NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1335134|emb|CAA33069|]
View 

unnamed protein product, partial [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein; immunoglobulin domain-containing protein( domain architecture ID 10166755)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets| immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and/or pattern recognition

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 5-102 2.63e-48

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: 149.14  E-value: 2.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    5 IRVFAIPPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEASICEDDWNSGERF 84
Cdd:cd07696   1 VSVFLIPPSPKDLFLTKSAKVTCLVVDLTSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGKTF 80

                        90
                ....*....|....*...
gi 1335134   85 TCTVTHTDLPSPLKQTIS 102
Cdd:cd07696  81 KCKVTHPDLPSPIVKSIQ 98
 
Name Accession Description Interval E-value
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 5-102 2.63e-48

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: 149.14  E-value: 2.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    5 IRVFAIPPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEASICEDDWNSGERF 84
Cdd:cd07696   1 VSVFLIPPSPKDLFLTKSAKVTCLVVDLTSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGKTF 80

                        90
                ....*....|....*...
gi 1335134   85 TCTVTHTDLPSPLKQTIS 102
Cdd:cd07696  81 KCKVTHPDLPSPIVKSIQ 98
C1-set pfam07654
Immunoglobulin C1-set domain;
7-93 3.07e-08

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 46.86  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134      7 VFAIPPSFASifLTKSTKLTCLVTDLttY-DSVTISWTRqNGEAVKTHTNISESHPNA--TFSAVGEASICEDDWNSGER 83
Cdd:pfam07654   1 VYVFPPSPEE--LGKPNTLTCLVTGF--YpPDITVTWLK-NGQEVTEGVKTTPPSPNSdwTYQLSSYLTVTPSDWESGDE 75

                          90
                  ....*....|
gi 1335134     84 FTCTVTHTDL 93
Cdd:pfam07654  76 YTCRVEHEGL 85
IGc1 smart00407
Immunoglobulin C-Type;
25-96 4.55e-06

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 41.15  E-value: 4.55e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335134      25 LTCLVTDLttY-DSVTISWTRqNGEAVKTHTNISESHPNA--TFSAVGEASICEDDWNSGERFTCTVTHTDLPSP 96
Cdd:smart00407   4 LVCLVSGF--YpPDITVTWLR-NGQEVTEGVSTTDPLKNSdgTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75
 
Name Accession Description Interval E-value
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 5-102 2.63e-48

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: 149.14  E-value: 2.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    5 IRVFAIPPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEASICEDDWNSGERF 84
Cdd:cd07696   1 VSVFLIPPSPKDLFLTKSAKVTCLVVDLTSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGKTF 80

                        90
                ....*....|....*...
gi 1335134   85 TCTVTHTDLPSPLKQTIS 102
Cdd:cd07696  81 KCKVTHPDLPSPIVKSIQ 98
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 6-106 2.30e-16

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: 68.13  E-value: 2.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    6 RVFAIPPSFASIFLTKSTKLTCLVTDLTTYDsVTISWTrQNGEAVKT---HTNISESHPNATFSAVGEASICEDDWNSGE 82
Cdd:cd05768   2 SVYLLPPPEEELSLNETVTLTCLVKGFYPED-IFVSWL-QNGEPLPSadyKTTAPVPESDGSFFVYSKLNVSTADWNSGD 79

                        90       100
                ....*....|....*....|....*
gi 1335134   83 RFTCTVTHTDLPSPLKQ-TISRPKG 106
Cdd:cd05768  80 VFSCVVGHEALPLQFTQkSIDKSPG 104
IgC1_CH2_IgA cd04986
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 11-101 1.70e-11

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: 55.46  E-value: 1.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134   11 PPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEasICEDDWNSGERFTCTVTH 90
Cdd:cd04986   8 RPALEDLLLGSNASLTCTLSGLKDPEGATFTWEPSGGKEAIQGPPERDSCGCYSVSSVLP--GCAEPWNSGDTFSCTVTH 85

