NCBI Conserved Domain Search

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: 140.16 E-value: 1.05e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   48 APTLFPLAQCGSGTGDMMTLGCIATGFTPASLTFKWNEQGGKSLTDFVQYPAVQTGGSYTGVSQLRVKRADWDSK-IFEC 126
Cdd:cd21819      1 APTLFPLVSCGSSTSDPVTVGCLATDFLPDSITFSWTDDNNSLTTGVKTYPSVLTGGTYTASSQLQVPESEWKSKeNFYC 80

                           90
                   ....*....|....*
gi 1696205678  127 AVEHSAGSKTVPVKK 141
Cdd:cd21819     81 KVEHPGGNKEVPVPK 95

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: 89.44 E-value: 7.67e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2495 VRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSipSVLYAGSSTYSMNSRLIVPRSEWDHNSNYSCA 2574
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTS--SPVEPNDGTYSVTSSLTVPPSDWDEGATYTCV 81

                           90
                   ....*....|....
gi 1696205678 2575 VRHESSERPITSTI 2588
Cdd:cd00098     82 VTHESLKSPLSKTW 95

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: 84.05 E-value: 6.17e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2594 SVTPSAPTATL-LQGPSELACLVLGFSSSDINITWLLDDVTELWNNNTSTTYRAPGGKFGIRSHLSLAHQDWTPGAVYTC 2672
Cdd:cd00098      1 TVTLLPPSPEEkGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTC 80

                           90
                   ....*....|....
gi 1696205678 2673 RVTHTTQNLALNIS 2686
Cdd:cd00098     81 VVTHESLKSPLSKT 94

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: 76.61 E-value: 3.05e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2490 PSIKIVRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSIPSVLyAGSSTYSMNSRLIVPRSEWDHNS 2569
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVP-ESDGSFFVYSKLNVSTADWNSGD 79

                           90
                   ....*....|....*..
gi 1696205678 2570 NYSCAVRHESSERPITS 2586
Cdd:cd05768     80 VFSCVVGHEALPLQFTQ 96

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: 74.02 E-value: 1.53e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   48 APTLFPLAQC-GSGTGDMMTLGCIATGFTPASLTFKWNEQggkSLTDFVQ-YPAV-QTGGSYTGVSQLRVKRADWDSKIF 124
Cdd:cd21817      1 APSVFPLAPCcKSTNGSSVTLGCLVTGYFPEPVTVTWNSG---SLTSGVKtFPAVlQSSGLYTTSSQVTVPSSSWGSQTF 77

                           90
                   ....*....|...
gi 1696205678  125 ECAVEHSAGSKTV 137
Cdd:cd21817     78 TCNVEHKPSSTKV 90

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 71.13 E-value: 1.54e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2595 VTPSAPTATLLQGPSELACLVLGFSSSDINITWLLDDVTELWNNNTSTTYRAPGGKFGIRSHLSLAHQDWTPGAVYTCRV 2674
Cdd:pfam07654    1 VYVFPPSPEELGKPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTCRV 80


                   ....
gi 1696205678 2675 THTT 2678
Cdd:pfam07654   81 EHEG 84

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: 70.95 E-value: 2.18e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDLwGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSIPSvlYAGSSTYSMNSRLIVPRSEWDHN 2568
Cdd:cd07699      1 APSVTIFPPSSEEL-SSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTE--QQSDNTYSMSSYLTLSSSDWNKH 77

                           90       100
                   ....*....|....*....|
gi 1696205678 2569 SNYSCAVRHESSERPITSTI 2588
Cdd:cd07699     78 KVYTCEVTHEGLSSTITKSF 97

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: 70.57 E-value: 2.73e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  151 ITLYPLWEELEGGSKVGLLCILSEFYPDKLSVEWLLDDKTVTTSPVQRklQSVEGEEKTFSLSSQLELDQSQWTQGSEVT 230
Cdd:cd00098      2 VTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTS--SPVEPNDGTYSVTSSLTVPPSDWDEGATYT 79

                           90
                   ....*....|.
gi 1696205678  231 CKAIHNAAQGP 241
Cdd:cd00098     80 CVVTHESLKSP 90

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 66.57 E-value: 4.48e-13

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696205678  2508 ATLLCLVSGFFPSDVIVNWEKAGSrLPFSRYSSIPSVLyAGSSTYSMNSRLIVPRSEWDHNSNYSCAVRHESSERP 2583
Cdd:smart00407    2 ATLVCLVSGFYPPDITVTWLRNGQ-EVTEGVSTTDPLK-NSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75

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: 67.03 E-value: 5.81e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  148 PPNITLY-PLWEELEGGSKVGLLCILSEFYPDKLSVEWLLDDKTVTTSPVQRKLQSVEGEEKTFSLSSQLELDQSQWTQG 226
Cdd:cd16093      1 PPTVSLHaPSREEFLGNRTATFVCLATGFSPKTISFKWLRNGKEVTSSTGAVVEEPKEDGKTLYSATSFLTITESEWKSQ 80

                           90       100
                   ....*....|....*....|....*.
gi 1696205678  227 SEVTCKAIHnaaqgppPGTTVSRTIS 252
Cdd:cd16093     81 TEFTCEFKH-------KGEIVEKNAS 99

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, and delta chains, and CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, epsilon, and mu chains; member of the C1-set of I; The members here are composed of the third and fourth immunoglobulin constant domain (IgC) of alpha, delta, gamma and alpha, epsilon, and mu heavy chains, respectively. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409425 Cd Length: 105 Bit Score: 66.98 E-value: 6.95e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  149 PNITLY-PLWEELEGGSKVGLLCILSEFYPDKLSVEWLLDDKTV------TTSPVQRklqsvegEEKTFSLSSQLELDQS 221
Cdd:cd05768      1 PSVYLLpPPEEELSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLpsadykTTAPVPE-------SDGSFFVYSKLNVSTA 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1696205678  222 QWTQGSEVTCKAIHNAAqgppPGTTVSRTIS 252
Cdd:cd05768     74 DWNSGDVFSCVVGHEAL----PLQFTQKSID 100

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin constant-1 set domain of alpha chains. It belongs to a family composed of the first immunoglobulin constant-1 set domain of alpha, epsilon, gamma, and mu heavy chains. This domain is found on the Fab antigen-binding fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors.

Pssm-ID: 409623 Cd Length: 94 Bit Score: 64.45 E-value: 4.53e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   49 PTLFPLAQCGSGTGDMMTLGCIATGFTPASLTFKWNEQGGKSLTdfVQYPAVQ-TGGSYTGVSQLRVKrAD--WDSKIFE 125
Cdd:cd21818      2 PTVFPLSLCPSLSSDPVVIGCLVQGFFPEPVNVTWNYSGKGGTA--RNFPAMLaSGGRYTQSSQLTLP-ADqcPEGEAYK 78

                           90
                   ....*....|....
gi 1696205678  126 CAVEHSAGSKTVPV 139
Cdd:cd21818     79 CSVQHYSPSQDLNV 92

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: 63.58 E-value: 9.79e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  162 GGSKVGLLCILSEFYPDKLSVEWLLDDKTVTTSPVQRKLQSVEGeeKTFSLSSQLELDQSQWTQGSEVTCKAIHnaaqgp 241
Cdd:cd05847     15 TSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAASTAPQKEEG--GTFSTTSKLNVTQEDWKSGKTYTCKVTH------ 86

                           90
                   ....*....|
gi 1696205678  242 pPGTTVSRTI 251
Cdd:cd05847     87 -QGTTFEAHT 95

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: 63.55 E-value: 1.31e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2488 KPPSIKIVRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEW-D 2566
Cdd:cd05769      1 TPPTVALFPPSEAEIRNKRKATLVCLATGFYPDHVSLSWKVNGKEVK-DGVATDPQALRENTSTYSLSSRLRVSATEWfN 79

                           90
                   ....*....|..
gi 1696205678 2567 HNSNYSCAVRHE 2578
Cdd:cd05769     80 PRNTFTCIVKFY 91

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 62.27 E-value: 1.92e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2497 PSDSDLwgSNNATLLCLVSGFFPSDVIVNWEKAGSRLPfSRYSSIPSVLYaGSSTYSMNSRLIVPRSEWDHNSNYSCAVR 2576
Cdd:pfam07654    6 PSPEEL--GKPNTLTCLVTGFYPPDITVTWLKNGQEVT-EGVKTTPPSPN-SDWTYQLSSYLTVTPSDWESGDEYTCRVE 81


                   ....
gi 1696205678 2577 HESS 2580
Cdd:pfam07654   82 HEGL 85

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: 62.04 E-value: 2.72e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2490 PSIKIVRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSIPSVlyAGSSTYSMNSRLIVPRSEWDHNS 2569
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAASTAPQK--EEGGTFSTTSKLNVTQEDWKSGK 78

                           90
                   ....*....|.
gi 1696205678 2570 NYSCAVRHESS 2580
Cdd:cd05847     79 TYTCKVTHQGT 89

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: 61.32 E-value: 5.85e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  148 PPNITLYPLWEELEGGSKVGLLCILSEFYPDKLSVEWLLDDKTV-----TTSPVQRKlqsvegeEKTFSLSSQLELDQSQ 222
Cdd:cd07699      1 APSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVssgvtTSKTEQQS-------DNTYSMSSYLTLSSSD 73

                           90
                   ....*....|....*....
gi 1696205678  223 WTQGSEVTCKAIHNAAQGP 241
Cdd:cd07699     74 WNKHKVYTCEVTHEGLSST 92

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 60.41 E-value: 6.01e-11

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696205678  2611 LACLVLGFSSSDINITWLLDDVTELWNNNTSTTYRAPGGKFGIRSHLSLAHQDWTPGAVYTCRVTHTT 2678
Cdd:smart00407    4 LVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEG 71

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 60.73 E-value: 6.32e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  151 ITLYPLWEElEGGSKVGLLCILSEFYPDKLSVEWLLDDKTVT-----TSPVQRKlqsvegeEKTFSLSSQLELDQSQWTQ 225
Cdd:pfam07654    1 VYVFPPSPE-ELGKPNTLTCLVTGFYPPDITVTWLKNGQEVTegvktTPPSPNS-------DWTYQLSSYLTVTPSDWES 72

                           90
                   ....*....|..
gi 1696205678  226 GSEVTCKAIHNA 237
Cdd:pfam07654   73 GDEYTCRVEHEG 84

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: 60.17 E-value: 1.23e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2387 VYLQGPTLQELrTDGQVPVTCLLVGLSLGDFSVSWKVDGVVASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVSC 2466
Cdd:cd00098      2 VTLLPPSPEEK-GGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTC 80

                           90
                   ....*....|..
gi 1696205678 2467 EVKHRCSSQAQE 2478
Cdd:cd00098     81 VVTHESLKSPLS 92

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: 60.08 E-value: 2.50e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  147 IPPNITLY-PLWEELEGGSKVGLLCILSEFYPDKLSVEWLLDDKTVTTSpVQRKLQSVEGEEKTFSLSSQLELDQSQWT 224
Cdd:cd05769      1 TPPTVALFpPSEAEIRNKRKATLVCLATGFYPDHVSLSWKVNGKEVKDG-VATDPQALRENTSTYSLSSRLRVSATEWF 78

