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Conserved domains on  [gi|332823708|ref|XP_003339166.1|]
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PREDICTED: HLA class II histocompatibility antigen, DQ beta 1 chain isoform X2 [Pan troglodytes]

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List of domain hits

Name Accession Description Interval E-value
IgC_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; ...
129-222 5.05e-54

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; IgC_MHC_II_beta: Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II beta chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. 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: 143243  Cd Length: 94  Bit Score: 171.82  E-value: 5.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 129 PTVTISPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVE 208
Cdd:cd05766    1 PSVKISPSQTGSLSHPHLLVCHVWGFYPPEITVKWFKNGQEETEGVVSTELIPNGDWTYQILVMLETTPSRGDTYTCVVE 80
                         90
                 ....*....|....
gi 332823708 209 HPSLQNPITVEWRA 222
Cdd:cd05766   81 HSSLQEPLTVDWRP 94
MHC_II_beta pfam00969
Class II histocompatibility antigen, beta domain;
45-118 2.72e-49

Class II histocompatibility antigen, beta domain;


:

Pssm-ID: 250263  Cd Length: 75  Bit Score: 158.84  E-value: 2.72e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332823708   45 GMCYFTNGTERVRLVTRYIYNREEYVRFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRHNYQLE 118
Cdd:pfam00969   1 SECYFTNGTERVRFLDRYIYNREEYVRFDSDVGEFVAVTELGRPDAEYWNSQKDLLEQRRAEVDTYCRHNYGVW 74
 
Name Accession Description Interval E-value
IgC_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; ...
129-222 5.05e-54

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; IgC_MHC_II_beta: Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II beta chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. 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: 143243  Cd Length: 94  Bit Score: 171.82  E-value: 5.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 129 PTVTISPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVE 208
Cdd:cd05766    1 PSVKISPSQTGSLSHPHLLVCHVWGFYPPEITVKWFKNGQEETEGVVSTELIPNGDWTYQILVMLETTPSRGDTYTCVVE 80
                         90
                 ....*....|....
gi 332823708 209 HPSLQNPITVEWRA 222
Cdd:cd05766   81 HSSLQEPLTVDWRP 94
MHC_II_beta pfam00969
Class II histocompatibility antigen, beta domain;
45-118 2.72e-49

Class II histocompatibility antigen, beta domain;


Pssm-ID: 250263  Cd Length: 75  Bit Score: 158.84  E-value: 2.72e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332823708   45 GMCYFTNGTERVRLVTRYIYNREEYVRFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRHNYQLE 118
Cdd:pfam00969   1 SECYFTNGTERVRFLDRYIYNREEYVRFDSDVGEFVAVTELGRPDAEYWNSQKDLLEQRRAEVDTYCRHNYGVW 74
MHC_II_beta smart00921
Class II histocompatibility antigen, beta domain; Class II MHC glycoproteins are expressed on ...
45-116 4.32e-42

Class II histocompatibility antigen, beta domain; Class II MHC glycoproteins are expressed on the surface of antigen-presenting cells (APC), including macrophages, dendritic cells and B cells. MHC II proteins present peptide antigens that originate extracellularly from foreign bodies such as bacteria. Proteins from the pathogen are degraded into peptide fragments within the APC, which sequesters these fragments into the endosome so they can bind to MHC class II proteins, before being transported to the cell surface. MHC class II receptors display antigens for recognition by helper T cells (stimulate development of B cell clones) and inflammatory T cells (cause the release of lymphokines that attract other cells to site of infection).