                        90
                ....*....|.
gi 1335134   91 TDLPSPLKQTI 101
Cdd:cd04986  86 PESKGTLTATI 96
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 6-101 7.02e-11

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


Pssm-ID: 409354  Cd Length: 95  Bit Score: 54.00  E-value: 7.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    6 RVFAIPPSfASIFLTKSTKLTCLVTDLTtYDSVTISWTRQNGEAVKTHTNISESHPNA-TFSAVGEASICEDDWNSGERF 84
Cdd:cd00098   1 TVTLLPPS-PEEKGGGKVTLVCLVSGFY-PKDITVTWLKNGVPLTSGVSTSSPVEPNDgTYSVTSSLTVPPSDWDEGATY 78

                        90
                ....*....|....*..
gi 1335134   85 TCTVTHTDLPSPLKQTI 101
Cdd:cd00098  79 TCVVTHESLKSPLSKTW 95
C1-set pfam07654
Immunoglobulin C1-set domain;
7-93 3.07e-08

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 46.86  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134      7 VFAIPPSFASifLTKSTKLTCLVTDLttY-DSVTISWTRqNGEAVKTHTNISESHPNA--TFSAVGEASICEDDWNSGER 83
Cdd:pfam07654   1 VYVFPPSPEE--LGKPNTLTCLVTGF--YpPDITVTWLK-NGQEVTEGVKTTPPSPNSdwTYQLSSYLTVTPSDWESGDE 75

                          90
                  ....*....|
gi 1335134     84 FTCTVTHTDL 93
Cdd:pfam07654  76 YTCRVEHEGL 85
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 7-90 1.09e-06

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: 43.17  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    7 VFAIPPSFASIFLTKSTKLTCLVTDLTTyDSVTISWTRQNGEA-VKTHTNISESHPNATFSAVGEASICEDDWNSGERFT 85
Cdd:cd05847   3 VQILHSSCASTLTSETIQLLCLISGYTP-STIEVEWLVDGQVAtLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTYT 81


                ....*
gi 1335134   86 CTVTH 90
Cdd:cd05847  82 CKVTH 86
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 7-103 1.12e-06

Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) light chain constant (C) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determine the type of immunoglobulin: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


Pssm-ID: 409496  Cd Length: 99  Bit Score: 43.21  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    7 VFAIPPSFASIFLTKSTkLTCLVTDLTTYDsVTISW-----TRQNGEAvkthTNISESHPNATFSAVGEASICEDDWNSG 81
Cdd:cd07699   4 VTIFPPSSEELSSGKAT-LVCLINKFYPGF-ATVTWkvdgsTVSSGVT----TSKTEQQSDNTYSMSSYLTLSSSDWNKH 77

                        90       100
                ....*....|....*....|..
gi 1335134   82 ERFTCTVTHTDLPSPLKQTISR 103
Cdd:cd07699  78 KVYTCEVTHEGLSSTITKSFNR 99
IGc1 smart00407
Immunoglobulin C-Type;
25-96 4.55e-06

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 41.15  E-value: 4.55e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335134      25 LTCLVTDLttY-DSVTISWTRqNGEAVKTHTNISESHPNA--TFSAVGEASICEDDWNSGERFTCTVTHTDLPSP 96
Cdd:smart00407   4 LVCLVSGF--YpPDITVTWLR-NGQEVTEGVSTTDPLKNSdgTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 7-91 3.44e-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: 39.30  E-value: 3.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    7 VFAIPPSFASIFLTKSTKLTCLVTDLTTYDsVTISWTRqNGEAVKTHTNISESHPNA----TFSAVGEASICEDDWNSGE 82
Cdd:cd16093   4 VSLHAPSREEFLGNRTATFVCLATGFSPKT-ISFKWLR-NGKEVTSSTGAVVEEPKEdgktLYSATSFLTITESEWKSQT 81


                ....*....
gi 1335134   83 RFTCTVTHT 91
Cdd:cd16093  82 EFTCEFKHK 90
IgC1_CH2_IgD cd16084
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; ...
 7-94 5.93e-05