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: 58.58 E-value: 4.82e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2595 VTPSAPTATLLQGPSELACLVLGFSSSDINITWLLDD-VTELWNNNTSTTYRApGGKFGIRSHLSLAHQDWTPGAVYTCR 2673
Cdd:cd05847      5 ILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGqVATLSAASTAPQKEE-GGTFSTTSKLNVTQEDWKSGKTYTCK 83


                   ...
gi 1696205678 2674 VTH 2676
Cdd:cd05847     84 VTH 86

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 57.32 E-value: 7.05e-10

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   165 KVGLLCILSEFYPDKLSVEWLLD-----DKTVTTSPVQRKlqsvegeEKTFSLSSQLELDQSQWTQGSEVTCKAIHNAAQ 239
Cdd:smart00407    1 KATLVCLVSGFYPPDITVTWLRNgqevtEGVSTTDPLKNS-------DGTYFLSSYLTVPASTWESGDVYTCQVTHEGLK 73


                    ..
gi 1696205678   240 GP 241
Cdd:smart00407   74 EP 75

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: 58.11 E-value: 7.72e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDLWGSnnATLLCLVSGFFPSDVIVNWEKAGSRLpFSRYSSIPSVLYAGssTYSMNSRLIVPRSEWDHN 2568
Cdd:cd21819      1 APTLFPLVSCGSSTSDP--VTVGCLATDFLPDSITFSWTDDNNSL-TTGVKTYPSVLTGG--TYTASSQLQVPESEWKSK 75

                           90
                   ....*....|....
gi 1696205678 2569 SNYSCAVRHESSER 2582
Cdd:cd21819     76 ENFYCKVEHPGGNK 89

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: 58.12 E-value: 7.96e-10

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696205678 2611 LACLVLGFSSSDINITWLLDDVTELWNN-NTSTTYRAPGGKFGIRSHLSLAHQDWTPGAVYTCRVTH 2676
Cdd:cd05768     21 LTCLVKGFYPEDIFVSWLQNGEPLPSADyKTTAPVPESDGSFFVYSKLNVSTADWNSGDVFSCVVGH 87

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: 58.17 E-value: 7.99e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPfsrySSIPSVLYA----GSSTYSMNSRLIVPRSE 2564
Cdd:cd16093      1 PPTVSLHAPSREEFLGNRTATFVCLATGFSPKTISFKWLRNGKEVT----SSTGAVVEEpkedGKTLYSATSFLTITESE 76

                           90
                   ....*....|....*.
gi 1696205678 2565 WDHNSNYSCAVRHESS 2580
Cdd:cd16093     77 WKSQTEFTCEFKHKGE 92

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: 58.12 E-value: 8.36e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678   62 GDMMTLGCIATGFTPASLTFKWnEQGGKSL--TDFVQY-PAVQTGGSYTGVSQLRVKRADWDS-KIFECAVEHSA 132
Cdd:cd05768     16 NETVTLTCLVKGFYPEDIFVSW-LQNGEPLpsADYKTTaPVPESDGSFFVYSKLNVSTADWNSgDVFSCVVGHEA 89

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: 57.45 E-value: 1.45e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2386 GVYLQGPTLQELRTDGQVPVTCLLVGLSLGDFSVSWKVDGVVASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVS 2465
Cdd:cd16084      1 GVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVT 80


                   ....*
gi 1696205678 2466 CEVKH 2470
Cdd:cd16084     81 CTLNH 85

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: 57.21 E-value: 1.85e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696205678 2505 SNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSIPSVLyAGSSTYSMNSRLIVPRSEWDHNSNYSCAVRHESS 2580
Cdd:cd04985     16 NGPVALGCLISDYFPESITVSWQKNTNSITSGFTRTFPVVL-RSGGDYSCSSQLTVPLQEWNSGEVYKCQVQHSAS 90

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: 56.58 E-value: 2.99e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2387 VYLQGPTLQELRTDGQVPVTCLLVGLSLGDFSVSWKVDGV-VASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVS 2465
Cdd:cd05768      3 VYLLPPPEEELSLNETVTLTCLVKGFYPEDIFVSWLQNGEpLPSADYKTTAPVPESDGSFFVYSKLNVSTADWNSGDVFS 82


                   ....*
gi 1696205678 2466 CEVKH 2470
Cdd:cd05768     83 CVVGH 87

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: 55.54 E-value: 5.46e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   49 PTLFPLAQCGSGTGDMmTLGCIATGFTPASLTFKWnEQGGKSLTDFVQY--PAVQTGGSYTGVSQLRVKRADWDS-KIFE 125
Cdd:cd00098      2 VTLLPPSPEEKGGGKV-TLVCLVSGFYPKDITVTW-LKNGVPLTSGVSTssPVEPNDGTYSVTSSLTVPPSDWDEgATYT 79

                           90
                   ....*....|..
gi 1696205678  126 CAVEHSAGSKTV 137
Cdd:cd00098     80 CVVTHESLKSPL 91

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: 54.00 E-value: 1.89e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2599 APTATLLQGPSE--------LACLVLGFSSSDINITWLLDDVTELWNNNTSTTYRAPGGKFGIRSHLSLAHQDWTPGAVY 2670
Cdd:cd07699      1 APSVTIFPPSSEelssgkatLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVY 80


                   ....*...
gi 1696205678 2671 TCRVTHTT 2678
Cdd:cd07699     81 TCEVTHEG 88

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: 53.65 E-value: 2.57e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2502 LWGSNNATLLCLVSGFFPSDVIVNWekagSRLPFSrySSIPSVLYAGSS----------TYSMNSRLIVPRSEWDHNSNY 2571
Cdd:cd05771     11 VKPDLPQTLSCHIAGYYPLDVDVEW----LREEPG--GSESQVSRDGVSlsshrqsvdgTYSISSYLTLEPGTENRGATY 84

                           90
                   ....*....|....
gi 1696205678 2572 SCAVRHESSERPIT 2585
Cdd:cd05771     85 TCRVTHVSLEEPLS 98

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: 53.09 E-value: 3.78e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2495 VRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSipSVLYAGSSTYSMNSRLIVPRSEWDhnsNYSCA 2574
Cdd:cd21029      5 VRLSSRPSPGDGHLQLSCHVTGFYPRPIEVTWLRDGQEQMDGTQSG--GILPNHDGTYQLRKTLDIAPGEGA---GYSCR 79

                           90
                   ....*....|.
gi 1696205678 2575 VRHESSERPIT 2585
Cdd:cd21029     80 VDHSSLKQDLI 90

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: 53.36 E-value: 4.10e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   48 APTLFPLAQ-CGSGTGDMMTLGCIATGFTPASLTFKW--NEQGGKSLTDFVQYPAVQTGGSYTGVSQLRVKRADWDS-KI 123
Cdd:cd04985      1 APTVFPLQSaTKSQSNGPVALGCLISDYFPESITVSWqkNTNSITSGFTRTFPVVLRSGGDYSCSSQLTVPLQEWNSgEV 80


                   ....*....
gi 1696205678  124 FECAVEHSA 132
Cdd:cd04985     81 YKCQVQHSA 89

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 52.64 E-value: 4.64e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   66 TLGCIATGFTPASLTFKWnEQGGKSLTDFVQY--PAVQTGGSYTGVSQLRVKRADWDS-KIFECAVEHSA 132
Cdd:pfam07654   16 TLTCLVTGFYPPDITVTW-LKNGQEVTEGVKTtpPSPNSDWTYQLSSYLTVTPSDWESgDEYTCRVEHEG 84

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: 52.62 E-value: 5.96e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGsrLPFSRYSSIPSVLYAGSSTYSMNSRLIVPRSEWdhn 2568
Cdd:cd07698      2 PPKVHVTHHPRSD----GESTLRCWALGFYPAEITLTWQRDG--EDQTQDMELVETRPNGDGTFQKWAAVVVPSGEE--- 72

                           90
                   ....*....|....*..
gi 1696205678 2569 SNYSCAVRHESSERPIT 2585
Cdd:cd07698     73 QRYTCHVQHEGLPEPLT 89

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: 52.72 E-value: 7.79e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1372 PSMELLLVPNEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQRSAAD---NERRMREDGHVAVTSHITVTQQEWNEGKG 1445
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQNGEPLPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|
gi 1696205678 1446 FICEVIDKDL-QKTVRKSIS 1464
Cdd:cd05768     81 FSCVVGHEALpLQFTQKSID 100

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: 52.72 E-value: 7.79e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  463 PSMELLLVPNEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQRSAAD---NERRMREDGHVAVTSHITVTQQEWNEGKG 536
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQNGEPLPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|
gi 1696205678  537 FICEVIDKDL-QKTVRKSIS 555
Cdd:cd05768     81 FSCVVGHEALpLQFTQKSID 100

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: 52.34 E-value: 9.74e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2281 PSMELLLVPNEDLSGSGTQKLMCSGRGFNPQ---IKWLS----VSAAAY---EIRMGDDERVAVTSQITVTQQEWNQGKN 2350
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQngepLPSADYkttAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|..
gi 1696205678 2351 FTCEVidkYLQKEDLQKVRKSI 2372
Cdd:cd05768     81 FSCVV---GHEALPLQFTQKSI 99

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: 51.29 E-value: 1.60e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDLWGSNnATLLCLVSGFFPSDVIVNWeKAGSRLpfSRYSSIPSVLyAGSSTYSMNSRLIVPRSEWdHN 2568
Cdd:cd21817      1 APSVFPLAPCCKSTNGSS-VTLGCLVTGYFPEPVTVTW-NSGSLT--SGVKTFPAVL-QSSGLYTTSSQVTVPSSSW-GS 74

                           90       100
                   ....*....|....*....|
gi 1696205678 2569 SNYSCAVRHESSERPITSTI 2588
Cdd:cd21817     75 QTFTCNVEHKPSSTKVDKKI 94

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 49.56 E-value: 5.08e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2387 VYLQGPTLQELRtdGQVPVTCLLVGLSLGDFSVSWKVDGVVASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVSC 2466
Cdd:pfam07654    1 VYVFPPSPEELG--KPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTC 78


                   ....
gi 1696205678 2467 EVKH 2470
Cdd:pfam07654   79 RVEH 82

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: 50.03 E-value: 5.40e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1978 PSMELLLVANEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQRSAAD---NERRIREDGHVAVTSHITVTQQEWNEGKD 2051
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQNGEPLPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|...
gi 1696205678 2052 FICEVIDKDL-----QKTVRKST 2069
Cdd:cd05768     81 FSCVVGHEALplqftQKSIDKSP 103

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: 50.03 E-value: 5.40e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1675 PSMELLLVANEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQRSAAD---NERRIREDGHVAVTSHITVTQQEWNEGKD 1748
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQNGEPLPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|...
gi 1696205678 1749 FICEVIDKDL-----QKTVRKST 1766
Cdd:cd05768     81 FSCVVGHEALplqftQKSIDKSP 103

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: 49.70 E-value: 7.98e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696205678   66 TLGCIATGFTPASLTFKWNeQGGKSLTD---FVQYPAV-QTGGSYTGVSQLRVKRADW-DSKIFECAVEHSAG 133
Cdd:cd16093     21 TFVCLATGFSPKTISFKWL-RNGKEVTSstgAVVEEPKeDGKTLYSATSFLTITESEWkSQTEFTCEFKHKGE 92

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: 49.38 E-value: 9.13e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1377 LLVPNEDLSGSGTQKLMCSGRGFNP---QIKWLSGSKQRSAADNER--RMREDGHVAVTSHITVTQQEWNEGKGFICEVI 1451
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLKNGVPLTSGVSTSspVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVT 83

