TYQLSSYLTVTPSDWESGDEYTCRVEHE 83
IgC1_CD1 cd21029
Immunoglobulin domain of Cluster of Differentiation (CD) 1; member of the C1-set of Ig ...
 133-229 8.33e-06

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: 44.23  E-value: 8.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      133 KAPDVFPIIsgcRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRT-FPEI--QRRDSYYMTSsqlSTPLQQWRQG 209
Cdd:cd21029   1 VKPRVRLSS---RPSPGDGHLQLSCHVTGFYPRPIEVTWLRDGQEQMDGTqSGGIlpNHDGTYQLRK---TLDIAPGEGA 74

                        90       100
                ....*....|....*....|
1ZVO_C      210 EYKCVVQHtASKSKKEIFRW 229
Cdd:cd21029  75 GYSCRVDH-SSLKQDLIVYW 93
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 12-105 9.26e-06

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: 44.69  E-value: 9.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C       12 VKPSETLSLTCIVSGGPIRrtgYYWGWIRQPPGKGLEWIggVYYTGSIYYNPSLRgrvtISVDTSRNQFSLNLRSMSAAD 91
Cdd:cd04980  12 VSPGERVTISCKASQSISS---NYLAWYQQKPGQAPKLL--IYYASTLHSGVPSR----FSGSGSGTDFTLTISSVEPED 82

                        90
                ....*....|....
1ZVO_C       92 TAMYYCARGNPPPY 105
Cdd:cd04980  83 AAVYYCQQGYTFPY 96
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 150-226 1.44e-05

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: 43.92  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      150 NSPVVLACLITGYHPTSVTVTWYMG----TQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQW-RQGEYKCVVQHTASKSKK 224
Cdd:cd16093  17 NRTATFVCLATGFSPKTISFKWLRNgkevTSSTGAVVEEPKEDGKTLYSATSFLTITESEWkSQTEFTCEFKHKGEIVEK 96


                ..
1ZVO_C      225 EI 226
Cdd:cd16093  97 NA 98
IgC1_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain, alpha3 immunoglobulin domain; ...
 415-489 1.79e-05

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: 43.37  E-value: 1.79e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1ZVO_C      415 PEAASWLLCEVSGFSPPNILLMWLEDQREVN-TSGFAPARPppqPGSTTFWAWSVLRVpapPSPQPATYTCVVSHE 489
Cdd:cd07698  13 SDGESTLRCWALGFYPAEITLTWQRDGEDQTqDMELVETRP---NGDGTFQKWAAVVV---PSGEEQRYTCHVQHE 82
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 421-499 3.86e-05

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: 42.40  E-value: 3.86e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1ZVO_C      421 LLCEVSGFSPPNILLMWLEDQREVNTSgfAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATYTCVVSHEDSRTLLNASR 499
Cdd:cd05847  21 LLCLISGYTPSTIEVEWLVDGQVATLS--AASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTYTCKVTHQGTTFEAHTKK 97
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 155-225 4.90e-05

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: 42.44  E-value: 4.90e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1ZVO_C      155 LACLITGYHPTSVTVTWYM--GTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQW-RQGEYKCVVQHTASKSKKE 225
Cdd:cd07699  21 LVCLINKFYPGFATVTWKVdgSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWnKHKVYTCEVTHEGLSSTIT 94
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 299-383 5.27e-05

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: 42.01  E-value: 5.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      299 VYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 378
Cdd:cd05847   3 VQILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTYTC 82


                ....*
1ZVO_C      379 TLNHP 383
Cdd:cd05847  83 KVTHQ 87
IgC1_beta2m cd05770
Class I major histocompatibility complex (MHC) beta-2-microglobulin; member of the C1-set of ...
 145-229 5.94e-05

Class I major histocompatibility complex (MHC) beta-2-microglobulin; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in beta-2-microglobulin (beta2m). Beta2m is the non-covalently bound light chain of the human class I major histocompatibility complex (MHC-I). Beta2m is structured as a beta-sandwich domain composed of two facing beta-sheets (four stranded and three stranded), that is typical of the C-type immunoglobulin superfamily. This structure is stabilized by an intramolecular disulfide bridge connecting two Cys residues in the facing beta-sheets. In vivo, MHC-I continuously exposes beta2m on the cell surface, where it may be released to plasmatic fluids, transported to the kidneys, degraded, and finally excreted.


