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Conserved domains on  [gi|589911017]
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Chain B, IG EPSILON CHAIN C REGION

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 11577487)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 12-110 3.26e-48

CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, and mu chains, and CH2 domain (second constant Ig domain of the gheavy chain) in immunoglobulin heavy gamma chain; member of the C1-set of Ig superfamily (IgSF) ; The members here are composed of the third immunoglobulin constant domain (IgC) of the gamma heavy chains and the second immunoglobulin constant domain (IgC) of alpha, epsilon, and mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


:

Pssm-ID: 409493  Cd Length: 98  Bit Score: 153.38  E-value: 3.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  12 VSAYLSRPSPFDLFIRKSPTITCLVVDLaPSKGTVQLTWSRASGKPVQHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGET 91
Cdd:cd07696    1 VSVFLIPPSPKDLFLTKSAKVTCLVVDL-TSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGKT 79

                         90
                 ....*....|....*....
gi 589911017  92 YQCRVTHPHLPRALMRSTT 110
Cdd:cd07696   80 FKCKVTHPDLPSPIVKSIQ 98
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 119-223 9.71e-42

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: 137.08  E-value: 9.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 119 PEVYAFATPEWPGSR-DKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd05768    1 PSVYLLPPPEEELSLnETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                         90       100
                 ....*....|....*....|....*.
gi 589911017 198 FICRAVHEaASPSQTVQRAVSVNPGK 223
Cdd:cd05768   81 FSCVVGHE-ALPLQFTQKSIDKSPGK 105
 
Name Accession Description Interval E-value
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 12-110 3.26e-48

CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, and mu chains, and CH2 domain (second constant Ig domain of the gheavy chain) in immunoglobulin heavy gamma chain; member of the C1-set of Ig superfamily (IgSF) ; The members here are composed of the third immunoglobulin constant domain (IgC) of the gamma heavy chains and the second immunoglobulin constant domain (IgC) of alpha, epsilon, and mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


Pssm-ID: 409493  Cd Length: 98  Bit Score: 153.38  E-value: 3.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  12 VSAYLSRPSPFDLFIRKSPTITCLVVDLaPSKGTVQLTWSRASGKPVQHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGET 91
Cdd:cd07696    1 VSVFLIPPSPKDLFLTKSAKVTCLVVDL-TSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGKT 79

                         90
                 ....*....|....*....
gi 589911017  92 YQCRVTHPHLPRALMRSTT 110
Cdd:cd07696   80 FKCKVTHPDLPSPIVKSIQ 98
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 119-223 9.71e-42

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: 137.08  E-value: 9.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 119 PEVYAFATPEWPGSR-DKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd05768    1 PSVYLLPPPEEELSLnETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                         90       100
                 ....*....|....*....|....*.
gi 589911017 198 FICRAVHEaASPSQTVQRAVSVNPGK 223
Cdd:cd05768   81 FSCVVGHE-ALPLQFTQKSIDKSPGK 105
C1-set pfam07654
Immunoglobulin C1-set domain;
121-206 3.58e-26

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 96.55  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  121 VYAFATPEWPGsRDKRTLACLIQNFMPEDISVQWLHNEVQLPDArHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFIC 200
Cdd:pfam07654   1 VYVFPPSPEEL-GKPNTLTCLVTGFYPPDITVTWLKNGQEVTEG-VKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTC 78


                  ....*.
gi 589911017  201 RAVHEA 206
Cdd:pfam07654  79 RVEHEG 84
IGc1 smart00407
Immunoglobulin C-Type;
135-206 2.31e-20

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 81.21  E-value: 2.31e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 589911017   135 KRTLACLIQNFMPEDISVQWLHNEVQLPDaRHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFICRAVHEA 206
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTE-GVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEG 71
C1-set pfam07654
Immunoglobulin C1-set domain;
15-101 3.29e-13

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 63.04  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017   15 YLSRPSPFDLfiRKSPTITCLVVDLAPskGTVQLTWSRaSGKPVQ--HSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETY 92
Cdd:pfam07654   2 YVFPPSPEEL--GKPNTLTCLVTGFYP--PDITVTWLK-NGQEVTegVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEY 76


                  ....*....
gi 589911017   93 QCRVTHPHL 101
Cdd:pfam07654  77 TCRVEHEGL 85
IGc1 smart00407
Immunoglobulin C-Type;
31-102 7.81e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 50.78  E-value: 7.81e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589911017    31 TITCLVVDLAPSKGTVqlTWSRaSGKPVQ--HSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLP 102
Cdd:smart00407   3 TLVCLVSGFYPPDITV--TWLR-NGQEVTegVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLK 73
 