                           90
                   ....*....|..
gi 1696205678 1452 DKDLQKTVRKSI 1463
Cdd:cd00098     84 HESLKSPLSKTW 95

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: 49.38 E-value: 9.13e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  468 LLVPNEDLSGSGTQKLMCSGRGFNP---QIKWLSGSKQRSAADNER--RMREDGHVAVTSHITVTQQEWNEGKGFICEVI 542
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLKNGVPLTSGVSTSspVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVT 83

                           90
                   ....*....|..
gi 1696205678  543 DKDLQKTVRKSI 554
Cdd:cd00098     84 HESLKSPLSKTW 95

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: 49.37 E-value: 9.73e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2595 VTPSAPTATLLQGPSELACLVLGFSSSD-INITWLLDDVTELwnnNTSTTYR--APGGKFGIRSHLSLAHQDWTPGAVYT 2671
Cdd:cd07696      5 LIPPSPKDLFLTKSAKVTCLVVDLTSIEeVNVTWSREDGNEV---LASTTNPekHYNATLSVVSTLTVCADDWDNGKTFK 81


                   ....*.
gi 1696205678 2672 CRVTHT 2677
Cdd:cd07696     82 CKVTHP 87

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: 49.00 E-value: 9.97e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  571 TPRFRTVMTQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 645
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678  646 RCFNPTQTTS 655
Cdd:cd00098     85 ESLKSPLSKT 94

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: 49.13 E-value: 1.08e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  152 TLYPLW--EELEGGSKVGLLCILSEFYPDKLSVEWLLDDKTVTTSpVQRKLQSVEGEEKTFSLSSQLELDQSQWTQGSEV 229
Cdd:cd04985      3 TVFPLQsaTKSQSNGPVALGCLISDYFPESITVSWQKNTNSITSG-FTRTFPVVLRSGGDYSCSSQLTVPLQEWNSGEVY 81

                           90
                   ....*....|.
gi 1696205678  230 TCKAIHNAAQG 240
Cdd:cd04985     82 KCQVQHSASNS 92

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: 48.95 E-value: 1.09e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696205678 2399 TDGQVPVTCLLVGLSLGDFSVSWKVDGVVASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVSCEVKH 2470
Cdd:cd05847     15 TSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTYTCKVTH 86

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: 48.61 E-value: 1.38e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  874 TPRFRTVMTQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRAPVKQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 948
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678  949 RCFNPTQTTS 958
Cdd:cd00098     85 ESLKSPLSKT 94

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: 48.61 E-value: 1.38e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1177 TPRFRTVMTQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRAPVKQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 1251
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678 1252 RCFNPTQTTS 1261
Cdd:cd00098     85 ESLKSPLSKT 94

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: 48.61 E-value: 1.49e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  268 TPRFRTVMTQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 342
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678  343 RCFNTTQRTS 352
Cdd:cd00098     85 ESLKSPLSKT 94

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 48.02 E-value: 1.90e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  886 VTATCVVHSAY--DAKVSWLLDGKDPTSRA----PVKQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 948
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGVkttpPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 48.02 E-value: 1.90e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678 1189 VTATCVVHSAY--DAKVSWLLDGKDPTSRA----PVKQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 1251
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGVkttpPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

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: 47.88 E-value: 2.47e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2505 SNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYssiPSVLYAGsSTYSMNSRLIVPRSEWDHNSNYSCAVRHESSERPI 2584
Cdd:cd21818     15 SDPVVIGCLVQGFFPEPVNVTWNYSGKGGTARNF---PAMLASG-GRYTQSSQLTLPADQCPEGEAYKCSVQHYSPSQDL 90


                   .
gi 1696205678 2585 T 2585
Cdd:cd21818     91 N 91

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 47.31 E-value: 2.74e-06

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678   582 EVTATCVVHSAY--DAKVSWLLDGKDPTS---RTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 645
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEgvsTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 47.31 E-value: 2.74e-06

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678   279 EVTATCVVHSAY--DAKVSWLLDGKDPTS---RTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 342
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEgvsTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

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: 47.61 E-value: 3.70e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2487 PKPPSIKIVRPSDSdlwgsnNAT----LLCLVSGFFPSDVIVNWEKAGSrlPFSRYSSIP-SVLYAGSSTYSMNSRLIVP 2561
Cdd:cd21002      1 RRPPSVRVAPTTPF------NTRepvmLACHVWGFYPADVTITWLKNGD--PVAPHSSAPkTAQPNGDWTYQTQVTLAVT 72

                           90       100
                   ....*....|....*....|....
gi 1696205678 2562 RSEWDhnsNYSCAVRHESSERPIT 2585
Cdd:cd21002     73 PSPGD---TYTCSVQHASLPEPLL 93

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: 47.45 E-value: 3.79e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1480 TPRFRTVMTQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRAPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 1554
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678 1555 RCFNPTQTTS 1564
Cdd:cd00098     85 ESLKSPLSKT 94

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: 47.45 E-value: 3.89e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2392 PTLQELRTdGQVPVTCLLVGLSLGDFSVSWKVDGVVASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVSCEVKHR 2471
Cdd:cd07699      9 PSSEELSS-GKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHE 87

                           90
                   ....*....|..
gi 1696205678 2472 CSSQAQEEHITK 2483
Cdd:cd07699     88 GLSSTITKSFNR 99

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 46.86 E-value: 4.24e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  583 VTATCVVHSAY--DAKVSWLLDGKDPTSR----TPVNQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 645
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGvkttPPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 46.86 E-value: 4.24e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  280 VTATCVVHSAY--DAKVSWLLDGKDPTSR----TPVNQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 342
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGvkttPPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

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: 47.39 E-value: 4.84e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1372 PSMELLLVPNEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQ----RSAADNERRMREDGHVAVTSHITVTQQEWNEGK 1444
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLRNGKEvtssTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81

                           90       100
                   ....*....|....*....|
gi 1696205678 1445 GFICEVIDKDLqkTVRKSIS 1464
Cdd:cd16093     82 EFTCEFKHKGE--IVEKNAS 99

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: 47.39 E-value: 4.84e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  463 PSMELLLVPNEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQ----RSAADNERRMREDGHVAVTSHITVTQQEWNEGK 535
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLRNGKEvtssTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81

                           90       100
                   ....*....|....*....|
gi 1696205678  536 GFICEVIDKDLqkTVRKSIS 555
Cdd:cd16093     82 EFTCEFKHKGE--IVEKNAS 99

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: 47.33 E-value: 4.96e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  766 PSMELLLVANEDLSGSGTQKIMCSGRGFNPQ---IKWLSGTKQRSAAD---NERRIREDGHVAVTSHITVTQQEWNEGKD 839
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQNGEPLPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|...
gi 1696205678  840 FICEVIDKDL-----QKTVRKST 857
Cdd:cd05768     81 FSCVVGHEALplqftQKSIDKSP 103

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: 47.33 E-value: 4.96e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1069 PSMELLLVANEDLSGSGTQKIMCSGRGFNPQ---IKWLSGTKQRSAAD---NERRIREDGHVAVTSHITVTQQEWNEGKD 1142
Cdd:cd05768      1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEdifVSWLQNGEPLPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                           90       100
                   ....*....|....*....|...
gi 1696205678 1143 FICEVIDKDL-----QKTVRKST 1160
Cdd:cd05768     81 FSCVVGHEALplqftQKSIDKSP 103

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 46.54 E-value: 5.39e-06

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  2097 EVTANCVVHSAY--DAKVSWLLDGKDPTS---RTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 2160
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEgvsTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 46.54 E-value: 5.39e-06

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  1794 EVTANCVVHSAY--DAKVSWLLDGKDPTS---RTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 1857
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEgvsTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 46.86 E-value: 5.57e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678 1492 VTATCVVHSAY--DAKVSWLLDGKDPTSRA----PVNQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 1554
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGVkttpPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

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: 47.10 E-value: 6.20e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2595 VTPSAPTATLLQGPSELACLVLGFSSSDINITWLLDDVTE------LWNNNTSTTYRAPGGKFGIRSHLSLAHQDWTPGA 2668
Cdd:cd05771      3 VRLSPKNLVKPDLPQTLSCHIAGYYPLDVDVEWLREEPGGsesqvsRDGVSLSSHRQSVDGTYSISSYLTLEPGTENRGA 82


                   ....*....
gi 1696205678 2669 VYTCRVTHT 2677
Cdd:cd05771     83 TYTCRVTHV 91

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: 46.68 E-value: 6.49e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1680 LLVANEDLSGSGTQKLMCSGRGFNP---QIKWLSGSKQRSAADNERRIRE--DGHVAVTSHITVTQQEWNEGKDFICEVI 1754
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLKNGVPLTSGVSTSSPVEpnDGTYSVTSSLTVPPSDWDEGATYTCVVT 83

                           90
                   ....*....|..
gi 1696205678 1755 DKDLQKTVRKST 1766
Cdd:cd00098     84 HESLKSPLSKTW 95

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: 46.68 E-value: 6.49e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1983 LLVANEDLSGSGTQKLMCSGRGFNP---QIKWLSGSKQRSAADNERRIRE--DGHVAVTSHITVTQQEWNEGKDFICEVI 2057
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLKNGVPLTSGVSTSSPVEpnDGTYSVTSSLTVPPSDWDEGATYTCVVT 83

                           90
                   ....*....|..
gi 1696205678 2058 DKDLQKTVRKST 2069
Cdd:cd00098     84 HESLKSPLSKTW 95

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 46.15 E-value: 6.55e-06

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696205678  2405 VTCLLVGLSLGDFSVSWKVDGVVASQGGVTRAPKDHSNGTQTEQIMFNVPARDWHAHKLVSCEVKH 2470
Cdd:smart00407    4 LVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

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: 46.94 E-value: 6.72e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2594 SVTPSAPTATLLQGPSELACLVLGFSSSDINITWLLDDVTELWNNNTSTTYRAPGGKFGIRSHLSLAHQdwtPGAVYTCR 2673
Cdd:cd05766      5 SVKVSPTKTGPLEHPNLLVCSVTGFYPAEIEVKWFRNGQEETAGVVSTELIPNGDWTFQILVMLETTPR---RGDVYTCQ 81


                   ....
gi 1696205678 2674 VTHT 2677
Cdd:cd05766     82 VEHS 85

Class Ia major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) B and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the class Ia major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) B and similar proteins. The classical class I molecules (HLA-A, -B, and -C) are responsible for the presentation of endogenous antigen to CD8+ T cells. The receptor is a heterodimer, and is composed of a heavy alpha chain and smaller beta chain. The alpha chain is encoded by a variant HLA-B gene, and the beta chain (beta-2-microglobulin) is an invariant beta-2-microglobulin molecule. The beta-2-microglobulin protein is coded for by a separate region of the human genome. Human leukocyte antigen (HLA) B*3501 (B35) is a common human allele involved in mediating protective immunity against HIV. 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: 409617 Cd Length: 97 Bit Score: 46.73 E-value: 6.84e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhN 2568
Cdd:cd21026      5 PPKTHVTHHPISD----HEATLRCWALGFYPAEITLTWQRDGEDQ--TQDTELVETRPAGDRTFQKWAAVVVPSGE---E 75

                           90
                   ....*....|....*..
gi 1696205678 2569 SNYSCAVRHESSERPIT 2585
Cdd:cd21026     76 QRYTCHVQHEGLPKPLT 92

