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Conserved domains on  [gi|1209667|gb|AAA91163|]
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IgG heavy chain, partial [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

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
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 22-154 5.02e-45

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. 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 by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd04981:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 118  Bit Score: 144.37  E-value: 5.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   22 QLQESGPGLVKPPGTLSLTCAISGGSISSSNWWSwVRQPPGKGLEWIGELShtastrdklYQSGNTNYNPSLRSRVTISV 101
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGW-VRQAPGKGLEWIGLIY---------PGGGDTYYADSFKGRFTITR 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 1209667  102 DKSRNQFSLRLSSVTAADTAVYYCARGqrsyiWGSYRDPYFDYWGLGTLVTVS 154
Cdd:cd04981  71 DTSKSTAYLQLNSLTSEDTAVYYCARG-----LGGYGYSYFDYWGQGTTVTVS 118
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 160-181 1.41e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. 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 by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd21817:

Pssm-ID: 472250  Cd Length: 94  Bit Score: 36.27  E-value: 1.41e-03
                        10        20
                ....*....|....*....|..
gi 1209667  160 GPSVFPLAPCSRSTSGGTAALG 181
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLG 22
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 22-154 5.02e-45

Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains.


Pssm-ID: 409370 [Multi-domain]  Cd Length: 118  Bit Score: 144.37  E-value: 5.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   22 QLQESGPGLVKPPGTLSLTCAISGGSISSSNWWSwVRQPPGKGLEWIGELShtastrdklYQSGNTNYNPSLRSRVTISV 101
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGW-VRQAPGKGLEWIGLIY---------PGGGDTYYADSFKGRFTITR 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 1209667  102 DKSRNQFSLRLSSVTAADTAVYYCARGqrsyiWGSYRDPYFDYWGLGTLVTVS 154
Cdd:cd04981  71 DTSKSTAYLQLNSLTSEDTAVYYCARG-----LGGYGYSYFDYWGQGTTVTVS 118
IGv smart00406
Immunoglobulin V-Type;
57-127 8.03e-20

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 78.96  E-value: 8.03e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209667      57 VRQPPGKGLEWIGELShtastrdklyQSGNTNYNPSLRSRVTISVDKSRNQFSLRLSSVTAADTAVYYCAR 127
Cdd:smart00406  21 VRQPPGKGLEWLGYIG----------SNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 24-153 1.43e-07

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 47.84  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667     24 QESGPGLVKPPGTLSLTCAISGGSISSSNWWSWVRQPPGKGLEWigelshtastrdKLYQSGNTNYNPSLRSRVTISVDK 103
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTF------------LIAYYSNGSEEGVKKGRFSGRGDP 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209667    104 SRNQFSLRLSSVTAADTAVYYCARGQRSYiwgsyrdpyfDYWGLGTLVTV 153
Cdd:pfam07686  69 SNGDGSLTIQNLTLSDSGTYTCAVIPSGE----------GVFGKGTRLTV 108
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 160-181 1.41e-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: 1.41e-03
                        10        20
                ....*....|....*....|..
gi 1209667  160 GPSVFPLAPCSRSTSGGTAALG 181
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLG 22
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 22-154 5.02e-45

Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains.


Pssm-ID: 409370 [Multi-domain]  Cd Length: 118  Bit Score: 144.37  E-value: 5.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   22 QLQESGPGLVKPPGTLSLTCAISGGSISSSNWWSwVRQPPGKGLEWIGELShtastrdklYQSGNTNYNPSLRSRVTISV 101
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGW-VRQAPGKGLEWIGLIY---------PGGGDTYYADSFKGRFTITR 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 1209667  102 DKSRNQFSLRLSSVTAADTAVYYCARGqrsyiWGSYRDPYFDYWGLGTLVTVS 154
Cdd:cd04981  71 DTSKSTAYLQLNSLTSEDTAVYYCARG-----LGGYGYSYFDYWGQGTTVTVS 118
IGv smart00406
Immunoglobulin V-Type;
57-127 8.03e-20

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 78.96  E-value: 8.03e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209667      57 VRQPPGKGLEWIGELShtastrdklyQSGNTNYNPSLRSRVTISVDKSRNQFSLRLSSVTAADTAVYYCAR 127
Cdd:smart00406  21 VRQPPGKGLEWLGYIG----------SNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 58-153 2.40e-11

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


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 57.73  E-value: 2.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   58 RQPPGKGLEWIGELShtastrdklyqSGNTNYNPSLRSRVTISVDKSrNQFSLRLSSVTAADTAVYYCArgqrSYIWGSY 137
Cdd:cd00099  35 RQKPGQGPEFLIYLS-----------SSKGKTKGGVPGRFSGSRDGT-SSFSLTISNLQPEDSGTYYCA----VSESGGT 98

                        90
                ....*....|....*.
gi 1209667  138 RDPYFdywGLGTLVTV 153
Cdd:cd00099  99 DKLTF---GSGTRLTV 111
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 58-153 1.12e-07

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


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 48.04  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   58 RQPPGKGLEWIgelshtastrdkLYQSGNTNYNPSlrSRVTISVDKSRNQFSLRLSSVTAADTAVYYCARGqrsyIWGSY 137
Cdd:cd04983  34 RQYPGQGPQFL------------IYISSDSGNKKK--GRFSATLDKSRKSSSLHISAAQLSDSAVYFCALS----ESGGT 95