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: 38.57  E-value: 5.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    7 VFAIPPSFASIFLTKSTKLTCLVTDLTTYDSvTISWtrQNGEAVKT---HTNISESHPNATFSAVGEASICEDDWNSGER 83
Cdd:cd16084   2 VYLLTPAVQDLWLRDKATFTCFVVGSDLKDA-HLTW--EVAGKVPTggvEEGLLERHSNGSQSQHSRLTLPRSLWNAGTS 78

                        90
                ....*....|.
gi 1335134   84 FTCTVTHTDLP 94
Cdd:cd16084  79 VTCTLNHPSLP 89
IgC1_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of ...
 17-97 9.58e-05

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: 38.08  E-value: 9.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134   17 IFLTKS------TKLTCLVTDLTTYDsVTISWtRQNGEAVKTHTNISESHPNA--TFSAVgeaSICEDDWNSGERFTCTV 88
Cdd:cd05766   8 VSPTKTgplehpNLLVCSVTGFYPAE-IEVKW-FRNGQEETAGVVSTELIPNGdwTFQIL---VMLETTPRRGDVYTCQV 82


                ....*....
gi 1335134   89 THTDLPSPL 97
Cdd:cd05766  83 EHSSLQSPL 91
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 27-90 1.62e-04

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: 37.31  E-value: 1.62e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1335134   27 CLVTDLTTyDSVTISWTRQNgeavKTHTNISESHP----NATFSAVGEASICEDDWNSGERFTCTVTH 90
Cdd:cd21819  22 CLATDFLP-DSITFSWTDDN----NSLTTGVKTYPsvltGGTYTASSQLQVPESEWKSKENFYCKVEH 84
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 17-97 3.31e-04

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: 36.70  E-value: 3.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134   17 IFLTKSTKLTCLVTDLTTYDsVTISWTRQ---NGEAVKTHTNISES----HPNATFSAVGEASICEDDWNSGERFTCTVT 89
Cdd:cd05771  11 VKPDLPQTLSCHIAGYYPLD-VDVEWLREepgGSESQVSRDGVSLSshrqSVDGTYSISSYLTLEPGTENRGATYTCRVT 89


                ....*...
gi 1335134   90 HTDLPSPL 97
Cdd:cd05771  90 HVSLEEPL 97
IgC1_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain, alpha3 immunoglobulin domain; ...
 22-97 1.73e-03

Class I major histocompatibility complex (MHC) alpha chain, alpha3 immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta-2-microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells.


Pssm-ID: 409495  Cd Length: 92  Bit Score: 34.51  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134   22 STKLTCLVTDLttYDS-VTISWTRqNGEAVKTHTNISESHPN--ATF---SAVGEASICEddwnsgERFTCTVTHTDLPS 95
Cdd:cd07698  16 ESTLRCWALGF--YPAeITLTWQR-DGEDQTQDMELVETRPNgdGTFqkwAAVVVPSGEE------QRYTCHVQHEGLPE 86


                ..
gi 1335134   96 PL 97
Cdd:cd07698  87 PL 88
IgC1_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig ...
 5-106 6.51e-03

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


Pssm-ID: 409426 [Multi-domain]  Cd Length: 116  Bit Score: 33.51  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335134    5 IRVFaiPPSFASIFLTKSTKLTCLVTDLttY-DSVTISWtRQNGEAVKT--HTNISESHPNA-TFSAVGEASICEDDW-N 79
Cdd:cd05769   5 VALF--PPSEAEIRNKRKATLVCLATGF--YpDHVSLSW-KVNGKEVKDgvATDPQALRENTsTYSLSSRLRVSATEWfN 79

                        90       100
                ....*....|....*....|....*..
gi 1335134   80 SGERFTCTVTHTDLPSPLKQTISRPKG 106
Cdd:cd05769  80 PRNTFTCIVKFYGGTDTDTWTQGIAGP 106
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH