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Conserved domains on  [gi|4504377|ref|NP_000401|]
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hereditary hemochromatosis protein isoform 1 precursor [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
MHC_I super family cl08246
Class I Histocompatibility antigen, domains alpha 1 and 2;
27-202 3.62e-43

Class I Histocompatibility antigen, domains alpha 1 and 2;


The actual alignment was detected with superfamily member pfam00129:

Pssm-ID: 298647  Cd Length: 179  Bit Score: 149.08  E-value: 3.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377     27 SHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDH--ESRRVEPRTPWVSsRISSQMWLQLSQSLKGWDHMFTVDFWT 104
Cdd:pfam00129   2 SHSLRYFYTAVSRPGLGEPRFIAVGYVDDTQFVRFDSdaANPRMEPRAPWIE-QEGPEYWERETQIAKGNEQIFRENLRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377    105 IMENHNHSK-ESHTLQVILGCEMQEDN-STEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQnRAY 182
Cdd:pfam00129  81 LLGYYNQSEgGSHTLQWMYGCDVGPDGrLLRGYEQFAYDGKDYIALNEDLRSWTAADPAAQITKRKWEAAGEAERQ-RAY 159
                         170       180
                  ....*....|....*....|
gi 4504377    183 LERDCPAQLQQLLELGRGVL 202
Cdd:pfam00129 160 LEGECVEWLRRYLENGKETL 179
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
206-298 5.01e-34

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: 122.01  E-value: 5.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  206 VPPLVKVTHHVTS-SVTTLRCRALNYYPQNITMKWLKDKQPMDaKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQV 284
Cdd:cd07698   1 VPPEVRVTRKRAPdGSLTLSCHATGFYPRDIEVTWLRDGEDSV-DDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCRV 79
                        90
                ....*....|....
gi 4504377  285 EHPGLDQPLIVIWE 298
Cdd:cd07698  80 EHSGLKEPLIVPWE 93
 
Name Accession Description Interval E-value
MHC_I pfam00129
Class I Histocompatibility antigen, domains alpha 1 and 2;
27-202 3.62e-43

Class I Histocompatibility antigen, domains alpha 1 and 2;


Pssm-ID: 278555  Cd Length: 179  Bit Score: 149.08  E-value: 3.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377     27 SHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDH--ESRRVEPRTPWVSsRISSQMWLQLSQSLKGWDHMFTVDFWT 104
Cdd:pfam00129   2 SHSLRYFYTAVSRPGLGEPRFIAVGYVDDTQFVRFDSdaANPRMEPRAPWIE-QEGPEYWERETQIAKGNEQIFRENLRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377    105 IMENHNHSK-ESHTLQVILGCEMQEDN-STEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQnRAY 182
Cdd:pfam00129  81 LLGYYNQSEgGSHTLQWMYGCDVGPDGrLLRGYEQFAYDGKDYIALNEDLRSWTAADPAAQITKRKWEAAGEAERQ-RAY 159
                         170       180
                  ....*....|....*....|
gi 4504377    183 LERDCPAQLQQLLELGRGVL 202
Cdd:pfam00129 160 LEGECVEWLRRYLENGKETL 179
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
206-298 5.01e-34

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: 122.01  E-value: 5.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  206 VPPLVKVTHHVTS-SVTTLRCRALNYYPQNITMKWLKDKQPMDaKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQV 284
Cdd:cd07698   1 VPPEVRVTRKRAPdGSLTLSCHATGFYPRDIEVTWLRDGEDSV-DDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCRV 79
                        90
                ....*....|....
gi 4504377  285 EHPGLDQPLIVIWE 298
Cdd:cd07698  80 EHSGLKEPLIVPWE 93
C1-set pfam07654
Immunoglobulin C1-set domain;
222-294 4.42e-16

Immunoglobulin C1-set domain;


Pssm-ID: 284964  Cd Length: 86  Bit Score: 72.32  E-value: 4.42e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504377    222 TLRCRALNYYPQNITMKWLKDKQPM--DAKEFEPkdvLPNGDGTYQGWITLAVPPGEEQR---YTCQVEHPGLDQPLI 294
Cdd:pfam07654  12 TLTCLVTGFYPPDITVTWLKNGQEVteGVKTTDP---SPNSDWSYQLSSYLTVTPSDWESgdeYTCRVEHEGLPEPVE 86
IGc1 smart00407
Immunoglobulin C-Type;
222-292 6.09e-15