Pssm-ID: 197989  Cd Length: 72  Bit Score: 140.43  E-value: 4.32e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332823708    45 GMCYFTNGTERVRLVTRYIYNREEYVRFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRHNYQ 116
Cdd:smart00921   1 SECYFSNGTEDVRYVVRYIYNKEELVRFDSDVGKFVAFTELGRPAAEYWNSQKDLLERLRAEVDTVCRHNYQ 72
C1-set pfam07654
Immunoglobulin C1-set domain;
135-217 3.42e-40

Immunoglobulin C1-set domain;


Pssm-ID: 254335  Cd Length: 83  Bit Score: 135.84  E-value: 3.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708  135 PSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVEHPSLQN 214
Cdd:pfam07654   1 PPSPEELGKPNTLVCLVTGFYPPDITVTWLKNGQEVTEGVESTEELPNGDGTYQLSSYLTFTPESGDEYTCRVEHESLPE 80

                  ...
gi 332823708  215 PIT 217
Cdd:pfam07654  81 PIT 83
IGc1 smart00407
Immunoglobulin C-Type;
144-215 2.46e-25

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 96.23  E-value: 2.46e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332823708   144 HNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEM---TPQHGDVYTCHVEHPSLQNP 215
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVpasTWESGDVYTCQVTHEGLKEP 75
 
Name Accession Description Interval E-value
IgC_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; ...
129-222 5.05e-54

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; IgC_MHC_II_beta: Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II beta chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. 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: 143243  Cd Length: 94  Bit Score: 171.82  E-value: 5.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 129 PTVTISPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVE 208
Cdd:cd05766    1 PSVKISPSQTGSLSHPHLLVCHVWGFYPPEITVKWFKNGQEETEGVVSTELIPNGDWTYQILVMLETTPSRGDTYTCVVE 80
                         90
                 ....*....|....
gi 332823708 209 HPSLQNPITVEWRA 222
Cdd:cd05766   81 HSSLQEPLTVDWRP 94
MHC_II_beta pfam00969
Class II histocompatibility antigen, beta domain;
45-118 2.72e-49

Class II histocompatibility antigen, beta domain;


Pssm-ID: 250263  Cd Length: 75  Bit Score: 158.84  E-value: 2.72e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332823708   45 GMCYFTNGTERVRLVTRYIYNREEYVRFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRHNYQLE 118
Cdd:pfam00969   1 SECYFTNGTERVRFLDRYIYNREEYVRFDSDVGEFVAVTELGRPDAEYWNSQKDLLEQRRAEVDTYCRHNYGVW 74
MHC_II_beta smart00921
Class II histocompatibility antigen, beta domain; Class II MHC glycoproteins are expressed on ...
45-116 4.32e-42

Class II histocompatibility antigen, beta domain; Class II MHC glycoproteins are expressed on the surface of antigen-presenting cells (APC), including macrophages, dendritic cells and B cells. MHC II proteins present peptide antigens that originate extracellularly from foreign bodies such as bacteria. Proteins from the pathogen are degraded into peptide fragments within the APC, which sequesters these fragments into the endosome so they can bind to MHC class II proteins, before being transported to the cell surface. MHC class II receptors display antigens for recognition by helper T cells (stimulate development of B cell clones) and inflammatory T cells (cause the release of lymphokines that attract other cells to site of infection).


Pssm-ID: 197989  Cd Length: 72  Bit Score: 140.43  E-value: 4.32e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332823708    45 GMCYFTNGTERVRLVTRYIYNREEYVRFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRHNYQ 116
Cdd:smart00921   1 SECYFSNGTEDVRYVVRYIYNKEELVRFDSDVGKFVAFTELGRPAAEYWNSQKDLLERLRAEVDTVCRHNYQ 72
C1-set pfam07654
Immunoglobulin C1-set domain;
135-217 3.42e-40

Immunoglobulin C1-set domain;


Pssm-ID: 254335  Cd Length: 83  Bit Score: 135.84  E-value: 3.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708  135 PSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVEHPSLQN 214
Cdd:pfam07654   1 PPSPEELGKPNTLVCLVTGFYPPDITVTWLKNGQEVTEGVESTEELPNGDGTYQLSSYLTFTPESGDEYTCRVEHESLPE 80

                  ...
gi 332823708  215 PIT 217
Cdd:pfam07654  81 PIT 83
IgC cd00098
Immunoglobulin Constant domain; IgC: Immunoglobulin constant domain (IgC). Members of the IgC ...
131-221 2.73e-28