Pssm-ID: 409427  Cd Length: 94  Bit Score: 42.08  E-value: 5.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      145 RHPKDN-SPVVLACLITGYHPTSVTVTWYMGTQSQP--QRTFPEIQRRDSYYMTSSQLSTPLQqwrQGEYKCVVQHtASK 221
Cdd:cd05770  10 RFPAENgKPNVLNCYVSGFHPPDIEIRLLKNGVKIEdvEQSDLSFSKDWTFYLLKYTEFTPTK---GDEYACRVRH-NTL 85


                ....*...
1ZVO_C      222 SKKEIFRW 229
Cdd:cd05770  86 SEPKIYKW 93
IgC1_MHC_Ib_HLA-H cd21021
Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte ...
 421-488 1.87e-04

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen H; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen H (HLA-H). HLA-H (also known as hereditary hemochromatosis protein; HFE) is a major histocompatibility complex (MHC) class I-like protein that is mutated in Hereditary Hemochromatosis. HFE is a protein of 343 amino acids that includes a signal peptide, an extracellular transferrin receptor-binding region (a1 and a2), an immunoglobulin-like domain (a3), a transmembrane region, and a short cytoplasmic tail. HFE binds beta-2-microglobulin to form a heterodimer expressed at the cell surface. It binds transferrin receptor (TFRC) in its extracellular alpha1-alpha2 domain. HFE plays an important part in the regulation of hepcidin expression in response to iron overload and the liver is important in the pathophysiology of HFE-associated hemochromatosis. Nine HFE splicing variants have been reported with transcripts lacking exon 2 or exon 3, or exons 2-3, 2-4, or 2-5. Diverse mutations involving HFE introns and exons discovered in persons with hemochromatosis or their family members cause or probably cause high iron phenotypes. 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: 409612  Cd Length: 94  Bit Score: 40.53  E-value: 1.87e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1ZVO_C      421 LLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQpGSTTFWAWSVLRVPaPPSPQpaTYTCVVSH 488
Cdd:cd21021  20 LRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVLPN-GDGTYQGWITLAVP-PGEEQ--RYTCQVEH 83
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 4-110 1.94e-04

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: 40.89  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C        4 LQESGPGLVKPSETLSLTCIVSGGPiRRTGYYWGWIRQPPGKG--LEWIGGVYYTGSIYYNPSL-RGRVTISVDTSRNQF 80
Cdd:cd07700   2 LQTPGSLLVQTNQTVKMSCEAKTSP-KNTRIYWLRQRQAPSKDshFEFLASWDPSKGIVYGEGVdQEKLIILSDSDSSRY 80

                        90       100       110
                ....*....|....*....|....*....|.
1ZVO_C       81 SLNLRSMSAADTAMYYCAR-GNPPPYYDIGT 110
Cdd:cd07700  81 ILSLMSVKPEDSGTYFCMTvGSPELIFGTGT 111
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 16-127 2.17e-04

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


Pssm-ID: 409503  Cd Length: 112  Bit Score: 40.97  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C       16 ETLSLTCIVSggpIRRTGYYWGWIRQPPGKGLEWiggVYYTGSIYYNpSLRGRVTISVDTSRNQFSLNLRSMSAADTAMY 95
Cdd:cd07706  15 EEVTLNCRYE---TSWTNYYLFWYKQLPSGEMTF---LIRQDSSEQN-AKSGRYSVNFQKAQKSISLTISALQLEDSAKY 87

                        90       100       110
                ....*....|....*....|....*....|..
1ZVO_C       96 YCARGNPPPyydigtgSDDGIdvWGQGTTVHV 127
Cdd:cd07706  88 FCALSLPYD-------TDKLI--FGKGTRLTV 110
IgC1_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of ...
 149-218 4.93e-04

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


Pssm-ID: 409423  Cd Length: 96  Bit Score: 39.24  E-value: 4.93e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ZVO_C      149 DNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPE--IQRRDSYYMTSSQLSTPLqqwRQGE-YKCVVQHT 218
Cdd:cd05766  16 LEHPNLLVCSVTGFYPAEIEVKWFRNGQEETAGVVSTelIPNGDWTFQILVMLETTP---RRGDvYTCQVEHS 85
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 38-105 1.32e-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: 38.59  E-value: 1.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C       38 WIRQPPGKGLEWIGgVYYTGSIY--YNPSLRGRVTISVDTSRNQFSLNLRSMSAADTAMYYCARGNPPPY 105
Cdd:cd20960  38 WLLLPSDKVEKVVI-TYSGDRVYnhYYPALKGRVAFTSNDLSGDASLNISNLKLSDTGTYQCKVKKAPGY 106
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 148-219 1.59e-03

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: 37.86  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      148 KDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEI--------QRRDSYYMTSSQLSTPLQQWRQGE-YKCVVQHT 218
Cdd:cd05771  12 KPDLPQTLSCHIAGYYPLDVDVEWLREEPGGSESQVSRDgvslsshrQSVDGTYSISSYLTLEPGTENRGAtYTCRVTHV 91