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: 46.68 E-value: 8.32e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  579 TQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNPTQT 653
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678  654 TS 655
Cdd:cd07699     95 KS 96

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 46.09 E-value: 9.18e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678 1795 VTANCVVHSAY--DAKVSWLLDGKDPTSR----TPVNQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 1857
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGvkttPPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 46.09 E-value: 9.18e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678 2098 VTANCVVHSAY--DAKVSWLLDGKDPTSR----TPVNQASSTTQsISSNLTLPSSQWKTLNTITCRAEH 2160
Cdd:pfam07654   15 NTLTCLVTGFYppDITVTWLKNGQEVTEGvkttPPSPNSDWTYQ-LSSYLTVTPSDWESGDEYTCRVEH 82

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: 46.25 E-value: 9.64e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  868 PSLHLETPRFRTVMTQTEVTATCVV--HSAYDAKVSWLLDGK----DPTSRAPVKQASSTTqSISSNLTLPSSQWKTLNT 941
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKT 79


                   ....*..
gi 1696205678  942 ITCRAEH 948
Cdd:cd05847     80 YTCKVTH 86

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: 46.25 E-value: 9.64e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1171 PSLHLETPRFRTVMTQTEVTATCVV--HSAYDAKVSWLLDGK----DPTSRAPVKQASSTTqSISSNLTLPSSQWKTLNT 1244
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKT 79


                   ....*..
gi 1696205678 1245 ITCRAEH 1251
Cdd:cd05847     80 YTCKVTH 86

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409513 Cd Length: 99 Bit Score: 46.23 E-value: 1.03e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  766 PSMELLLVANEDLSGSGTQKIMCSGRGFNPQ---IKWLSGTKQ----RSAADNERRIREDGHVAVTSHITVTQQEWNEGK 838
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLRNGKEvtssTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81


                   ....*....
gi 1696205678  839 DFICEVIDK 847
Cdd:cd16093     82 EFTCEFKHK 90

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409513 Cd Length: 99 Bit Score: 46.23 E-value: 1.03e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1069 PSMELLLVANEDLSGSGTQKIMCSGRGFNPQ---IKWLSGTKQ----RSAADNERRIREDGHVAVTSHITVTQQEWNEGK 1141
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLRNGKEvtssTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81


                   ....*....
gi 1696205678 1142 DFICEVIDK 1150
Cdd:cd16093     82 EFTCEFKHK 90

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: 46.56 E-value: 1.05e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  280 VTATCVVHSAY--DAKVSWLLDGKD-PTSR---TPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHR--CFNTTQRT 351
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGEPlPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDVFSCVVGHEalPLQFTQKS 98

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409513 Cd Length: 99 Bit Score: 46.23 E-value: 1.12e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1675 PSMELLLVANEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQ----RSAADNERRIREDGHVAVTSHITVTQQEWNEGK 1747
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLRNGKEvtssTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81


                   ....*....
gi 1696205678 1748 DFICEVIDK 1756
Cdd:cd16093     82 EFTCEFKHK 90

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant domain (IgC) of mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.

Pssm-ID: 409513 Cd Length: 99 Bit Score: 46.23 E-value: 1.12e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1978 PSMELLLVANEDLSGSGTQKLMCSGRGFNPQ---IKWLSGSKQ----RSAADNERRIREDGHVAVTSHITVTQQEWNEGK 2050
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLRNGKEvtssTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81


                   ....*....
gi 1696205678 2051 DFICEVIDK 2059
Cdd:cd16093     82 EFTCEFKHK 90

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: 46.30 E-value: 1.14e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1185 TQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRAPVKQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNPTQT 1259
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678 1260 TS 1261
Cdd:cd07699     95 KS 96

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: 46.30 E-value: 1.14e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  882 TQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRAPVKQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNPTQT 956
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678  957 TS 958
Cdd:cd07699     95 KS 96

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: 45.87 E-value: 1.28e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   51 LFPLAQCGSGTGDMMTLGCIATGFTPASLTFKWNEQG-GKSLTDFVQYPAVQTGGSYTGVSQLRVKRADWDS-KIFECAV 128
Cdd:cd05847      5 ILHSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGqVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSgKTYTCKV 84


                   ....*
gi 1696205678  129 EHSAG 133
Cdd:cd05847     85 THQGT 89

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: 45.91 E-value: 1.28e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  771 LLVANEDLSGSGTQKIMCSGRGFNP---QIKWLSGTKQRSAADNERRIRE--DGHVAVTSHITVTQQEWNEGKDFICEVI 845
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLKNGVPLTSGVSTSSPVEpnDGTYSVTSSLTVPPSDWDEGATYTCVVT 83

                           90
                   ....*....|..
gi 1696205678  846 DKDLQKTVRKST 857
Cdd:cd00098     84 HESLKSPLSKTW 95

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: 45.91 E-value: 1.28e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1074 LLVANEDLSGSGTQKIMCSGRGFNP---QIKWLSGTKQRSAADNERRIRE--DGHVAVTSHITVTQQEWNEGKDFICEVI 1148
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLKNGVPLTSGVSTSSPVEpnDGTYSVTSSLTVPPSDWDEGATYTCVVT 83

                           90
                   ....*....|..
gi 1696205678 1149 DKDLQKTVRKST 1160
Cdd:cd00098     84 HESLKSPLSKTW 95

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: 46.30 E-value: 1.29e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1488 TQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRAPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNPTQT 1562
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678 1563 TS 1564
Cdd:cd07699     95 KS 96

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

Pssm-ID: 409496 Cd Length: 99 Bit Score: 45.91 E-value: 1.32e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  276 TQTEVTATCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNTTQR 350
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678  351 TS 352
Cdd:cd07699     95 KS 96

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 45.38 E-value: 1.34e-05

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  1188 EVTATCVVHSAY--DAKVSWLLDGKDPTSRA---PVKQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 1251
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEGVsttDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 45.38 E-value: 1.34e-05

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678   885 EVTATCVVHSAY--DAKVSWLLDGKDPTSRA---PVKQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 948
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEGVsttDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) E; 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 (HLA) E. HLA-E is the first human class Ib major histocompatibility complex molecule to be crystallized. Like other MHC class I molecules, HLA-E is a heterodimer consisting of an a heavy chain and light chain beta-2-microglobulin. HLA-E is highly conserved and almost nonpolymorphic, and has recently been shown to be the first specialized ligand for natural killer cell receptors. 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: 409615 Cd Length: 95 Bit Score: 45.94 E-value: 1.47e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2488 KPPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGSrlPFSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdh 2567
Cdd:cd21024      4 EPPKTHVTHHPISD----HEATLRCWALGFYPAEITLTWQQDGE--GHTQDTELVETRPAGDGTFQKWAAVVVPSGE--- 74

                           90
                   ....*....|....*...
gi 1696205678 2568 NSNYSCAVRHESSERPIT 2585
Cdd:cd21024     75 EQRYTCHVQHEGLPEPVT 92

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 45.00 E-value: 1.54e-05

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  1491 EVTATCVVHSAY--DAKVSWLLDGKDPTSRA---PVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 1554
Cdd:smart00407    1 KATLVCLVSGFYppDITVTWLRNGQEVTEGVsttDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTH 69

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: 45.48 E-value: 1.75e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1675 PSMELLLVANEDLSGSGTQKLMCSGRGFNP---QIKWL-SGSKQRSAADNERRIREDGHVAVT-SHITVTQQEWNEGKDF 1749
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvDGQVATLSAASTAPQKEEGGTFSTtSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678 1750 ICEVI 1754
Cdd:cd05847     81 TCKVT 85

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: 45.48 E-value: 1.75e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1978 PSMELLLVANEDLSGSGTQKLMCSGRGFNP---QIKWL-SGSKQRSAADNERRIREDGHVAVT-SHITVTQQEWNEGKDF 2052
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvDGQVATLSAASTAPQKEEGGTFSTtSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678 2053 ICEVI 2057
Cdd:cd05847     81 TCKVT 85

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: 45.48 E-value: 2.08e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  463 PSMELLLVPNEDLSGSGTQKLMCSGRGFNP---QIKWL-SGSKQRSAADNERRMREDGHVAVT-SHITVTQQEWNEGKGF 537
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvDGQVATLSAASTAPQKEEGGTFSTtSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678  538 ICEVI 542
Cdd:cd05847     81 TCKVT 85

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: 45.48 E-value: 2.08e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1372 PSMELLLVPNEDLSGSGTQKLMCSGRGFNP---QIKWL-SGSKQRSAADNERRMREDGHVAVT-SHITVTQQEWNEGKGF 1446
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvDGQVATLSAASTAPQKEEGGTFSTtSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678 1447 ICEVI 1451
Cdd:cd05847     81 TCKVT 85

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: 45.58 E-value: 2.13e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhN 2568
Cdd:cd21023      5 PPKAHVAHHPISD----HEATLRCWALGFYPAEITLTWQRDGEEQ--TQDTELVETRPAGDGTFQKWAAVVVPPGE---E 75

                           90
                   ....*....|....*.
gi 1696205678 2569 SNYSCAVRHESSERPI 2584
Cdd:cd21023     76 QRYTCHVQHEGLPQPL 91

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: 45.14 E-value: 2.26e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1783 TPRFRTVMTQTEVTANCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 1857
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678 1858 RCFNPTQRTS 1867
Cdd:cd00098     85 ESLKSPLSKT 94

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: 45.14 E-value: 2.26e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2086 TPRFRTVMTQTEVTANCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEH 2160
Cdd:cd00098      5 LPPSPEEKGGGKVTLVCLVSGFYpkDITVTWLKNGVpltSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTH 84

                           90
                   ....*....|
gi 1696205678 2161 RCFNPTQRTS 2170
Cdd:cd00098     85 ESLKSPLSKT 94

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: 45.14 E-value: 2.72e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678 2286 LLVPNEDLSGSGTQKLMCSGRGFNP---QIKWL------SVSAAAYEIRMGDDERVAVTSQITVTQQEWNQGKNFTCEV 2355
Cdd:cd00098      4 LLPPSPEEKGGGKVTLVCLVSGFYPkdiTVTWLkngvplTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVV 82

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: 45.12 E-value: 3.19e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2492 IKIVRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGsRLP--------FSRYSsipsvlyagSSTYSMNSRLIVPRS 2563
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAG-KVPtggveeglLERHS---------NGSQSQHSRLTLPRS 71

                           90
                   ....*....|....*.
gi 1696205678 2564 EWDHNSNYSCAVRHES 2579
Cdd:cd16084     72 LWNAGTSVTCTLNHPS 87

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: 44.75 E-value: 3.58e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2385 VGVYLQGPTLQELRTDGQVPVTCLLVGL-SLGDFSVSWKV-DGVVASQggVTRAPKDHSNGTQTEQIMFNVPARDWHAHK 2462
Cdd:cd07696      1 VSVFLIPPSPKDLFLTKSAKVTCLVVDLtSIEEVNVTWSReDGNEVLA--STTNPEKHYNATLSVVSTLTVCADDWDNGK 78


                   ....*...
gi 1696205678 2463 LVSCEVKH 2470
Cdd:cd07696     79 TFKCKVTH 86

Signal-regulatory protein (SIRP) immunoglobulin-like domain 2; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in Signal-Regulatory Protein (SIRP), domain 2 (C1 repeat 1). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three Immunoglobulin superfamily domains, a single V-set and two C1-set IgSF domains. Their cytoplasmic tails contain either ITIMs or transmembrane regions that have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47, but with much less affinity.