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 68.88  E-value: 6.09e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504377     222 TLRCRALNYYPQNITMKWLKDKQPMdAKEFEPKDVLPNGDGTYQGWITLAVP---PGEEQRYTCQVEHPGLDQP 292
Cdd:smart00407   3 TLVCLVSGFYPPDITVTWLRNGQEV-TEGVSTTDPLKNSDGTYFLSSYLTVPastWESGDVYTCQVTHEGLKEP 75
PHA02865 PHA02865
MHC-like TNF binding protein; Provisional
41-245 7.96e-05

MHC-like TNF binding protein; Provisional


Pssm-ID: 165199 [Multi-domain]  Cd Length: 338  Bit Score: 42.54  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377    41 DLGLSLFEALGYVDDQLF--VFYDHESRRVEPRTpwvssriSSQMWLQLSQS--LKGWDHMFtvDFW------TIME-NH 109
Cdd:PHA02865  32 DTGLYDFVVTDYFNDQLIkrIKLNHETGRPENVN-------FRPTWFNETKIphYPGNDYNF--NFWlnlmkeTLEEiNK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377   110 NHSKESHTLQVILGCEmqedNSTEGYWKYGY---DGQDHLEFCPDTLDWRAAEPRAWP-------TKLEWERHKiraRQN 179
Cdd:PHA02865 103 NESTKYTSLSLIVGCT----DLGQLFGSFGYvevAGGILARFDTKNKRFTKVTSKGFPkvgmltvKSPFWKDVM---KYL 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504377   180 RAYLERDCPAQLQQLLELGRGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKW--LKDKQP 245
Cdd:PHA02865 176 GSFVYLTCGLTANDYQKMAKGNIPKPVTPTVKVTGEELGDNTTLFCTFDSHYPSSVAAKWynSEDFAP 243
 
Name Accession Description Interval E-value
MHC_I pfam00129
Class I Histocompatibility antigen, domains alpha 1 and 2;
27-202 3.62e-43

Class I Histocompatibility antigen, domains alpha 1 and 2;


Pssm-ID: 278555  Cd Length: 179  Bit Score: 149.08  E-value: 3.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377     27 SHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDH--ESRRVEPRTPWVSsRISSQMWLQLSQSLKGWDHMFTVDFWT 104
Cdd:pfam00129   2 SHSLRYFYTAVSRPGLGEPRFIAVGYVDDTQFVRFDSdaANPRMEPRAPWIE-QEGPEYWERETQIAKGNEQIFRENLRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377    105 IMENHNHSK-ESHTLQVILGCEMQEDN-STEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQnRAY 182
Cdd:pfam00129  81 LLGYYNQSEgGSHTLQWMYGCDVGPDGrLLRGYEQFAYDGKDYIALNEDLRSWTAADPAAQITKRKWEAAGEAERQ-RAY 159
                         170       180
                  ....*....|....*....|
gi 4504377    183 LERDCPAQLQQLLELGRGVL 202
Cdd:pfam00129 160 LEGECVEWLRRYLENGKETL 179
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
206-298 5.01e-34

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: 122.01  E-value: 5.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  206 VPPLVKVTHHVTS-SVTTLRCRALNYYPQNITMKWLKDKQPMDaKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQV 284
Cdd:cd07698   1 VPPEVRVTRKRAPdGSLTLSCHATGFYPRDIEVTWLRDGEDSV-DDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCRV 79
                        90
                ....*....|....
gi 4504377  285 EHPGLDQPLIVIWE 298
Cdd:cd07698  80 EHSGLKEPLIVPWE 93
IgC cd00098
Immunoglobulin Constant domain; IgC: Immunoglobulin constant domain (IgC). Members of the IgC ...
208-298 1.42e-20

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: 84.43  E-value: 1.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  208 PLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPkDVLPNGDGTYQGWITLAVPPGEEQR---YTCQV 284
Cdd:cd00098   3 LLPPSPEELLGGSVTLTCLATGFYPPDITVTWLKNGKELTSGVTTT-PPVPNSDGTYSVSSQLTVSPSDWNSgdtYTCVV 81
                        90
                ....*....|....
gi 4504377  285 EHPGLDQPLIVIWE 298
Cdd:cd00098  82 THESLPEPLTKSIP 95
IgC_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; ...
217-299 1.11e-17

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: 76.67  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  217 TSSVTTLRCRALNYYPQNITMKWLKDKQpMDAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVI 296
Cdd:cd05766  13 LSHPHLLVCHVWGFYPPEITVKWFKNGQ-EETEGVVSTELIPNGDWTYQILVMLETTPSRGDTYTCVVEHSSLQEPLTVD 91

                ...
gi 4504377  297 WEP 299
Cdd:cd05766  92 WRP 94
C1-set pfam07654
Immunoglobulin C1-set domain;
222-294 4.42e-16