Name Accession Description Interval E-value
IgC1_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, ...
 12-110 3.26e-48

CH3 domain (third constant Ig domain of heavy chains) in immunoglobulin heavy alpha, epsilon, and mu chains, and CH2 domain (second constant Ig domain of the gheavy chain) in immunoglobulin heavy gamma chain; member of the C1-set of Ig superfamily (IgSF) ; The members here are composed of the third immunoglobulin constant domain (IgC) of the gamma heavy chains and the second immunoglobulin constant domain (IgC) of alpha, epsilon, and mu heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


Pssm-ID: 409493  Cd Length: 98  Bit Score: 153.38  E-value: 3.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  12 VSAYLSRPSPFDLFIRKSPTITCLVVDLaPSKGTVQLTWSRASGKPVQHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGET 91
Cdd:cd07696    1 VSVFLIPPSPKDLFLTKSAKVTCLVVDL-TSIEEVNVTWSREDGNEVLASTTNPEKHYNATLSVVSTLTVCADDWDNGKT 79

                         90
                 ....*....|....*....
gi 589911017  92 YQCRVTHPHLPRALMRSTT 110
Cdd:cd07696   80 FKCKVTHPDLPSPIVKSIQ 98
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 119-223 9.71e-42

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: 137.08  E-value: 9.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 119 PEVYAFATPEWPGSR-DKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd05768    1 PSVYLLPPPEEELSLnETVTLTCLVKGFYPEDIFVSWLQNGEPLPSADYKTTAPVPESDGSFFVYSKLNVSTADWNSGDV 80

                         90       100
                 ....*....|....*....|....*.
gi 589911017 198 FICRAVHEaASPSQTVQRAVSVNPGK 223
Cdd:cd05768   81 FSCVVGHE-ALPLQFTQKSIDKSPGK 105
C1-set pfam07654
Immunoglobulin C1-set domain;
121-206 3.58e-26

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 96.55  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  121 VYAFATPEWPGsRDKRTLACLIQNFMPEDISVQWLHNEVQLPDArHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFIC 200
Cdd:pfam07654   1 VYVFPPSPEEL-GKPNTLTCLVTGFYPPDITVTWLKNGQEVTEG-VKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEYTC 78


                  ....*.
gi 589911017  201 RAVHEA 206
Cdd:pfam07654  79 RVEHEG 84
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 120-213 1.95e-21

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: 84.82  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 120 EVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARhSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFI 199
Cdd:cd00098    1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKDITVTWLKNGVPLTSGV-STSSPVEPNDGTYSVTSSLTVPPSDWDEGATYT 79

                         90
                 ....*....|....
gi 589911017 200 CRAVHEAASPSQTV 213
Cdd:cd00098   80 CVVTHESLKSPLSK 93
IGc1 smart00407
Immunoglobulin C-Type;
135-206 2.31e-20

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 81.21  E-value: 2.31e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 589911017   135 KRTLACLIQNFMPEDISVQWLHNEVQLPDaRHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFICRAVHEA 206
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTE-GVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEG 71
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 13-109 1.76e-18

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


Pssm-ID: 409354  Cd Length: 95  Bit Score: 77.11  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  13 SAYLSRPSPFDLFiRKSPTITCLVVDLAPSkgTVQLTWSRaSGKPVQH--STRKEEKQRNGTLTVTSTLPVGTRDWIEGE 90
Cdd:cd00098    1 TVTLLPPSPEEKG-GGKVTLVCLVSGFYPK--DITVTWLK-NGVPLTSgvSTSSPVEPNDGTYSVTSSLTVPPSDWDEGA 76

                         90
                 ....*....|....*....
gi 589911017  91 TYQCRVTHPHLPRALMRST 109
Cdd:cd00098   77 TYTCVVTHESLKSPLSKTW 95
C1-set pfam07654
Immunoglobulin C1-set domain;
15-101 3.29e-13

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 63.04  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017   15 YLSRPSPFDLfiRKSPTITCLVVDLAPskGTVQLTWSRaSGKPVQ--HSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETY 92
Cdd:pfam07654   2 YVFPPSPEEL--GKPNTLTCLVTGFYP--PDITVTWLK-NGQEVTegVKTTPPSPNSDWTYQLSSYLTVTPSDWESGDEY 76


                  ....*....
gi 589911017   93 QCRVTHPHL 101
Cdd:pfam07654  77 TCRVEHEGL 85
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 137-218 3.42e-11

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: 57.79  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 137 TLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFF-VFSRLEVTRAEWEQKDEFICRAVHEAAspsqTVQR 215
Cdd:cd16093   21 TFVCLATGFSPKTISFKWLRNGKEVTSSTGAVVEEPKEDGKTLYsATSFLTITESEWKSQTEFTCEFKHKGE----IVEK 96


                 ...
gi 589911017 216 AVS 218
Cdd:cd16093   97 NAS 99
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
 12-114 4.74e-11

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: 57.73  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  12 VSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVQltWSRaSGKPVQ---HSTRKEEKQRNGTLTVTSTLPVGTRDWIE 88
Cdd:cd05768    1 PSVYLLPPPEEELSLNETVTLTCLVKGFYPEDIFVS--WLQ-NGEPLPsadYKTTAPVPESDGSFFVYSKLNVSTADWNS 77

                         90       100
                 ....*....|....*....|....*..
gi 589911017  89 GETYQCRVTHPHLP-RALMRSTTKTSG 114
Cdd:cd05768   78 GDVFSCVVGHEALPlQFTQKSIDKSPG 104
IgC1_CH2_IgA cd04986
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; ...
 16-112 1.91e-10

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin heavy alpha chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin constant-1 set domain (IgC) of alpha heavy chains. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors.


Pssm-ID: 409375  Cd Length: 96  Bit Score: 55.85  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  16 LSRPSPFDLFIRKSPTITCLVVDLAPSKGTVqLTWSRASGK-PVQHSTrkeEKQRNGTLTVTSTLPVGTRDWIEGETYQC 94
Cdd:cd04986    6 LQRPALEDLLLGSNASLTCTLSGLKDPEGAT-FTWEPSGGKeAIQGPP---ERDSCGCYSVSSVLPGCAEPWNSGDTFSC 81

                         90
                 ....*....|....*...
gi 589911017  95 RVTHPHLPralmRSTTKT 112
Cdd:cd04986   82 TVTHPESK----GTLTAT 95
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 119-206 2.65e-09

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: 52.80  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 119 PEVYAF-ATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHsTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd05847    1 PTVQILhSSCASTLTSETIQLLCLISGYTPSTIEVEWLVDGQVATLSAA-STAPQKEEGGTFSTTSKLNVTQEDWKSGKT 79


                 ....*....
gi 589911017 198 FICRAVHEA 206
Cdd:cd05847   80 YTCKVTHQG 88
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 118-215 3.30e-09

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: 52.46  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 118 APEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARhSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd07699    1 APSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGV-TTSKTEQQSDNTYSMSSYLTLSSSDWNKHKV 79

                         90       100
                 ....*....|....*....|
gi 589911017 198 FICRAVHEAASP--SQTVQR 215
Cdd:cd07699   80 YTCEVTHEGLSStiTKSFNR 99
IGc1 smart00407
Immunoglobulin C-Type;
31-102 7.81e-09

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 50.78  E-value: 7.81e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589911017    31 TITCLVVDLAPSKGTVqlTWSRaSGKPVQ--HSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLP 102
Cdd:smart00407   3 TLVCLVSGFYPPDITV--TWLR-NGQEVTegVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLK 73
IgC1_L cd07699
Immunoglobulin light chain Constant domain; member of the C1-set of Ig superfamily (IgSF) ...
 18-108 7.89e-08

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


Pssm-ID: 409496  Cd Length: 99  Bit Score: 48.61  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  18 RPSPFDLFIRKSpTITCLVVDLAPSKGTVqlTWsRASGKPVQH--STRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCR 95
Cdd:cd07699    8 PPSSEELSSGKA-TLVCLINKFYPGFATV--TW-KVDGSTVSSgvTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYTCE 83

                         90
                 ....*....|...
gi 589911017  96 VTHPHLPRALMRS 108
Cdd:cd07699   84 VTHEGLSSTITKS 96
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 118-206 1.02e-07

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: 48.48  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 118 APEVYAFATPEwPGSRDKRTLACLIQNFMPEDISVQWlhNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd21819    1 APTLFPLVSCG-SSTSDPVTVGCLATDFLPDSITFSW--TDDNNSLTTGVKTYPSVLTGGTYTASSQLQVPESEWKSKEN 77


                 ....*....
gi 589911017 198 FICRAVHEA 206
Cdd:cd21819   78 FYCKVEHPG 86
IgC1_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); member of ...
 19-99 2.51e-07

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: 47.41  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  19 PSPFDLFIRKSPTITCLVVDLAPskGTVQLTW-SRASGKPVQHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVT 97
Cdd:cd05847    8 SSCASTLTSETIQLLCLISGYTP--STIEVEWlVDGQVATLSAASTAPQKEEGGTFSTTSKLNVTQEDWKSGKTYTCKVT 85


                 ..
gi 589911017  98 HP 99
Cdd:cd05847   86 HQ 87
IgC1_beta2m cd05770
Class I major histocompatibility complex (MHC) beta-2-microglobulin; member of the C1-set of ...
 119-213 3.68e-07

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


Pssm-ID: 409427  Cd Length: 94  Bit Score: 46.70  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 119 PEVYAFAtpEWPGSRDKR-TLACLIQNFMPEDISVQWLHNEVQLPDARHSttQPRKTKGSGFFVFSRLEVTRaewEQKDE 197
Cdd:cd05770    3 PKVQVYS--RFPAENGKPnVLNCYVSGFHPPDIEIRLLKNGVKIEDVEQS--DLSFSKDWTFYLLKYTEFTP---TKGDE 75

                         90
                 ....*....|....*.
gi 589911017 198 FICRAVHEAASPSQTV 213
Cdd:cd05770   76 YACRVRHNTLSEPKIY 91
IgC1_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; member of the C1-set of Ig ...
 135-222 1.09e-06

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: 46.22  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 135 KRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQ-KDEFICRAVHEAASPSQTV 213
Cdd:cd05769   20 KATLVCLATGFYPDHVSLSWKVNGKEVKDGVATDPQALRENTSTYSLSSRLRVSATEWFNpRNTFTCIVKFYGGTDTDTW 99


                 ....*....
gi 589911017 214 QRAVSVNPG 222
Cdd:cd05769  100 TQGIAGPVT 108
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 118-211 3.04e-06

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: 44.50  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 118 APEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDE 197
Cdd:cd04985    1 APTVFPLQSATKSQSNGPVALGCLISDYFPESITVSWQKNTNSITSGFTRTFPVVLRSGGDYSCSSQLTVPLQEWNSGEV 80

                         90
                 ....*....|....
gi 589911017 198 FICRAVHEAASPSQ 211
Cdd:cd04985   81 YKCQVQHSASNSKQ 94
IgC1_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; member of ...
 137-213 3.41e-06

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: 44.22  E-value: 3.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589911017 137 TLACLIQNFMPEDISVQWLHNEVQLPDA-RHSTTQPRktKGSGFFVFSRLEVTRaewEQKDEFICRAVHEAASPSQTV 213
Cdd:cd05767   20 TLICFVDNFFPPVINVTWLRNGQPVTDGvSETVFLPR--EDHSFRKFSYLPFTP---SEGDIYDCRVEHWGLEEPLLK 92
IgC1_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin mu chain; member ...
 19-99 4.23e-05

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


Pssm-ID: 409513  Cd Length: 99  Bit Score: 41.23  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  19 PSPFDLFIRKSPTITCLVVDLAPSkgTVQLTWSRaSGKPVQHSTR---KEEKQRNGTL-TVTSTLPVGTRDWIEGETYQC 94
Cdd:cd16093    9 PSREEFLGNRTATFVCLATGFSPK--TISFKWLR-NGKEVTSSTGavvEEPKEDGKTLySATSFLTITESEWKSQTEFTC 85


                 ....*
gi 589911017  95 RVTHP 99
Cdd:cd16093   86 EFKHK 90
IgC1_CD1 cd21029
Immunoglobulin domain of Cluster of Differentiation (CD) 1; member of the C1-set of Ig ...
 118-204 6.54e-05

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: 40.38  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 118 APEVYAFATPewPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHS---------TTQPRKTkgsgffvfsrLEVT 188
Cdd:cd21029    2 KPRVRLSSRP--SPGDGHLQLSCHVTGFYPRPIEVTWLRDGQEQMDGTQSggilpnhdgTYQLRKT----------LDIA 69

                         90
                 ....*....|....*.
gi 589911017 189 RAEweqKDEFICRAVH 204
Cdd:cd21029   70 PGE---GAGYSCRVDH 82
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 32-99 9.47e-05

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: 40.27  E-value: 9.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  32 ITCLVVDLAPSkgTVQLTWSRASGKPVQHSTRK--EEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHP 99
Cdd:cd04985   21 LGCLISDYFPE--SITVSWQKNTNSITSGFTRTfpVVLRSGGDYSCSSQLTVPLQEWNSGEVYKCQVQHS 88
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 17-102 1.10e-04

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: 39.87  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017   17 SRPSPFDLFIRKSPTITCLVVDLAPSkgtVQLTWSRASGkpvQHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGeTYQCRV 96
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPG---PDVTWSKEGG---TLIESLKVKHDNGRTTQSSLLISNVTKEDAG-TYTCVV 73


                  ....*.
gi 589911017   97 THPHLP 102
Cdd:pfam00047  74 NNPGGS 79
IgC1_CH2_IgD cd16084
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin delta chain; ...
 15-102 3.37e-04

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


Pssm-ID: 409506  Cd Length: 97  Bit Score: 38.57  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  15 YLSRPSPFDLFIRKSPTITCLVV--DLAPSkgtvQLTWSRASGKPVQHSTRKE-EKQRNGTLTVTSTLPVGTRDWIEGET 91
Cdd:cd16084    3 YLLTPAVQDLWLRDKATFTCFVVgsDLKDA----HLTWEVAGKVPTGGVEEGLlERHSNGSQSQHSRLTLPRSLWNAGTS 78

                         90
                 ....*....|.
gi 589911017  92 YQCRVTHPHLP 102
Cdd:cd16084   79 VTCTLNHPSLP 89
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 118-208 2.35e-03

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: 36.27  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017 118 APEVYafatPEWPGSRDKR----TLACLIQNFMPEDISVQWlhnevqLPDARHSTTQ--PRKTKGSGFFVFSRLEVTRAE 191
Cdd:cd21817    1 APSVF----PLAPCCKSTNgssvTLGCLVTGYFPEPVTVTW------NSGSLTSGVKtfPAVLQSSGLYTTSSQVTVPSS 70

                         90
                 ....*....|....*..
gi 589911017 192 WEQKDEFICRAVHEAAS 208
Cdd:cd21817   71 SWGSQTFTCNVEHKPSS 87
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 137-206 4.54e-03

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


Pssm-ID: 409428  Cd Length: 100  Bit Score: 35.55  E-value: 4.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589911017 137 TLACLIQNFMPEDISVQWLH-----NEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFICRAVHEA 206
Cdd:cd05771   18 TLSCHIAGYYPLDVDVEWLReepggSESQVSRDGVSLSSHRQSVDGTYSISSYLTLEPGTENRGATYTCRVTHVS 92
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 24-108 5.36e-03

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


Pssm-ID: 409428  Cd Length: 100  Bit Score: 35.16  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  24 LFIRKSPTITCLVVDLAPSKgtVQLTWSR----ASGKPV---QHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRV 96
Cdd:cd05771   11 VKPDLPQTLSCHIAGYYPLD--VDVEWLReepgGSESQVsrdGVSLSSHRQSVDGTYSISSYLTLEPGTENRGATYTCRV 88

                         90
                 ....*....|..
gi 589911017  97 THPHLPRALMRS 108
Cdd:cd05771   89 THVSLEEPLSVS 100
IgC1_SIRP_domain_2 cd05772
Signal-regulatory protein (SIRP) immunoglobulin-like domain 2; member of the C1-set of Ig ...
 140-206 5.62e-03

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: 35.38  E-value: 5.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589911017 140 CLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTkgSGFFVFSRLEVTRAEWEQKDEFICRAVHEA 206
Cdd:cd05772   24 CKSHGFSPRDITLKWFKNGNELSALQTTVFPEGDS--VSYSVSSTVQVVLTKDDVHSQLTCEVAHVT 88
IgC1_CH1_IgM cd21819
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy mu chain; ...
 31-99 5.72e-03

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: 35.00  E-value: 5.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589911017  31 TITCLVVDLAPSkgTVQLTWSRaSGKPVQHSTRKEEK-QRNGTLTVTSTLPVGTRDWIEGETYQCRVTHP 99
Cdd:cd21819   19 TVGCLATDFLPD--SITFSWTD-DNNSLTTGVKTYPSvLTGGTYTASSQLQVPESEWKSKENFYCKVEHP 85
IgC1_MHC_II_alpha_HLA-DM cd21009
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of ...
 137-205 7.49e-03

Class II major histocompatibility complex (MHC) alpha 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 immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II alpha chain of histocompatibility antigen (HLA) DM. Human HLA-DM, also known as H2-M in mice, plays a critical role in antigen presentation to CD4 T cells by catalyzing the exchange of peptides bound to MHC class II molecules. 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: 409600  Cd Length: 94  Bit Score: 34.63  E-value: 7.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589911017 137 TLACLIQNFMPEDISVQWLHNEVqlPDARHSTTQPRKTKGSGFFVFSRLEVTRaewEQKDEFICRAVHE 205
Cdd:cd21009   20 TLVCFVSNLFPPMLTVNWQLHSV--PVEGFGPTFVSAVDGLSFQAFSYLNFTP---EPSDIFSCIVTHE 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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