Pssm-ID: 409429 Cd Length: 102 Bit Score: 45.01 E-value: 3.73e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2508 ATLLCLVSGFFPSDVIVNWEKAGSRLPfsrySSIPSVLYAGSS-TYSMNSRLIVPRSEWDHNSNYSCAVRHESSERPITS 2586
Cdd:cd05772     20 VSFTCKSHGFSPRDITLKWFKNGNELS----ALQTTVFPEGDSvSYSVSSTVQVVLTKDDVHSQLTCEVAHVTLQAPLRG 95


                   .
gi 1696205678 2587 T 2587
Cdd:cd05772     96 T 96

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: 44.53 E-value: 3.88e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2595 VTPSAPTATllQGPSELACLVLGFSSSDINITWLL-DDVTELWNNNTST-------TYRApggkfgiRSHLSLAHQdwtP 2666
Cdd:cd21002      8 VAPTTPFNT--REPVMLACHVWGFYPADVTITWLKnGDPVAPHSSAPKTaqpngdwTYQT-------QVTLAVTPS---P 75

                           90
                   ....*....|
gi 1696205678 2667 GAVYTCRVTH 2676
Cdd:cd21002     76 GDTYTCSVQH 85

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: 44.69 E-value: 4.29e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2281 PSMELLLVPNEDLSGSGTQKLMCSGRGFNPQ---IKWL--------SVSAAAYEIRMGDDERVAVTSQITVTQQEWNQGK 2349
Cdd:cd16093      2 PTVSLHAPSREEFLGNRTATFVCLATGFSPKtisFKWLrngkevtsSTGAVVEEPKEDGKTLYSATSFLTITESEWKSQT 81


                   ....*....
gi 1696205678 2350 NFTCEVIDK 2358
Cdd:cd16093     82 EFTCEFKHK 90

Class Ia major histocompatibility complex (MHC) immunoglobulin domain of RT1-Aa; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ia major histocompatibility complex (MHC) immunoglobulin domain of RT1-Aa. While most mammalian species transport these peptides into the ER via a single allele of TAP, rats have evolved different TAPs, TAP-A and TAP-B, RT1-Aa and RT1-A1c, which are associated with TAP-A and TAP-B. The rat MHC class Ia molecule RT1-Aa has the unusual capacity to bind long peptides ending in arginine, such as MTF-E, a thirteen-residue, maternally transmitted minor histocompatibility antigen. 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: 409606 Cd Length: 95 Bit Score: 44.37 E-value: 4.42e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2507 NATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPITS 2586
Cdd:cd21015     18 DVTLRCWALGFYPADITLTWQLNGEDL--TQDMELVETRPAGDGTFQKWASVVVPLGK---EQNYTCRVEHEGLPKPLSQ 92


                   ...
gi 1696205678 2587 TIE 2589
Cdd:cd21015     93 RWE 95

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

Pssm-ID: 409496 Cd Length: 99 Bit Score: 44.37 E-value: 4.71e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1791 TQTEVTANCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNPTQR 1865
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678 1866 TS 1867
Cdd:cd07699     95 KS 96

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

Pssm-ID: 409496 Cd Length: 99 Bit Score: 44.37 E-value: 4.71e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2094 TQTEVTANCVVHSAY--DAKVSWLLDGK---DPTSRTPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCFNPTQR 2168
Cdd:cd07699     15 SSGKATLVCLINKFYpgFATVTWKVDGStvsSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCEVTHEGLSSTIT 94


                   ..
gi 1696205678 2169 TS 2170
Cdd:cd07699     95 KS 96

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: 44.63 E-value: 4.83e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678  583 VTATCVVHSAY--DAKVSWLLDGKD-PTSR---TPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCfNPTQTTS 655
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGEPlPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDVFSCVVGHEA-LPLQFTQ 96

T cell receptor (TCR) gamma chain constant immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) constant (C) 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 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.

Pssm-ID: 409494 Cd Length: 98 Bit Score: 44.56 E-value: 4.91e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2487 PKPpsiKIVRPSDSDLWGSNNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSIPsvlYAGSSTYSMNSRLIVPRSEWD 2566
Cdd:cd07697      2 PKP---TIFLPSIAETEKQKAGTYLCLLENFFPDVIKIHWREKKSDTILESQEGNT---EKTKDTYMKFSWLTVPKKSLG 75

                           90       100
                   ....*....|....*....|..
gi 1696205678 2567 hnSNYSCAVRHESSERPITSTI 2588
Cdd:cd07697     76 --KEHRCIYKHENNKNGVKQEI 95

Class Ia major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) H2Db and H2Ld; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ia major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) H2Db and H2Ld. H-2Ld complexed with peptide QL9 (or p2Ca) and complexed with influenza virus peptide NP366-374 (ASNEN-METM), respectively are high-affinity alloantigens for the 2C T cell receptor (TCR). The a1-a2 super domains of H-2Ld, H-2Db, and H-2Kb closely superimpose. 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: 409609 Cd Length: 95 Bit Score: 44.35 E-value: 5.85e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696205678 2509 TLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPIT 2585
Cdd:cd21018     21 TLRCWALGFYPADITLTWQLNGEEL--TQDMELVETRPAGDGTFQKWASVVVPLGK---EQNYTCRVYHEGLPEPLT 92

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

Pssm-ID: 409424 Cd Length: 95 Bit Score: 43.83 E-value: 6.47e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKiVRPSDSDLWGSNNaTLLCLVSGFFPSDVIVNWEKAGSrlPFSRYSSiPSVLYAgSSTYSMN--SRLIVPRSEWD 2566
Cdd:cd05767      2 PPEVT-VFPKSPVELGEPN-TLICFVDNFFPPVINVTWLRNGQ--PVTDGVS-ETVFLP-REDHSFRkfSYLPFTPSEGD 75

                           90
                   ....*....|....*....
gi 1696205678 2567 HnsnYSCAVRHESSERPIT 2585
Cdd:cd05767     76 I---YDCRVEHWGLEEPLL 91

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: 43.94 E-value: 6.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1474 PSLHLETPRFRTVMTQTEVTATCVV--HSAYDAKVSWLLDGK----DPTSRAPVNQASSTTqSISSNLTLPSSQWKTLNT 1547
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKT 79


                   ....*..
gi 1696205678 1548 ITCRAEH 1554
Cdd:cd05847     80 YTCKVTH 86

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: 43.86 E-value: 6.98e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVrPSDSDLWGSNNaTLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSipSVLYAGSSTYSMNSRL-IVPRsewdH 2567
Cdd:cd05766      3 QPSVKVS-PTKTGPLEHPN-LLVCSVTGFYPAEIEVKWFRNGQEETAGVVST--ELIPNGDWTFQILVMLeTTPR----R 74

                           90
                   ....*....|....*...
gi 1696205678 2568 NSNYSCAVRHESSERPIT 2585
Cdd:cd05766     75 GDVYTCQVEHSSLQSPLT 92

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: 8.01e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2594 SVTPSAPTATLLQGPSELACLVLGFSSSDINITWLLDD---------VTELWNNNTSTTYRAPggkfgirSHLSLAHQDW 2664
Cdd:cd16093      5 SLHAPSREEFLGNRTATFVCLATGFSPKTISFKWLRNGkevtsstgaVVEEPKEDGKTLYSAT-------SFLTITESEW 77

                           90       100
                   ....*....|....*....|..
gi 1696205678 2665 TPGAVYTCRVTHTTQNLALNIS 2686
Cdd:cd16093     78 KSQTEFTCEFKHKGEIVEKNAS 99

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: 43.59 E-value: 8.45e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1382 EDLSGSGTQKLMC------SGRGFNpqIKWLSGSKQR-SAADNERRMREDGHVAVTSHITVTQQEWNEGKGFICEVIDKD 1454
Cdd:cd07696     11 KDLFLTKSAKVTClvvdltSIEEVN--VTWSREDGNEvLASTTNPEKHYNATLSVVSTLTVCADDWDNGKTFKCKVTHPD 88

                           90
                   ....*....|
gi 1696205678 1455 LQKTVRKSIS 1464
Cdd:cd07696     89 LPSPIVKSIQ 98

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: 43.59 E-value: 8.45e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  473 EDLSGSGTQKLMC------SGRGFNpqIKWLSGSKQR-SAADNERRMREDGHVAVTSHITVTQQEWNEGKGFICEVIDKD 545
Cdd:cd07696     11 KDLFLTKSAKVTClvvdltSIEEVN--VTWSREDGNEvLASTTNPEKHYNATLSVVSTLTVCADDWDNGKTFKCKVTHPD 88

                           90
                   ....*....|
gi 1696205678  546 LQKTVRKSIS 555
Cdd:cd07696     89 LPSPIVKSIQ 98

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: 43.93 E-value: 8.64e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhN 2568
Cdd:cd21016      5 PPKAHVTRHPRPE----GDVTLRCWALGFYPADITLTWQKDGEEL--TQDMEFVETRPAGDGTFQKWAAVVVPLGK---E 75

                           90
                   ....*....|....*..
gi 1696205678 2569 SNYSCAVRHESSERPIT 2585
Cdd:cd21016     76 QSYTCHVYHEGLPEPLT 92

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: 43.54 E-value: 9.09e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678 2112 VSWLLDGKDPTSRTPVNQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHR 2161
Cdd:cd16093     36 FKWLRNGKEVTSSTGAVVEepkedGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

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: 43.54 E-value: 9.09e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678 1809 VSWLLDGKDPTSRTPVNQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHR 1858
Cdd:cd16093     36 FKWLRNGKEVTSSTGAVVEepkedGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

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: 43.54 E-value: 9.09e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678  597 VSWLLDGKDPTSRTPVNQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHR 646
Cdd:cd16093     36 FKWLRNGKEVTSSTGAVVEepkedGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

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: 43.54 E-value: 9.09e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678  294 VSWLLDGKDPTSRTPVNQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHR 343
Cdd:cd16093     36 FKWLRNGKEVTSSTGAVVEepkedGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

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: 43.58 E-value: 9.14e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1173 LHLETPRFRTVMTQTEVTATCVVHSA--YDAKVSWLLDGKDPT---SRAPVKQASSTTQSISSNLTLPSSQWKTLNTITC 1247
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTggvEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81

                           90
                   ....*....|.
gi 1696205678 1248 RAEHRCFNPTQ 1258
Cdd:cd16084     82 TLNHPSLPPQR 92

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: 43.58 E-value: 9.14e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  870 LHLETPRFRTVMTQTEVTATCVVHSA--YDAKVSWLLDGKDPT---SRAPVKQASSTTQSISSNLTLPSSQWKTLNTITC 944
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTggvEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81

                           90
                   ....*....|.
gi 1696205678  945 RAEHRCFNPTQ 955
Cdd:cd16084     82 TLNHPSLPPQR 92

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: 43.55 E-value: 9.34e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  766 PSMELLLVANEDLSGSGTQKIMCSGRGFNP---QIKWL-SGTKQRSAADNERRIREDGHVAVT-SHITVTQQEWNEGKDF 840
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvDGQVATLSAASTAPQKEEGGTFSTtSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678  841 ICEVI 845
Cdd:cd05847     81 TCKVT 85