Immunoglobulin Constant domain; IgC: Immunoglobulin constant domain (IgC). 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: 143166  Cd Length: 95  Bit Score: 104.84  E-value: 2.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 131 VTI-SPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQ---HGDVYTCH 206
Cdd:cd00098    1 VFLlPPSPEELLGGSVTLTCLATGFYPPDITVTWLKNGKELTSGVTTTPPVPNSDGTYSVSSQLTVSPSdwnSGDTYTCV 80
                         90
                 ....*....|....*
gi 332823708 207 VEHPSLQNPITVEWR 221
Cdd:cd00098   81 VTHESLPEPLTKSIP 95
IGc1 smart00407
Immunoglobulin C-Type;
144-215 2.46e-25

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 96.23  E-value: 2.46e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332823708   144 HNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEM---TPQHGDVYTCHVEHPSLQNP 215
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVpasTWESGDVYTCQVTHEGLKEP 75
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
127-220 1.65e-20

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: 83.49  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 127 VEPTVTISPSRteALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCH 206
Cdd:cd07698    1 VPPEVRVTRKR--APDGSLTLSCHATGFYPRDIEVTWLRDGEDSVDDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCR 78
                         90
                 ....*....|....
gi 332823708 207 VEHPSLQNPITVEW 220
Cdd:cd07698   79 VEHSGLKEPLIVPW 92
IgC_beta2m cd05770
Class I major histocompatibility complex (MHC) beta2-microglobulin; IgC_beta2m: ...
145-221 8.16e-18

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: 75.98  E-value: 8.16e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332823708 145 NLLVCSVTDFYPGQIKVRWFRNDQEeTTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVEHPSLQNPITVEWR 221
Cdd:cd05770   18 NVLNCYVTGFHPPDIEIRLLKNGVK-IPKVEQSDLSFSKDWTFYLLKSTEFTPTKGDEYACRVRHNSMSEPKKYKWD 93
IgC_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
129-220 3.43e-17

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: 73.91  E-value: 3.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 129 PTVTISPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGDVYTCHVE 208
Cdd:cd05767    2 PEVTVFSLKPVELGEPNTLICFVDNFFPPVLNVTWLKNGVPVTDGVSETRYYPRQDLSFQKFSYLNFTPEEGDIYSCIVE 81
                         90
                 ....*....|..
gi 332823708 209 HPSLQNPITVEW 220
Cdd:cd05767   82 HWGLETPATRYW 93
IgC_L cd07699
Immunoglobulin Constant domain; IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. ...
128-217 7.76e-15

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: 143323  Cd Length: 100  Bit Score: 67.84  E-value: 7.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 128 EPTVTISPSRTEALNHHN--LLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQHGD---V 202
Cdd:cd07699    1 APSVTIFPPSSEELEKSGkaTLVCLINDFYPGFATVQWKVDGATVSSGVQTSTTEQQSDNTYSLSSYLTLTKSDWNkhkV 80
                         90
                 ....*....|....*
gi 332823708 203 YTCHVEHPSLQNPIT 217
Cdd:cd07699   81 YTCEVTHEGLSSTIT 95
IgC_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); ...
147-210 4.24e-09

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: 52.02  E-value: 4.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332823708 147 LVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQH---GDVYTCHVEHP 210
Cdd:cd05847   19 LLCLISGYTPGTIEVEWLVDGQVATLVAASTAPQKEEGSTFSTTSELNVTQEDwksGKTYTCKVTHQ 85
IgC_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain; IgC_TCR_beta: Constant domain ...
128-189 9.28e-09

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: 51.22  E-value: 9.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332823708 128 EPTVTI-SPSRTEALNHHNL-LVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPL-IRNGDWTFQI 189
Cdd:cd05769    2 PPTVAIfPPSEAEIRNKRKAtLVCLATGFYPDHVSLSWKVNGKEVTDGVATDPQaLRENTSTYSI 66
IgC_CH4 cd05768
CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH4: The ...
129-217 1.15e-07

CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH4: The fourth immunoglobulin constant domain (IgC), of immunoglobulin (Ig) 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: 143245  Cd Length: 102  Bit Score: 48.14  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 129 PTVTISPSRTEALNHHNL--LVCSVTDFYPGQIKVRWFRNDQE------ETTGVVSTPLIRNGDWTFQILVMLEMTPQHG 200
Cdd:cd05768    1 PSVYVLPPPSEELSLQETatLTCLVKGFSPSDIFVKWLQNGQPlskqkyVTTAPMQEPGGNESYFLYSKLTVSAEDWNAG 80
                         90
                 ....*....|....*..
gi 332823708 201 DVYTCHVEHPSLQNPIT 217
Cdd:cd05768   81 DVFTCVVGHEALPLQLT 97
Ig cd00096
Immunoglobulin domain; Ig: immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
147-219 1.10e-06

Immunoglobulin domain; Ig: 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, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, 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.


Pssm-ID: 143165 [Multi-domain]  Cd Length: 74  Bit Score: 44.79  E-value: 1.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332823708 147 LVCSVTDfyPGQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQ-ILVMLEMTPQHGDVYTCHVEHPSLQNPITVE 219
Cdd:cd00096    3 LTCLASG--PPPPTITWLKNGKPLPSSVLTRVRSSRGTSSGSsTLTISNVTLEDSGTYTCVASNSAGTVSASVT 74
IgC_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; IgC_Tapasin_R: Immunoglobulin-like domain on Tapasin-R. ...
129-218 3.89e-06

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: 143248 [Multi-domain]  Cd Length: 139  Bit Score: 44.07  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 129 PTVTISPSRTEALNHHNL-LVCSVTDFYPGQIKVRWFRndqEETTGVVSTPLIRNG---------DWTFQILVMLEMTP- 197
Cdd:cd05771   39 PRVRLSLEKLVSMIEEPQtLICHIAGYYPLDVQVEWTR---EPPGDSPPPVSLSNVsfsshrqhqDGTYSLSSHLTLEPg 115
                         90       100
                 ....*....|....*....|...
gi 332823708 198 --QHGDVYTCHVEHPSLQNPITV 218
Cdd:cd05771  116 teDAGATYTCRVSHVSLETPVSL 138
IgC_SIRP cd05772
Signal-regulatory protein (SIRP) immunoglobulin-like domain; IgC_SIRP: Immunoglobulin-like ...
126-216 2.79e-05

Signal-regulatory protein (SIRP) immunoglobulin-like domain; IgC_SIRP: Immunoglobulin-like domain of signal-regulatory proteins (SIRP); the signal-regulatory proteins (SIRP) are Ig-like cell surface receptors detected in hematopoietic and non-hematopoietic cells. While their extracellular domains are similar, SIRP are classified as alpha or beta based on the length of the intracytoplasmic domain. Those having a 110- to 113-amino acid tail are classified as SIRP-alpha, and those having a 5-amino acid tail as SIRP-beta. SIRP-alpha and SIRP-beta molecules are thought to have complementary roles in signal regulation: SIRP-alpha inhibit signalling via their immunoreceptor tyrosine (IT)-based inhibition motifs while SIRP-beta are activating. SIRP-beta lack the cytoplasmic domainof SIRP-alpha, and associate with at least one other transmembrane protein (DAP-12 or KARAP). The IT-based activation motifs within DAP-12's cytoplasmic domain may link SIRP-beta to the activating machinery.


