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Conserved domains on  [gi|298358585|ref|NP_001177254|]
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immunoglobulin lambda-like polypeptide 1 precursor [Mus musculus]

Protein Classification

IgC_L domain-containing protein (domain architecture ID 10166774)

IgC_L domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IgC_L cd07699
Immunoglobulin Constant domain; IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. ...
110-207 1.69e-38

Immunoglobulin Constant domain; IgC_L: 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: 319325  Cd Length: 99  Bit Score: 131.04  E-value: 1.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFLPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYS 189
Cdd:cd07699    2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYT 81
                         90
                 ....*....|....*...
gi 298358585 190 CRVTHEGNTVEKSVSPAE 207
Cdd:cd07699   82 CEVTHEGLSSTITKSFNR 99
 
Name Accession Description Interval E-value
IgC_L cd07699
Immunoglobulin Constant domain; IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. ...
110-207 1.69e-38

Immunoglobulin Constant domain; IgC_L: 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: 319325  Cd Length: 99  Bit Score: 131.04  E-value: 1.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFLPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYS 189
Cdd:cd07699    2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYT 81
                         90
                 ....*....|....*...
gi 298358585 190 CRVTHEGNTVEKSVSPAE 207
Cdd:cd07699   82 CEVTHEGLSSTITKSFNR 99
C1-set pfam07654
Immunoglobulin C1-set domain;
110-197 1.38e-32

Immunoglobulin C1-set domain;


Pssm-ID: 311543  Cd Length: 89  Bit Score: 115.45  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585  110 PLVTLFLPSLKNLQAN-KATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRY 188
Cdd:pfam07654   1 PSVYVFPPSKEPLELGkPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVTSTTLPQNGDWTYQLSSYLTVTPSDWESGDEY 80

                  ....*....
gi 298358585  189 SCRVTHEGN 197
Cdd:pfam07654  81 TCRVEHEGL 89
IGc1 smart00407
Immunoglobulin C-Type;
126-200 2.38e-30

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 109.33  E-value: 2.38e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298358585   126 KATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYSCRVTHEGNTVE 200
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75
 
Name Accession Description Interval E-value
IgC_L cd07699
Immunoglobulin Constant domain; IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. ...
110-207 1.69e-38

Immunoglobulin Constant domain; IgC_L: 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: 319325  Cd Length: 99  Bit Score: 131.04  E-value: 1.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFLPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYS 189
Cdd:cd07699    2 PSVTIFPPSSEELSSGKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYSMSSYLTLSSSDWNKHKVYT 81
                         90
                 ....*....|....*...
gi 298358585 190 CRVTHEGNTVEKSVSPAE 207
Cdd:cd07699   82 CEVTHEGLSSTITKSFNR 99
C1-set pfam07654
Immunoglobulin C1-set domain;
110-197 1.38e-32

Immunoglobulin C1-set domain;


Pssm-ID: 311543  Cd Length: 89  Bit Score: 115.45  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585  110 PLVTLFLPSLKNLQAN-KATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRY 188
Cdd:pfam07654   1 PSVYVFPPSKEPLELGkPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVTSTTLPQNGDWTYQLSSYLTVTPSDWESGDEY 80

                  ....*....
gi 298358585  189 SCRVTHEGN 197
Cdd:pfam07654  81 TCRVEHEGL 89
IGc1 smart00407
Immunoglobulin C-Type;
126-200 2.38e-30

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 109.33  E-value: 2.38e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298358585   126 KATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYSCRVTHEGNTVE 200
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCQVTHEGLKEP 75
IgC cd00098
Immunoglobulin Constant (IgC) domain; Members of the IgC family are components of ...
112-204 6.37e-25

Immunoglobulin Constant (IgC) domain; Members of the IgC family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 319274  Cd Length: 95  Bit Score: 95.59  E-value: 6.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 112 VTLFLPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYSCR 191
Cdd:cd00098    1 VTLLPPSPEEKLGGTVTLVCLVSGFYPKDITVTWLKNGKEVTSGVSTTPPTKNSDGTFSVTSYLTVPPSDWDEGTTYTCE 80
                         90
                 ....*....|...
gi 298358585 192 VTHEGNTVEKSVS 204
Cdd:cd00098   81 VSHESLSQPVSKS 93
IgC_CH3_IgAGD_CH4_IgAEM cd05768
CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin; ...
110-204 1.24e-17

CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH3_IgAGD_CH4_IgAEM: Contains 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 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) and three (in alpha, delta and gamma) or four (in 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: 319312  Cd Length: 100  Bit Score: 75.81  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFLPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVT-QGVETTQPSKQTNNK-YMVSSYLTLISDQWMPHSR 187
Cdd:cd05768    1 PSVYLLPPPEEELSLNTVTLTCLVKGFSPEDIFVRWLQNGQPLPeEDYKTTTPVKEESDGsFFVYSKLTVTASDWKSGDV 80
                         90       100
                 ....*....|....*....|
gi 298358585 188 YSCRVTHEG---NTVEKSVS 204
Cdd:cd05768   81 FSCVVGHEAlplQFTQKTID 100
IgC_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; IgC_TCR_beta: Constant domain ...
110-203 1.82e-17

T cell receptor (TCR) beta chain constant immunoglobulin domain; IgC_TCR_beta: Constant 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 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: 143246  Cd Length: 115  Bit Score: 75.87  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFLPSLKNL-QANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNK-YMVSSYLTLISDQWM-PHS 186
Cdd:cd05769    3 PTVAIFPPSEAEIrNKRKATLVCLATGFYPDHVSLSWKVNGKEVTDGVATDPQALRENTStYSISSRLRVSATEWFnPRN 82
                         90
                 ....*....|....*..
gi 298358585 187 RYSCRVTHEGNTVEKSV 203
Cdd:cd05769   83 TFTCIVQFYGGTDTDKW 99
IgC_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); ...
112-203 2.15e-16

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); IgC_CH2_IgE: 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 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) and three (in alpha, delta, and gamma) or four (in 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: 143255  Cd Length: 94  Bit Score: 72.44  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 112 VTLFLPSLK-NLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYSC 190
Cdd:cd05847    1 VQILHSSCCdTGTSETIQLLCLISGYTPGTIEVEWLVDGQVATLVAASTAPQKEEGSTFSTTSELNVTQEDWKSGKTYTC 80
                         90
                 ....*....|...
gi 298358585 191 RVTHEGNTVEKSV 203
Cdd:cd05847   81 KVTHQGTTFEDHT 93
IgC_TCR_gamma cd07697
T cell receptor (TCR) gamma chain constant immunoglobulin domain; IgC_TCR_gamma; ...
110-197 8.73e-14

T cell receptor (TCR) gamma chain constant immunoglobulin domain; IgC_TCR_gamma; immunoglobulin (Ig) constant (C) domain of the gamma chain of gamma-delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha-beta TCRs but a small subset contain gamma-delta TCRs. Alpha-beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma-delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma-delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds.


Pssm-ID: 319324  Cd Length: 97  Bit Score: 64.93  E-value: 8.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFLPSLKNLQ-ANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQwmPHSRY 188
Cdd:cd07697    1 PKPTIFPPSTAELEkQSKGFYLCLLEDFFPDVIEVHWKEDGKEQKELGSQDSVTKKGNNTYSLISWLTVTKLS--LGKPI 78

                 ....*....
gi 298358585 189 SCRVTHEGN 197
Cdd:cd07697   79 RCHYKHEID 87
IgC_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
110-196 1.57e-13

Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; IgC_MHC_II_alpha: Immunoglobulin (Ig) domain of 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. In both humans and in mice these molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), for example on B-lymphocytes, monocytes, and macrophages. 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 protelytic 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: 143244  Cd Length: 94  Bit Score: 64.28  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 110 PLVTLFlpSLKNLQANKA-TLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDqwmPHSRY 188
Cdd:cd05767    2 PEVTVF--SLKPVELGEPnTLICFVDNFFPPVLNVTWLKNGVPVTDGVSETRYYPRQDLSFQKFSYLNFTPE---EGDIY 76

                 ....*...
gi 298358585 189 SCRVTHEG 196
Cdd:cd05767   77 SCIVEHWG 84
IgC_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH2: The ...
112-204 1.28e-11

CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH2: 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 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) and three (in alpha, delta and gamma) or four (in 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: 319342  Cd Length: 100  Bit Score: 58.87  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 112 VTLFLPSLKNLQAN---KATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETT----QPSKQTNNKYMVSSYLTLISDQWMP 184
Cdd:cd16093    1 VSVFVPPRDGFSGNprrTSKLICQATGFSPRQISVSWLREGKQVGSGVTTDaveaEAKESGPTTFRVTSTLTITESEWLS 80
                         90       100
                 ....*....|....*....|
gi 298358585 185 HSRYSCRVTHEGNTVEKSVS 204
Cdd:cd16093   81 QSMFTCRVDHRGLTFQKNVS 100
IgC_CH1_IgAEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH2: The first ...
113-199 1.27e-08

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH2: The first immunoglobulin constant domain of alpha, epsilon, gamma, and mu heavy chains. This domain is found on the Fab antigen-binding fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each 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) and three (in alpha, delta and gamma) or four (in 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: 319288  Cd Length: 96  Bit Score: 50.75  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 113 TLF--LPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTqGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYSC 190
Cdd:cd04985    3 SVFplVPCCSSSSSDSVTLGCLATGFFPEPVTFTWNSGSNSTS-GVKTFPAVLQSGGLYTASSQLTVPASEWKSKKSFYC 81

                 ....*....
gi 298358585 191 RVTHEGNTV 199
Cdd:cd04985   82 KVEHPPTTS 90
IgC_CH3_IgAEM_CH2_IgG cd07696
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin; ...
112-195 1.52e-08

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH3_IgAEM_CH2_IgG: Contains the third and second immunoglobulin constant domain (IgC) of alpha, epsilon, and mu heavy chains and of gamma 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 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) and three (in alpha, delta and gamma) or four (in 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: 319323  Cd Length: 95  Bit Score: 50.50  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 112 VTLFLPSLKNLQANK-ATLVCLVSEF-YPGTLVVDWKVDGVPVtqgVETTQPS-KQTNNKYMVSSYLTLISDQWMPHSRY 188
Cdd:cd07696    1 VFLLPPSPKDLLLTKsVKLTCLVTDLtSPEGVNVTWTRGDGKE---VSHAKTKaREPNATLSVTSTLNVSTQDWISGKEF 77

                 ....*..
gi 298358585 189 SCRVTHE 195
Cdd:cd07696   78 QCKVTHP 84
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
108-196 6.47e-08

Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; IgC_MHC_I_alpha3; 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 beta2 microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells.


Pssm-ID: 143322  Cd Length: 93  Bit Score: 48.82  E-value: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585 108 SDPLVTLFLpslKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWmphSR 187
Cdd:cd07698    1 VPPEVRVTR---KRAPDGSLTLSCHATGFYPRDIEVTWLRDGEDSVDDVESGEILPNGDGTYQLWVTLEVPPEDK---AR 74

                 ....*....
gi 298358585 188 YSCRVTHEG 196
Cdd:cd07698   75 YSCRVEHSG 83
IgC_beta2m cd05770
Class I major histocompatibility complex (MHC) beta2-microglobulin; IgC_beta2m: ...
128-204 4.06e-06

Class I major histocompatibility complex (MHC) beta2-microglobulin; IgC_beta2m: Immunoglobulin-like domain in beta2-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 then excreted.


Pssm-ID: 143247  Cd Length: 93  Bit Score: 44.01  E-value: 4.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298358585 128 TLVCLVSEFYPGTLVVDWKVDGVPVTqGVETTQPSKQTNNKYMVSSYLTLISDQwmpHSRYSCRVTHEGNTVEKSVS 204
Cdd:cd05770   19 VLNCYVTGFHPPDIEIRLLKNGVKIP-KVEQSDLSFSKDWTFYLLKSTEFTPTK---GDEYACRVRHNSMSEPKKYK 91
IgC_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; IgC_Tapasin_R: Immunoglobulin-like domain on Tapasin-R. ...
98-194 1.20e-05

Tapasin-R immunoglobulin-like domain; IgC_Tapasin_R: 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: 319313  Cd Length: 138  Bit Score: 43.28  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298358585  98 TQLTILGQPKsdplVTLFLPSLKnLQANKATLVCLVSEFYPGTLVVDWKVdgVPVTQGVETTQPS--------KQTNNKY 169
Cdd:cd05771   31 IQLSVSEPPR----VRLSLEKTV-SIEEPQTLICHIAGYYPLDVQVEWTR--EPPGDSPPRVSVSnvsfsshrQHADGTY 103
                         90       100
                 ....*....|....*....|....*
gi 298358585 170 MVSSYLTLISDQWMPHSRYSCRVTH 194
Cdd:cd05771  104 SLSSALTLEPGTPHPGATYTCRVTH 128
IgC_CH1_IgD cd16092
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH1: The first ...
129-203 8.44e-03

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH1: The first immunoglobulin constant domain (IgC), of immunoglobulin (Ig) delta 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 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) and three (in alpha, delta and gamma) or four (in 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: 319341  Cd Length: 96  Bit Score: 34.43  E-value: 8.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298358585 129 LVCLVSEFYPGTLVVDWKVDgvPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMpHSRYSCRVTHEGNTVEKSV 203
Cdd:cd16092   22 LACLITGYHPTSVTVTWYMG--TQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWR-QGEYKCVVQHTASKSKKEI 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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