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: 43.55 E-value: 9.34e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1069 PSMELLLVANEDLSGSGTQKIMCSGRGFNP---QIKWL-SGTKQRSAADNERRIREDGHVAVT-SHITVTQQEWNEGKDF 1143
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvDGQVATLSAASTAPQKEEGGTFSTtSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678 1144 ICEVI 1148
Cdd:cd05847     81 TCKVT 85

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: 43.91 E-value: 1.03e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   66 TLGCIATGFTPASLTFKWnEQGGKSLTDFVQYPAVQTGGS---YTGVSQLRVKRADWD--SKIFECAVEHSAGSKTVPVK 140
Cdd:cd05769     22 TLVCLATGFYPDHVSLSW-KVNGKEVKDGVATDPQALRENtstYSLSSRLRVSATEWFnpRNTFTCIVKFYGGTDTDTWT 100


                   .
gi 1696205678  141 K 141
Cdd:cd05769    101 Q 101

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) G; 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 (HLA) G. HLA-G histocompatibility antigen (also known as human leukocyte antigen G ; HLA-G) is a protein that in humans is encoded by the HLA-G gene. HLA-G belongs to the HLA nonclassical class I heavy chain paralogs. This class I molecule is a heterodimer consisting of a heavy chain and light chain, beta-2-microglobulin. The heavy chain is anchored in the membrane. HLA-G may play a role in immune tolerance in pregnancy, being expressed in the placenta by extravillous trophoblast cells (EVT), while the classical MHC class I genes (HLA-A and HLA-B) are not. Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I and class II. 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. MHC class II molecules play a key role in the initiation of the antigen-specific immune repose. 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: 409613 Cd Length: 94 Bit Score: 43.21 E-value: 1.11e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696205678 2508 ATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPI 2584
Cdd:cd21022     19 ATLRCWALGFYPAEIILTWQRDGEDQ--TQDVELVETRPAGDGTFQKWAAVVVPSGE---EQRYTCHVQHEGLPEPL 90

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: 43.55 E-value: 1.11e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2281 PSMELLLVPNEDLSGSGTQKLMCSGRGFNP---QIKWL------SVSAAAYEIRMGDDERVAVTSQITVTQQEWNQGKNF 2351
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLISGYTPstiEVEWLvdgqvaTLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTY 80


                   ....*
gi 1696205678 2352 TCEVI 2356
Cdd:cd05847     81 TCKVT 85

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: 43.54 E-value: 1.12e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678 1203 VSWLLDGKDPTSRAPV-----KQASSTTQSISSNLTLPSSQWKTLNTITCRAEHR 1252
Cdd:cd16093     36 FKWLRNGKEVTSSTGAvveepKEDGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

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: 43.54 E-value: 1.12e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678  900 VSWLLDGKDPTSRAPV-----KQASSTTQSISSNLTLPSSQWKTLNTITCRAEHR 949
Cdd:cd16093     36 FKWLRNGKEVTSSTGAvveepKEDGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of Qa-2; 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 QA-2. Qa-2 is a nonclassical MHC Ib antigen, which has been implicated in both innate and adaptive immune responses, as well as embryonic development. Qa-2 has an unusual peptide binding specificity in that it requires two dominant C-terminal anchor residues and is capable of associating with a substantially more diverse array of peptide sequences than other nonclassical MHC. 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: 409605 Cd Length: 94 Bit Score: 43.20 E-value: 1.15e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696205678 2509 TLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPIT 2585
Cdd:cd21014     20 TLRCWALGFYPADITLTWQLNGEEL--TQDMELVETRPAGDGTFQKWASVVVPLGK---EQNYTCHVNHEGLPEPLT 91

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 43.01 E-value: 1.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  467 LLLVPNEDLSGSGTqkLMCSGRGFNP---QIKWLS-GSKQRSAADN-ERRMREDGHVAVTSHITVTQQEWNEGKGFICEV 541
Cdd:pfam07654    3 VFPPSPEELGKPNT--LTCLVTGFYPpdiTVTWLKnGQEVTEGVKTtPPSPNSDWTYQLSSYLTVTPSDWESGDEYTCRV 80

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 43.01 E-value: 1.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1376 LLLVPNEDLSGSGTqkLMCSGRGFNP---QIKWLS-GSKQRSAADN-ERRMREDGHVAVTSHITVTQQEWNEGKGFICEV 1450
Cdd:pfam07654    3 VFPPSPEELGKPNT--LTCLVTGFYPpdiTVTWLKnGQEVTEGVKTtPPSPNSDWTYQLSSYLTVTPSDWESGDEYTCRV 80

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: 43.20 E-value: 1.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1476 LHLETPRFRTVMTQTEVTATCVVHSA--YDAKVSWLLDGKDPT---SRAPVNQASSTTQSISSNLTLPSSQWKTLNTITC 1550
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTggvEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81

                           90
                   ....*....|.
gi 1696205678 1551 RAEHRCFNPTQ 1561
Cdd:cd16084     82 TLNHPSLPPQR 92

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

Pssm-ID: 409428 Cd Length: 100 Bit Score: 43.25 E-value: 1.33e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  149 PNITLYPLWEELEGGSKVgLLCILSEFYPDKLSVEWLLDDKTVTTSPVQRK-------LQSVEGeekTFSLSSQLELDQS 221
Cdd:cd05771      1 PRVRLSPKNLVKPDLPQT-LSCHIAGYYPLDVDVEWLREEPGGSESQVSRDgvslsshRQSVDG---TYSISSYLTLEPG 76

                           90       100
                   ....*....|....*....|
gi 1696205678  222 QWTQGSEVTCKAIHNAAQGP 241
Cdd:cd05771     77 TENRGATYTCRVTHVSLEEP 96

Immunoglobulin C-Type;

Pssm-ID: 214651 Cd Length: 75 Bit Score: 42.30 E-value: 1.52e-04

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696205678    66 TLGCIATGFTPASLTFKWNEQG-----GKSLTDFVQypavQTGGSYTGVSQLRVKRADWDS-KIFECAVEHSA 132
Cdd:smart00407    3 TLVCLVSGFYPPDITVTWLRNGqevteGVSTTDPLK----NSDGTYFLSSYLTVPASTWESgDVYTCQVTHEG 71

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: 42.81 E-value: 1.69e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  567 LHLETPRFRTVMTQTEVTATCVVHSA--YDAKVSWLLDGKDPTSRTP---VNQASSTTQSISSNLTLPSSQWKTLNTITC 641
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTGGVEeglLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81

                           90
                   ....*....|.
gi 1696205678  642 RAEHRCFNPTQ 652
Cdd:cd16084     82 TLNHPSLPPQR 92

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: 42.96 E-value: 1.88e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2599 APTATLLQ--------GPSELACLVLGFSSSDINITWLLDDVTELwnnnTSTTYRAP-----GGKFGIRSHLSLAHQDWT 2665
Cdd:cd04985      1 APTVFPLQsatksqsnGPVALGCLISDYFPESITVSWQKNTNSIT----SGFTRTFPvvlrsGGDYSCSSQLTVPLQEWN 76

                           90
                   ....*....|....*
gi 1696205678 2666 PGAVYTCRVTHTTQN 2680
Cdd:cd04985     77 SGEVYKCQVQHSASN 91

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: 42.78 E-value: 2.02e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  565 PSLHLETPRFRTVMTQTEVTATCVV--HSAYDAKVSWLLDGK----DPTSRTPVNQASSTTqSISSNLTLPSSQWKTLNT 638
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKT 79


                   ....*..
gi 1696205678  639 ITCRAEH 645
Cdd:cd05847     80 YTCKVTH 86

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: 42.71 E-value: 2.10e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1492 VTATCVVHSAY--DAKVSWLLDGKdPTSRA-----PVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHRCfNPTQTTS 1564
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGE-PLPSAdykttAPVPESDGSFFVYSKLNVSTADWNSGDVFSCVVGHEA-LPLQFTQ 96

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of Qa-1 and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; Class Ib major histocompatibility complex (MHC) immunoglobulin domain of Qa-1 and similar proteins. Qa-1 presents hydrophobic peptides including Qdm derived from the leader sequence of classical MHC I molecules for immune surveillance by NK cells. Qa-1 bound peptides derived from the TCR Vbeta8.2 of activated T cells also activates CD8+ regulatory T cells to control autoimmunity and maintain self-tolerance. Four allotypes of Qa-1 (Qa-1a-d) are expressed that are highly conserved in sequence but have several variations that could affect peptide binding to Qa-1 or TCR recognition. 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: 409604 Cd Length: 97 Bit Score: 42.80 E-value: 2.17e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhN 2568
Cdd:cd21013      4 PPKAHVTHHPRSE----GYVTLRCWALGFYPADITLTWQLNGEEL--TQDMEFVETRPAGDGTFQKWASVVVPLGK---E 74

                           90
                   ....*....|....*..
gi 1696205678 2569 SNYSCAVRHESSERPIT 2585
Cdd:cd21013     75 QKYTCHVEHEGLPEPLT 91

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: 42.71 E-value: 2.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2098 VTANCVVHSAY--DAKVSWLLDGKD-PTSR---TPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHR--CFNPTQRT 2169
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGEPlPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDVFSCVVGHEalPLQFTQKS 98

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: 42.71 E-value: 2.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1795 VTANCVVHSAY--DAKVSWLLDGKD-PTSR---TPVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHR--CFNPTQRT 1866
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGEPlPSADyktTAPVPESDGSFFVYSKLNVSTADWNSGDVFSCVVGHEalPLQFTQKS 98

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: 42.37 E-value: 2.67e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2490 PSIKIVRPSDSDLWGSNNATLLCLVSGFF-PSDVIVNWEKAGSRLPFSRYSSIPSvlyagSSTYSMNSRLIVPRSEWDHN 2568
Cdd:cd04986      2 PRLSLQRPALEDLLLGSNASLTCTLSGLKdPEGATFTWEPSGGKEAIQGPPERDS-----CGCYSVSSVLPGCAEPWNSG 76

                           90       100
                   ....*....|....*....|
gi 1696205678 2569 SNYSCAVRHESSERPITSTI 2588
Cdd:cd04986     77 DTFSCTVTHPESKGTLTATI 96

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: 42.06 E-value: 2.80e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1576 TVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 1653
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678 1654 KVN 1656
Cdd:cd00098     81 VVT 83

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: 42.06 E-value: 2.80e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  667 TVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 744
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678  745 KVN 747
Cdd:cd00098     81 VVT 83

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: 42.06 E-value: 2.80e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1879 TVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 1956
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678 1957 KVN 1959
Cdd:cd00098     81 VVT 83

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: 42.06 E-value: 2.80e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  364 TVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 441
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678  442 KVN 444
Cdd:cd00098     81 VVT 83

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: 42.06 E-value: 2.80e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2182 TVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 2259
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678 2260 KVN 2262
Cdd:cd00098     81 VVT 83

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of Qa-1b; member of the C1-set of Ig superfamily (IgSF) domains; The non-classical mouse MHC class I (MHC-I) molecule Qa-1b is a non-polymorphic MHC molecule with an important function in innate immunity. It binds and presents signal peptides of classical MHC-I molecules at the cell surface and, as such, act as an indirect sensor for the normal expression of MHC-I molecules. This signal peptide dominantly accommodated in the groove of Qa-1b is called Qdm, for Qa-1 determinant modifier, and its amino acid sequence AMAPRTLLL is highly conserved among mammalian species. The Qdm/Qa-1b complex serves as a ligand for the germ-line encoded heterodimeric CD94/NKG2A receptors expressed on natural killer (NK) cells and activated CD8+ T cells and transduces inhibitory signals to these lymphocytes. Thus, upon binding, Qa-1b signals NK cells not to engage in cell lysis. The molecular basis of Qa-1b function is unclear.