                        90
                ....*....|....*.
gi 1209667  138 RDPYFdywGLGTLVTV 153
Cdd:cd04983  96 GKLTF---GKGTRLTV 108
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 24-153 1.43e-07

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 47.84  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667     24 QESGPGLVKPPGTLSLTCAISGGSISSSNWWSWVRQPPGKGLEWigelshtastrdKLYQSGNTNYNPSLRSRVTISVDK 103
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTF------------LIAYYSNGSEEGVKKGRFSGRGDP 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209667    104 SRNQFSLRLSSVTAADTAVYYCARGQRSYiwgsyrdpyfDYWGLGTLVTV 153
Cdd:pfam07686  69 SNGDGSLTIQNLTLSDSGTYTCAVIPSGE----------GVFGKGTRLTV 108
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 58-154 7.42e-06

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


Pssm-ID: 409371  Cd Length: 117  Bit Score: 43.12  E-value: 7.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   58 RQPPGKGLEWIGELSHTASTRDklyQSGNTnynpslRSRVTISVDKSRNQFSLRLSSVTAADTAVYYCArgqrsyIWGSY 137
Cdd:cd04982  36 RQKPGQALERLLYVSSTSAVRK---DSGKT------KNKFEARKDVGKSTSTLTITNLEKEDSATYYCA------YWESG 100

                        90
                ....*....|....*..
gi 1209667  138 RDPYFDYWGLGTLVTVS 154
Cdd:cd04982 101 SGYYIKVFGSGTKLIVT 117
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 58-153 1.88e-05

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


Pssm-ID: 409480  Cd Length: 110  Bit Score: 41.88  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   58 RQPPGKGLEWIGElshtastrdklYQSGNTNYNPSL-RSRVTIS-VDKSRnqFSLRLSSVTAADTAVYYCARGQRsyiwG 135
Cdd:cd05899  33 RQDPGKGLQLLFY-----------SYGGGLNEEGDLpGDRFSASrPSLTR--SSLTIKSAEPEDSAVYLCASSLG----G 95

                        90
                ....*....|....*...
gi 1209667  136 SYRDPYFdywGLGTLVTV 153
Cdd:cd05899  96 GADEAYF---GPGTRLTV 110
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 99-153 3.34e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.57  E-value: 3.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1209667      99 ISVDKSRNQFSLRLSSVTAADTAVYYCARgqrsyiwgsyRDPYFDYWGlGTLVTV 153
Cdd:smart00410  42 FSVSRSGSTSTLTISNVTPEDSGTYTCAA----------TNSSGSASS-GTTLTV 85
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 20-127 1.20e-03

T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain of the T-cell receptor Mu. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409514  Cd Length: 115  Bit Score: 37.16  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209667   20 QVQLQESGPGLVKPPGTLSLTCAISGGSISSSNWWSWVRQPPGKGLeWIGELSHTASTRDKlyqsgntnynpslrSRVTI 99
Cdd:cd16095   1 ETQLEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPL-WLTSLDHISTKVSE--------------DRITS 65

                        90       100
                ....*....|....*....|....*...
gi 1209667  100 SVDKSRNQFSLRLSSVTAADTAVYYCAR 127
Cdd:cd16095  66 SREDTNSQIFLQIKGLGLRDSGQYHCAR 93
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 160-181 1.41e-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: 1.41e-03
                        10        20
                ....*....|....*....|..
gi 1209667  160 GPSVFPLAPCSRSTSGGTAALG 181
Cdd:cd21817   1 APSVFPLAPCCKSTNGSSVTLG 22
IgV_SIRP cd16097
Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The ...
 96-153 2.63e-03

Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). 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 that contain either ITIMs or transmembrane regions 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 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409516  Cd Length: 111  Bit Score: 35.99  E-value: 2.63e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209667   96 RVTISVDKS-RNQ--FSLRLSSVTAADTAVYYCARGQRsyiwGSYRDPYFDYwGLGTLVTV 153
Cdd:cd16097  55 RVTTVSDLTkRNNmdFSIRISNITPADAGTYYCVKFRK----GSPDDVEFKS-GAGTELSV 110
IgC1_CH1_IgADEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, delta, ...
 160-181 3.73e-03

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: 35.26  E-value: 3.73e-03
                        10        20
                ....*....|....*....|..
gi 1209667  160 GPSVFPLAPCSRSTSGGTAALG 181
Cdd:cd04985   1 APTVFPLQSATKSQSNGPVALG 22
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 76-153 6.96e-03

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


Pssm-ID: 409580  Cd Length: 114  Bit Score: 34.84  E-value: 6.96e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209667   76 STRDKLYQSGNTnYNPSLRSRVTISVDKSRNQFSLRLSSVTAADTAVYYCArgQRSYIWGSYRDPYFdyWGLGTLVTV 153
Cdd:cd20988  41 NTMTFIYREGGI-YGPGFKDNFRGDIDSSNNLAVLKILEASERDEGSYYCA--SDTPGGGREYDPLI--FGKGTYLTV 113
 
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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