Pssm-ID: 143249  Cd Length: 111  Bit Score: 41.04  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 126 RVEPTVTI--SPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVS-TPLIRNGDW--TFQILVMLEMTPQHG 200
Cdd:cd05772    3 RAKPSVPVvsGPSGRANPGQSVNFTCSAHGFSPRDITVKWLKNGNELSAEQPNiTPEGDSVSYnvTSTVQVKLTEDDVHS 82
                         90
                 ....*....|....*.
gi 332823708 201 DVyTCHVEHPSLQNPI 216
Cdd:cd05772   83 QV-TCEVQHRTLQAPL 97
IgC_CH1 cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH1: The first ...
149-219 9.66e-05

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH1: The first immunoglobulin constant domain (IgC), of immunoglobulin (Ig) 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: 143186  Cd Length: 95  Bit Score: 39.20  E-value: 9.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332823708 149 CSVTDFYPGQIKVRWFrNDQEETTGVVSTP--LIRNGDWTF--QILVMlEMTPQHGDVYTCHVEHPSLQNPITVE 219
Cdd:cd04985   23 CLATGFLPEPVTFTWN-SGSNSTSGVKTYPavLQSGGLYTAssQLTVP-ASEWKGKESFYCKVEHPSTSVDKTVP 95
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
129-216 1.09e-04

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 254659  Cd Length: 89  Bit Score: 39.34  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708  129 PTVTISPSRTEALNHHNLLVCSVTDFYPgQIKVRWFRNDQEETTGVVSTpLIRNGDWTFQILVMLEMTPQHGDV---YTC 205
Cdd:pfam08205   1 PTIEPPVSLLEGENLEVVATCSSAGGKP-APRITWYLDGRELEAITTSS-EQDPESGLYTVTSTLKLVPSREDHgrsLTC 78
                          90
                  ....*....|.
gi 332823708  206 HVEHPSLQNPI 216
Cdd:pfam08205  79 QVSYGALRGQK 89
IgC_TCR_gamma cd07697
T cell receptor (TCR) gamma chain constant immunoglobulin domain; IgC_TCR_gamma; ...
128-214 4.42e-04

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: 143321  Cd Length: 96  Bit Score: 37.63  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708 128 EPTVTISPSRTEALNHHNLLVCSVTDFYPGQIKVRWFRNDQEETTGVVSTPLIRNGD--WTFQILVMLEMTPqhGDVYTC 205
Cdd:cd07697    2 KPTIFSPSKKEIEKQGQGIYLCLLENFFPDVIQVHWREGNSPSILGSQKSEKDKDNDvySTTSWLTVTKDSL--GKKFRC 79

                 ....*....
gi 332823708 206 HVEHPSLQN 214
Cdd:cd07697   80 IYKHEGISK 88
Ig2_Necl-1-4_like cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4 (also ...
160-214 1.29e-03

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4 (also known as cell adhesion molecules CADM3, CADM1, CADM2, and CADM4, respectively); Ig2_Necl-1-4_like: domain similar to the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2) and Necl-4 (CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 143238  Cd Length: 82  Bit Score: 35.77  E-value: 1.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332823708 160 KVRWFRNDQEeTTGVVSTPLIRNGD-WTFQILVMLEMTPQ-HGDVYTCHVEHPSLQN 214
Cdd:cd05761   16 TIRWFKGDKE-LKGVKLKEEDENGKtFTVTSSLRFQVDREdDGAPIICRVDHPALKS 71
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
128-209 2.64e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 258189  Cd Length: 75  Bit Score: 35.03  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332823708  128 EPTVTISPSRTEALNHHNL-LVCSVTDfYPGQIKVRWFRNDQEETTGVVSTPLIrngdwtfQILVMLEMTPQHGDVYTCH 206
Cdd:pfam13927   1 KPVITVSPSPSVTSGGGGVtLTCSAEG-GPPPPTISWYRNGSISNGSGGLGSSG-------STLTISSVTPEDSGTYTCV 72

                  ...
gi 332823708  207 VEH 209
Cdd:pfam13927  73 ASN 75
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
147-207 6.32e-03

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. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.


Pssm-ID: 249539  Cd Length: 62  Bit Score: 33.66  E-value: 6.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332823708  147 LVCSVTDfyPGQIKVRWFRNDQEETTGVVSTPLIRNGdwTFQILVMLEMTPQHGDVYTCHV 207
Cdd:pfam00047   6 LTCSVSG--PPQVDVTWFKEGKGLEESTTVGTDTNRV--SSITLTISNVTPEDSGTYTCVV 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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