Pssm-ID: 409625 Cd Length: 98 Bit Score: 42.45 E-value: 2.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2489 PPSIKIVRPSDSDlwgsNNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEWDHn 2568
Cdd:cd21820      5 PPKAHVTHHPRSE----DEVTLRCWALGFYPADITLTWQLNGEEL--TQDMELVETRPAGDGTFQKWAAVVVPLGKEQY- 77

                           90
                   ....*....|....*..
gi 1696205678 2569 snYSCAVRHESSERPIT 2585
Cdd:cd21820     78 --YTCHVYHEGLPEPLT 92

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: 42.32 E-value: 3.12e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  886 VTATCVVHSAY--DAKVSWLLDGKdPTSRAPVKQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHRCfNPTQTTS 958
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGE-PLPSADYKTTapvpeSDGSFFVYSKLNVSTADWNSGDVFSCVVGHEA-LPLQFTQ 96

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: 42.32 E-value: 3.12e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1189 VTATCVVHSAY--DAKVSWLLDGKdPTSRAPVKQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHRCfNPTQTTS 1261
Cdd:cd05768     19 VTLTCLVKGFYpeDIFVSWLQNGE-PLPSADYKTTapvpeSDGSFFVYSKLNVSTADWNSGDVFSCVVGHEA-LPLQFTQ 96

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: 42.00 E-value: 3.16e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1696205678 1506 VSWLLDGKDPTSRAPVNQA-----SSTTQSISSNLTLPSSQWKTLNTITCRAEHR 1555
Cdd:cd16093     36 FKWLRNGKEVTSSTGAVVEepkedGKTLYSATSFLTITESEWKSQTEFTCEFKHK 90

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: 3.52e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696205678  273 TVMTQTEVTATCVV--HSAYDAKVSWLLDGK----DPTSRTPVNQASSTTqSISSNLTLPSSQWKTLNTITCRAEH 342
Cdd:cd05847     12 STLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKTYTCKVTH 86

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: 3.84e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2080 PSLHLETPRFRTVMTQTEVTANCVV--HSAYDAKVSWLLDGK----DPTSRTPVNQASSTTqSISSNLTLPSSQWKTLNT 2153
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKT 79


                   ....*..
gi 1696205678 2154 ITCRAEH 2160
Cdd:cd05847     80 YTCKVTH 86

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: 3.84e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1777 PSLHLETPRFRTVMTQTEVTANCVV--HSAYDAKVSWLLDGK----DPTSRTPVNQASSTTqSISSNLTLPSSQWKTLNT 1850
Cdd:cd05847      1 PTVQILHSSCASTLTSETIQLLCLIsgYTPSTIEVEWLVDGQvatlSAASTAPQKEEGGTF-STTSKLNVTQEDWKSGKT 79


                   ....*..
gi 1696205678 1851 ITCRAEH 1857
Cdd:cd05847     80 YTCKVTH 86

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: 41.65 E-value: 4.70e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  264 LHLETPRFRTVMTQTEVTATCVVHSA--YDAKVSWLLDGKDPTSRTP---VNQASSTTQSISSNLTLPSSQWKTLNTITC 338
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTGGVEeglLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81


                   ....
gi 1696205678  339 RAEH 342
Cdd:cd16084     82 TLNH 85

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: 41.68 E-value: 4.79e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  970 TVLIRRTLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 1047
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678 1048 KVN 1050
Cdd:cd00098     81 VVT 83

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: 41.68 E-value: 4.79e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1273 TVLIRRTLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVDLPASKDHH--SLTRRFSIPTSHWKKDNTFTC 1350
Cdd:cd00098      1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGVSTSSPVEPNDGtySVTSSLTVPPSDWDEGATYTC 80


                   ...
gi 1696205678 1351 KVN 1353
Cdd:cd00098     81 VVT 83

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 41.08 E-value: 5.16e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 1998 LMCSGRGFNP---QIKWLS-GSKQRSAADNERRIRE-DGHVAVTSHITVTQQEWNEGKDFICEV 2056
Cdd:pfam07654   17 LTCLVTGFYPpdiTVTWLKnGQEVTEGVKTTPPSPNsDWTYQLSSYLTVTPSDWESGDEYTCRV 80

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 41.08 E-value: 5.16e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 1695 LMCSGRGFNP---QIKWLS-GSKQRSAADNERRIRE-DGHVAVTSHITVTQQEWNEGKDFICEV 1753
Cdd:pfam07654   17 LTCLVTGFYPpdiTVTWLKnGQEVTEGVKTTPPSPNsDWTYQLSSYLTVTPSDWESGDEYTCRV 80

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: 41.28 E-value: 5.54e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  766 PSMELLLVANEDLSGSGTQKIMC------SGRGFNpqIKWL-SGTKQRSAADNERRIREDGHVAVTSHITVTQQEWNEGK 838
Cdd:cd07696      1 VSVFLIPPSPKDLFLTKSAKVTClvvdltSIEEVN--VTWSrEDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGK 78

                           90       100
                   ....*....|....*....|
gi 1696205678  839 DFICEVIDKDLQKTVRKSTS 858
Cdd:cd07696     79 TFKCKVTHPDLPSPIVKSIQ 98

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: 41.28 E-value: 5.54e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1069 PSMELLLVANEDLSGSGTQKIMC------SGRGFNpqIKWL-SGTKQRSAADNERRIREDGHVAVTSHITVTQQEWNEGK 1141
Cdd:cd07696      1 VSVFLIPPSPKDLFLTKSAKVTClvvdltSIEEVN--VTWSrEDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGK 78

                           90       100
                   ....*....|....*....|
gi 1696205678 1142 DFICEVIDKDLQKTVRKSTS 1161
Cdd:cd07696     79 TFKCKVTHPDLPSPIVKSIQ 98

Class Ib major histocompatibility complex (MHC) immunoglobulin domain of HLA-Cw3 and HLA-Cw4; 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 HLA-Cw3 and HLA-Cw4. HLA-C belongs to the MHC class I heavy chain receptors. The C receptor is a heterodimer consisting of a HLA-C mature gene product and beta-2-microglobulin. The mature C chain is anchored in the membrane. MHC Class I molecules, like HLA-C, are expressed in nearly all cells, and present small peptides to the immune system which surveys for non-self peptides. HLA-C is a locus on chromosome 6, which encodes for a large number of HLA-C alleles that are Class-I MHC receptors. Class Ib histocompatibility leukocyte antigens (HLA)-Cw3 and (HLA)-Cw4 are ligands for the natural killer (NK) cell inhibitory receptors KIR2DL2 and KIR2DL1, respectively. HLA-Cw3 and related alleles (HLA-Cw1, -Cw7, and -Cw8) contain Ser77 and Asn80 and interact with KIR that are reactive with the GL183 antibody Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. HLA-Cw4 and related alleles (HLA-Cw2, -Cw5, and -Cw6) have Asn77 and Lys80 and are recognized by KIR reactive with the EB6 15 or HP-3E4 16 antibody. 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: 409616 Cd Length: 96 Bit Score: 41.33 E-value: 5.78e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2506 NNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPIT 2585
Cdd:cd21025     18 HEATLRCWALGFYPAEITLTWQWDGEDQ--TQDTELVETRPAGDGTFQKWAAVVVPSGE---EQRYTCHVQHEGLPEPLT 92

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 1586 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 1656
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 2192 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 2262
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 1889 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 1959
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 1283 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 1353
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678  980 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 1050
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678  677 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 747
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

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: 41.55 E-value: 6.60e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678  374 LLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEKQYVD---LPASKDHHSLTRRFSIPTSHWKKDNTFTCKVN 444
Cdd:cd05768     13 LSLNETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTtapVPESDGSFFVYSKLNVSTADWNSGDVFSCVVG 86

Class Ia major histocompatibility complex (MHC) immunoglobulin domain of H2-Dd; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ia major histocompatibility complex (MHC) immunoglobulin domain of H2-Dd. Mouse MHC is composed of 11 subclasses. It includes the classical MHC class I (MHC-Ia) that comprises H-2D, H-2K and H-2L subclasses, the non-classical MHC class I (MHCIb) that comprises H-2Q, H-2M and H-2T subclasses, the classical MHC class II (MHC-IIa) that includes H-2A(I-A) and H-2E(I-E) subclasses, and the non-classical MHC class II (MHC-IIb) comprises H-2M and H-2O. H-2K, H-2D, and H-2L are 80 to 90% homologous at the amino acid level yet appear to be involved in different recognition reactions and are differentially expressed on lymphoid cells. 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: 409611 Cd Length: 95 Bit Score: 41.28 E-value: 6.76e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696205678 2507 NATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPIT 2585
Cdd:cd21020     19 DVTLRCWALGFYPADITLTWQLNGEEL--TQEMELVETRPAGDGTFQKWASVVVPLGK---EQKYTCHVEHEGLPEPLT 92

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: 40.98 E-value: 7.28e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696205678  164 SKVGLLCILSEFYPDKLSVEWLLDdktvTTSPVQRKLQSVEGEEKTFSLSSQLELDQSQWTQGsEVTCKAIHNAAQ 239
Cdd:cd16092     18 SPVVLACLITGYHPTSVTVTWYMG----TQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQG-EYKCVVQHTASK 88

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: 40.90 E-value: 7.35e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1978 PSMELLLVANEDLSGSGTQKLMC------SGRGFNpqIKWLSGSKQR-SAADNERRIREDGHVAVTSHITVTQQEWNEGK 2050
Cdd:cd07696      1 VSVFLIPPSPKDLFLTKSAKVTClvvdltSIEEVN--VTWSREDGNEvLASTTNPEKHYNATLSVVSTLTVCADDWDNGK 78

                           90       100
                   ....*....|....*....|
gi 1696205678 2051 DFICEVIDKDLQKTVRKSTS 2070
Cdd:cd07696     79 TFKCKVTHPDLPSPIVKSIQ 98

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: 40.90 E-value: 7.35e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1675 PSMELLLVANEDLSGSGTQKLMC------SGRGFNpqIKWLSGSKQR-SAADNERRIREDGHVAVTSHITVTQQEWNEGK 1747
Cdd:cd07696      1 VSVFLIPPSPKDLFLTKSAKVTClvvdltSIEEVN--VTWSREDGNEvLASTTNPEKHYNATLSVVSTLTVCADDWDNGK 78

                           90       100
                   ....*....|....*....|
gi 1696205678 1748 DFICEVIDKDLQKTVRKSTS 1767
Cdd:cd07696     79 TFKCKVTHPDLPSPIVKSIQ 98

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: 40.88 E-value: 7.66e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1779 LHLETPRFRTVMTQTEVTANCVVHSA--YDAKVSWLLDGKDPTSRTP---VNQASSTTQSISSNLTLPSSQWKTLNTITC 1853
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTGGVEeglLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81

                           90
                   ....*....|.
gi 1696205678 1854 RAEHRCFNPTQ 1864
Cdd:cd16084     82 TLNHPSLPPQR 92

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: 40.88 E-value: 7.66e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2082 LHLETPRFRTVMTQTEVTANCVVHSA--YDAKVSWLLDGKDPTSRTP---VNQASSTTQSISSNLTLPSSQWKTLNTITC 2156
Cdd:cd16084      2 VYLLTPAVQDLWLRDKATFTCFVVGSdlKDAHLTWEVAGKVPTGGVEeglLERHSNGSQSQHSRLTLPRSLWNAGTSVTC 81