Immunoglobulin C1-set domain;


Pssm-ID: 284964  Cd Length: 86  Bit Score: 72.32  E-value: 4.42e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504377    222 TLRCRALNYYPQNITMKWLKDKQPM--DAKEFEPkdvLPNGDGTYQGWITLAVPPGEEQR---YTCQVEHPGLDQPLI 294
Cdd:pfam07654  12 TLTCLVTGFYPPDITVTWLKNGQEVteGVKTTDP---SPNSDWSYQLSSYLTVTPSDWESgdeYTCRVEHEGLPEPVE 86
IGc1 smart00407
Immunoglobulin C-Type;
222-292 6.09e-15

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 68.88  E-value: 6.09e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504377     222 TLRCRALNYYPQNITMKWLKDKQPMdAKEFEPKDVLPNGDGTYQGWITLAVP---PGEEQRYTCQVEHPGLDQP 292
Cdd:smart00407   3 TLVCLVSGFYPPDITVTWLRNGQEV-TEGVSTTDPLKNSDGTYFLSSYLTVPastWESGDVYTCQVTHEGLKEP 75
IgC_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
207-298 1.21e-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: 65.82  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  207 PPLVKV--THHVTSSV-TTLRCRALNYYPQNITMKWLKDKQPMdAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQ 283
Cdd:cd05767   1 PPEVTVfsLKPVELGEpNTLICFVDNFFPPVLNVTWLKNGVPV-TDGVSETRYYPRQDLSFQKFSYLNFTPEEGDIYSCI 79
                        90
                ....*....|....*
gi 4504377  284 VEHPGLDQPLIVIWE 298
Cdd:cd05767  80 VEHWGLETPATRYWE 94
IgC_beta2m cd05770
Class I major histocompatibility complex (MHC) beta2-microglobulin; IgC_beta2m: ...
207-298 1.89e-09

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: 54.02  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  207 PPLVKV-THHVTSSVTT--LRCRALNYYPQNITMKWLKDKQPMDakEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQ 283
Cdd:cd05770   1 TPKVQVySRFPAENGKPnvLNCYVTGFHPPDIEIRLLKNGVKIP--KVEQSDLSFSKDWTFYLLKSTEFTPTKGDEYACR 78
                        90
                ....*....|....*
gi 4504377  284 VEHPGLDQPLIVIWE 298
Cdd:cd05770  79 VRHNSMSEPKKYKWD 93
IgC_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; IgC_Tapasin_R: Immunoglobulin-like domain on Tapasin-R. ...
188-293 6.73e-09

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: 52.93  E-value: 6.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  188 PAQLQQLLELgrgvlDQQVPPLVKVTHHVTSSVT----TLRCRALNYYPQNITMKWLKdKQPMDakefEPKDVLPNG--- 260
Cdd:cd05771  24 PHQAQQIIQL-----SVSEPPRVRLSLEKLVSMIeepqTLICHIAGYYPLDVQVEWTR-EPPGD----SPPPVSLSNvsf 93
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4504377  261 -------DGTYQGWITLAVPPGEEQR---YTCQVEHPGLDQPL 293
Cdd:cd05771  94 sshrqhqDGTYSLSSHLTLEPGTEDAgatYTCRVSHVSLETPV 136
IgC_CH1 cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH1: The first ...
208-295 1.21e-06

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: 45.75  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  208 PLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMD-AKEFEPkdVLPNGdGTYQGWITLAVPPGEE---QRYTCQ 283
Cdd:cd04985   6 PLVPCCSSSSSDSVTLGCLATGFLPEPVTFTWNSGSNSTSgVKTYPA--VLQSG-GLYTASSQLTVPASEWkgkESFYCK 82
                        90
                ....*....|..
gi 4504377  284 VEHPGLDQPLIV 295
Cdd:cd04985  83 VEHPSTSVDKTV 94
Ig cd00096
Immunoglobulin domain; Ig: immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
222-288 5.64e-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  Cd Length: 74  Bit Score: 43.63  E-value: 5.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  222 TLRCRAlnYYPQNITMKWLKDKQPMDAKEFEPKdvlPNGDGTYQGWITLAVPPGEEQ---RYTCQVEHPG 288
Cdd:cd00096   2 TLTCLA--SGPPPPTITWLKNGKPLPSSVLTRV---RSSRGTSSGSSTLTISNVTLEdsgTYTCVASNSA 66
IgC_L cd07699
Immunoglobulin Constant domain; IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. ...
217-292 8.55e-05