                .
1ZVO_C      219 A 219
Cdd:cd05771  92 S 92
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 299-385 2.29e-03

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: 37.37  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      299 VYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTW--------EVAGKVPTGGVEEGllerhsNGSQSQHSRLTLPRSLW 370
Cdd:cd16093   4 VSLHAPSREEFLGNRTATFVCLATGFSPKTISFKWlrngkevtSSTGAVVEEPKEDG------KTLYSATSFLTITESEW 77

                        90
                ....*....|....*
1ZVO_C      371 NAGTSVTCTLNHPSL 385
Cdd:cd16093  78 KSQTEFTCEFKHKGE 92
IgC1_MHC_Ia_HLA-F cd21023
Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte ...
 412-489 2.46e-03

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) F; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen alpha chain F (HLA-F). HLA-F, encoded by the HLA-F gene in humans, belongs to the non-classical HLA class I heavy chain paralogs. This class I molecule mainly exists as a heterodimer associated with the invariant light chain beta-2-microglobulin. HLA-F molecules can interact with both activating and inhibitory receptors on immune cells, such as NK cells, and can present a diverse panel of peptides. 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: 409614  Cd Length: 98  Bit Score: 37.49  E-value: 2.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      412 SDPPEA----------ASWLLCEVSGFSPPNILLMWLED-QREVNTSGFAPARPppqPGSTTFWAWSVLRVpapPSPQPA 480
Cdd:cd21023   3 ADPPKAhvahhpisdhEATLRCWALGFYPAEITLTWQRDgEEQTQDTELVETRP---AGDGTFQKWAAVVV---PPGEEQ 76


                ....*....
1ZVO_C      481 TYTCVVSHE 489
Cdd:cd21023  77 RYTCHVQHE 85
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 402-489 3.61e-03

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: 37.09  E-value: 3.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZVO_C      402 VKLSLNLLASsdpPEAASWLLCEVSGFSPPNILLMWLedqREVNTSGFAPARP-------PPQPGSTTFWAWSVLRVPAP 474
Cdd:cd05771   3 VRLSPKNLVK---PDLPQTLSCHIAGYYPLDVDVEWL---REEPGGSESQVSRdgvslssHRQSVDGTYSISSYLTLEPG 76

                        90
                ....*....|....*
1ZVO_C      475 PSPQPATYTCVVSHE 489
Cdd:cd05771  77 TENRGATYTCRVTHV 91
IgC1_MHC_Ib_T10_T22_like cd21016
Class Ib major histocompatibility complex (MHC) immunoglobulin domain of T10, T22, and similar ...
 415-489 8.55e-03

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of T10, T22, and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ib major histocompatibility complex (MHC) immunoglobulin domain of the murine H-2T-encoded T10, T22, and similar proteins. T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gammadelta T cell receptors (TCRs) in the absence of other components. Classical MHC class I (class Ia) molecules participate in immune responses by presenting peptide antigens to cytolytic alpha beta T cells. Many nonclassical MHC class I (class Ib) molecules have distinct antigen-binding capabilities, suggesting that they have evolved for specific tasks that are distinct from those of MHC class Ia. Members of the IgC 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, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 409607  Cd Length: 97  Bit Score: 35.85  E-value: 8.55e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1ZVO_C      415 PEAASWLLCEVSGFSPPNILLMWLEDQREVNTS-GFAPARPppqPGSTTFWAWSVLRVPAppsPQPATYTCVVSHE 489
Cdd:cd21016  16 PEGDVTLRCWALGFYPADITLTWQKDGEELTQDmEFVETRP---AGDGTFQKWAAVVVPL---GKEQSYTCHVYHE 85
IgC1_MHC_II_beta_HLA-DM cd21002
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of ...
 151-217 9.70e-03

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of histocompatibility antigen (HLA) DM; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain of histocompatibility antigen (HLA) DM. Human HLA-DM plays a critical role in antigen presentation to CD4 T cells by catalyzing the exchange of peptides bound to MHC class II molecules. Type 1 diabetes is correlated with DM activation and it is also implicated in viral infections such as herpes simplex virus, celiac disease, multiple sclerosis, other autoimmune diseases, and leukemia. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409593  Cd Length: 97  Bit Score: 35.67  E-value: 9.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1ZVO_C      151 SPVVLACLITGYHPTSVTVTWY-----MGTQSQPQRTfpeIQRR-DSYYMTSSQLSTPLQQWrqGEYKCVVQH 217
Cdd:cd21002  18 EPVMLACHVWGFYPADVTITWLkngdpVAPHSSAPKT---AQPNgDWTYQTQVTLAVTPSPG--DTYTCSVQH 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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