                           90
                   ....*....|.
gi 1696205678 2157 RAEHRCFNPTQ 2167
Cdd:cd16084     82 TLNHPSLPPQR 92

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 40.31 E-value: 9.85e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678  786 IMCSGRGFNP---QIKWLS-GTKQRSAADNERRIRE-DGHVAVTSHITVTQQEWNEGKDFICEV 844
Cdd:pfam07654   17 LTCLVTGFYPpdiTVTWLKnGQEVTEGVKTTPPSPNsDWTYQLSSYLTVTPSDWESGDEYTCRV 80

Immunoglobulin C1-set domain;

Pssm-ID: 462221 Cd Length: 85 Bit Score: 40.31 E-value: 9.85e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 1089 IMCSGRGFNP---QIKWLS-GTKQRSAADNERRIRE-DGHVAVTSHITVTQQEWNEGKDFICEV 1147
Cdd:pfam07654   17 LTCLVTGFYPpdiTVTWLKnGQEVTEGVKTTPPSPNsDWTYQLSSYLTVTPSDWESGDEYTCRV 80

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: 40.26 E-value: 1.04e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2495 VRPSDSDLWGSNNATLLCLVSgFFPSDVIVNWEKAGSRLPFSRYSSIpsvlyaGSSTYSMNSRLIVPRSEWDHnSNYSCA 2574
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAS-TGSPGPDVTWSKEGGTLIESLKVKH------DNGRTTQSSLLISNVTKEDA-GTYTCV 72

                           90
                   ....*....|....
gi 1696205678 2575 VRHESSERPITSTI 2588
Cdd:pfam00047   73 VNNPGGSATLSTSL 86

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: 40.00 E-value: 1.54e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696205678 2606 QGPSELACLVLGFSSSDINITWLLDDVtELWNNNTSTTYRAPG-GKFGIRSHLSLAHQDwtpGAVYTCRVTHTT 2678
Cdd:cd21029     15 DGHLQLSCHVTGFYPRPIEVTWLRDGQ-EQMDGTQSGGILPNHdGTYQLRKTLDIAPGE---GAGYSCRVDHSS 84

H-2 class I histocompatibility complex TLA (thymus leukemia antigen); member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the major histocompatibility complex (MHC) H-2 class I histocompatibility complex TLA (thymus leukemia antigen). The murine MHC class I histocompatibility TLA (Thymus leukemia antigen), which is encoded in the T region by T3 and T18 genes, is expressed mainly by intestinal epithelial cells and thymocytes. The murine TLAs are class I, beta-2-microglobulin-associated glycoproteins. The TLA function is not defined by antigen presentation, but rather by its relatively high affinity binding to CD8-alpha-alpha compared with CD8-alpha-beta. The existence of a human homolog for murine TLA remains unresolved. This group is a member of the C1-set Ig domains, which 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: 409603 Cd Length: 95 Bit Score: 39.71 E-value: 1.88e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696205678 2509 TLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPIT 2585
Cdd:cd21012     21 TLRCWALGFYPAHITLTWQLNGEEL--IQDTELVETRPAGDGTFQKWAAVVVPSGE---EQKYTCHVYHEGLPEPLT 92

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: 39.82 E-value: 1.95e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2481 ITKCRDPKPPSikivrpsdsdlwgsnNATLLCLVSGFFPSDVIVNWEKAGSRLPFSRYSSIPSvlyaGSSTYSMNSRLIV 2560
Cdd:cd16092      8 ISGCRHPKDNS---------------PVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQR----RDSYYMTSSQLST 68

                           90       100
                   ....*....|....*....|.
gi 1696205678 2561 PRSEWdHNSNYSCAVRHESSE 2581
Cdd:cd16092     69 PLQQW-RQGEYKCVVQHTASK 88

Class Ia major histocompatibility complex (MHC) immunoglobulin domain of H-2Kb; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the Class Ia major histocompatibility complex (MHC) immunoglobulin domain of H-2Kb. H-2Kb is an alloantigen for the 2C T cell receptor (TCR). H-2Kb forms a complex with beta-2-microglobulin, and a peptide, including VSV-8 (RGYVYNGL), SEV-9 (FAPGNYPAL), and OVA-8 (SIINFEKL). Comparison of the OVA-8, VSV-8, and SEV-9 complexes with H-2Kb indicates that four side chains (Lys-66, Glu-152, Arg-155, and Trp-167) adopt peptide-specific conformations. H-2Kb paralogs include H-2Db, H-2Kbml and H-2KbI1s. 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: 409610 Cd Length: 94 Bit Score: 39.32 E-value: 3.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2487 PKPPSIKIVRPSDsdlwgsnNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEWD 2566
Cdd:cd21019      5 PKAHVTHHSRPED-------KVTLRCWALGFYPADITLTWQLNGEEL--IQDMELVETRPAGDGTFQKWASVVVPLGKEQ 75

                           90
                   ....*....|....*....
gi 1696205678 2567 HnsnYSCAVRHESSERPIT 2585
Cdd:cd21019     76 Y---YTCHVYHQGLPEPLT 91

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: 39.03 E-value: 3.22e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1770 TAFPSSTPSLHLETPrfrtvmtqteVTANCVVHSAYDA--KVSWLLDGKDPTSRT-PVNQASSTTQSISSNLTLPSSQWK 1846
Cdd:cd21818      3 TVFPLSLCPSLSSDP----------VVIGCLVQGFFPEpvNVTWNYSGKGGTARNfPAMLASGGRYTQSSQLTLPADQCP 72

                           90       100
                   ....*....|....*....|....
gi 1696205678 1847 TLNTITCRAEHrcFNPTQrTSNVN 1870
Cdd:cd21818     73 EGEAYKCSVQH--YSPSQ-DLNVP 93

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: 39.03 E-value: 3.22e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2073 TAFPSSTPSLHLETPrfrtvmtqteVTANCVVHSAYDA--KVSWLLDGKDPTSRT-PVNQASSTTQSISSNLTLPSSQWK 2149
Cdd:cd21818      3 TVFPLSLCPSLSSDP----------VVIGCLVQGFFPEpvNVTWNYSGKGGTARNfPAMLASGGRYTQSSQLTLPADQCP 72

                           90       100
                   ....*....|....*....|....
gi 1696205678 2150 TLNTITCRAEHrcFNPTQrTSNVN 2173
Cdd:cd21818     73 EGEAYKCSVQH--YSPSQ-DLNVP 93

Class Ia major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) A; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the class Ia major histocompatibility complex (MHC) immunoglobulin domain of human leukocyte antigen (HLA) A. The classical class I molecules (HLA-A, -B, and -C) are responsible for the presentation of endogenous antigen to CD8+ T cells. The receptor is a heterodimer, and is composed of a heavy alpha chain and smaller beta chain. The alpha chain is encoded by a variant HLA-A gene, and the beta chain (beta-2-microglobulin) is an invariant beta-2-microglobulin molecule. The beta-2-microglobulin protein is coded for by a separate region of the human genome. HLA-A2 is associated with spontaneous abortions, HIV, and Hodgkin lymphoma. 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: 409618 Cd Length: 95 Bit Score: 39.05 E-value: 3.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2506 NNATLLCLVSGFFPSDVIVNWEKAGSRLpfSRYSSIPSVLYAGSSTYSMNSRLIVPRSEwdhNSNYSCAVRHESSERPIT 2585
Cdd:cd21027     18 HEATLRCWALSFYPAEITLTWQRDGEDQ--TQDTELVETRPAGDGTFQKWAAVVVPSGQ---EQRYTCHVQHEGLPKPLT 92

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: 39.05 E-value: 3.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678   48 APTLFPLAQCGSGTGDM--MTLGCIATGFTPASLTFKWnEQGGKSLTDFVqYPAVQTGGS-YTGVSQLRVKRADWDSKIF 124
Cdd:cd16092      1 APDVFPIISGCRHPKDNspVVLACLITGYHPTSVTVTW-YMGTQSQPQRT-FPEIQRRDSyYMTSSQLSTPLQQWRQGEY 78

                           90       100
                   ....*....|....*....|.
gi 1696205678  125 ECAVEHSAgSKTvpvKKQVQR 145
Cdd:cd16092     79 KCVVQHTA-SKS---KKEIFR 95

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: 39.03 E-value: 3.84e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  558 TAFPSSTPSLHLETPrfrtvmtqteVTATCVVHSAYDA--KVSWLLDGKDPTSRT-PVNQASSTTQSISSNLTLPSSQWK 634
Cdd:cd21818      3 TVFPLSLCPSLSSDP----------VVIGCLVQGFFPEpvNVTWNYSGKGGTARNfPAMLASGGRYTQSSQLTLPADQCP 72

                           90
                   ....*....|....*....
gi 1696205678  635 TLNTITCRAEHrcFNPTQT 653
Cdd:cd21818     73 EGEAYKCSVQH--YSPSQD 89

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: 39.03 E-value: 4.03e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696205678  294 VSWLLDGKDPTSRT-PVNQASSTTQSISSNLTLPSSQWKTLNTITCRAEHrcfNTTQRTSNVN 355
Cdd:cd21818     34 VTWNYSGKGGTARNfPAMLASGGRYTQSSQLTLPADQCPEGEAYKCSVQH---YSPSQDLNVP 93

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: 38.21 E-value: 6.71e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  363 PTVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 440
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678  441 CKVNQGYSNSWMSNS 455
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.21 E-value: 6.71e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  666 PTVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 743
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678  744 CKVNQGYSNSWMSNS 758
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.21 E-value: 6.71e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1575 PTVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 1652
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678 1653 CKVNQGYSNSWMSNS 1667
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.21 E-value: 6.71e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1878 PTVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 1955
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678 1956 CKVNQGYSNSWMSNS 1970
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.21 E-value: 6.71e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2181 PTVLIRRSLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 2258
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678 2259 CKVNQGYSNSWMSNS 2273
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.21 E-value: 7.26e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678  969 PTVLIRRTLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 1046
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678 1047 CKVNQGYSNSWMSNS 1061
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.21 E-value: 8.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 1272 PTVLIRRTLPDLLDGDSAVLECAITQLSSSDLYVTFQANGVDFPEK-QYVDLPASKDH-HSLTRRFSIPTSHWKKDNTFT 1349
Cdd:cd07699      2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGvTTSKTEQQSDNtYSMSSYLTLSSSDWNKHKVYT 81

                           90
                   ....*....|....*
gi 1696205678 1350 CKVNQGYSDSWMSNS 1364
Cdd:cd07699     82 CEVTHEGLSSTITKS 96

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: 38.20 E-value: 8.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696205678 2490 PSIKIVRPSDSDLWGSNNATLLCLVSGFFPSD-VIVNWEKAgSRLPFSRYSSIPSVLYagSSTYSMNSRLIVPRSEWDHN 2568
Cdd:cd07696      1 VSVFLIPPSPKDLFLTKSAKVTCLVVDLTSIEeVNVTWSRE-DGNEVLASTTNPEKHY--NATLSVVSTLTVCADDWDNG 77

                           90       100
                   ....*....|....*....|
gi 1696205678 2569 SNYSCAVRHESSERPITSTI 2588
Cdd:cd07696     78 KTFKCKVTHPDLPSPIVKSI 97