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: 40.11  E-value: 8.55e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504377  217 TSSVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVlPNGDGTYQGWITLAVPPGE---EQRYTCQVEHPGLDQP 292
Cdd:cd07699  16 KSGKATLVCLINDFYPGFATVQWKVDGATVSSGVQTSTTE-QQSDNTYSLSSYLTLTKSDwnkHKVYTCEVTHEGLSST 93
IgC_SIRP cd05772
Signal-regulatory protein (SIRP) immunoglobulin-like domain; IgC_SIRP: Immunoglobulin-like ...
225-293 1.71e-04

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: 39.50  E-value: 1.71e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504377  225 CRALNYYPQNITMKWLKDKQPMDAkefEPKDVLPNGDG-TYQGWITLAVPPGEE---QRYTCQVEHPGLDQPL 293
Cdd:cd05772  28 CSAHGFSPRDITVKWLKNGNELSA---EQPNITPEGDSvSYNVTSTVQVKLTEDdvhSQVTCEVQHRTLQAPL 97
MHC_I_3 pfam16497
MHC-I family domain;
61-148 2.11e-04

MHC-I family domain;


Pssm-ID: 293106  Cd Length: 180  Bit Score: 40.41  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377     61 YDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFwtimenHNHSKESH-----TLQVILGCEMQEDNSTEGY 135
Cdd:pfam16497  40 WDNKSGTIIFLKPWSKGNLSNEEWEELEHLFRVYRISFTRDF------QEHASMWQleypfEVQLSAGCELHPGNASVGF 113
                          90
                  ....*....|...
gi 4504377    136 WKYGYDGQDHLEF 148
Cdd:pfam16497 114 LRVAYQGSDLLSF 126
IgC_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE); ...
217-290 2.99e-04

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: 38.54  E-value: 2.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377  217 TSSVTTLRCRALNYYPQNITMKWLKDKQPMdakefepKDVLPN------GDGTYQGWITLAVPPGE---EQRYTCQVEHP 287
Cdd:cd05847  13 TSETIQLLCLISGYTPGTIEVEWLVDGQVA-------TLVAAStapqkeEGSTFSTTSELNVTQEDwksGKTYTCKVTHQ 85

                ...
gi 4504377  288 GLD 290
Cdd:cd05847  86 GTT 88
IgC_CH4 cd05768
CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin; IgC_CH4: The ...
222-290 3.16e-03

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: 35.42  E-value: 3.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504377  222 TLRCRALNYYPQNITMKWLKDKQPMDAKEF---EPKDVLPnGDGTYQGWITLAVPPGEEQR---YTCQVEHPGLD 290
Cdd:cd05768  20 TLTCLVKGFSPSDIFVKWLQNGQPLSKQKYvttAPMQEPG-GNESYFLYSKLTVSAEDWNAgdvFTCVVGHEALP 93
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
216-285 9.43e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar proteins; Ig2_FGFR_like: domain similar to the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 143206  Cd Length: 85  Bit Score: 33.90  E-value: 9.43e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504377  216 VTSSVTtLRCRALNYYPQNITmkWLKdkqpmDAKEFEPKDVLPNGDGTYQGW--ITLAVPPGEEQRYTCQVE 285
Cdd:cd05729   8 AGSTVR-LKCPASGNPRPTIT--WLK-----DGKPFKKEHRIGGYKVRKKKWtlILESVVPSDSGKYTCIVE 71
PHA02865 PHA02865
MHC-like TNF binding protein; Provisional
41-245 7.96e-05

MHC-like TNF binding protein; Provisional


Pssm-ID: 165199 [Multi-domain]  Cd Length: 338  Bit Score: 42.54  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377    41 DLGLSLFEALGYVDDQLF--VFYDHESRRVEPRTpwvssriSSQMWLQLSQS--LKGWDHMFtvDFW------TIME-NH 109
Cdd:PHA02865  32 DTGLYDFVVTDYFNDQLIkrIKLNHETGRPENVN-------FRPTWFNETKIphYPGNDYNF--NFWlnlmkeTLEEiNK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504377   110 NHSKESHTLQVILGCEmqedNSTEGYWKYGY---DGQDHLEFCPDTLDWRAAEPRAWP-------TKLEWERHKiraRQN 179
Cdd:PHA02865 103 NESTKYTSLSLIVGCT----DLGQLFGSFGYvevAGGILARFDTKNKRFTKVTSKGFPkvgmltvKSPFWKDVM---KYL 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504377   180 RAYLERDCPAQLQQLLELGRGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKW--LKDKQP 245
Cdd:PHA02865 176 GSFVYLTCGLTANDYQKMAKGNIPKPVTPTVKVTGEELGDNTTLFCTFDSHYPSSVAAKWynSEDFAP 243
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
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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