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Conserved domains on  [gi|20150824|pdb|1KJ2|H]
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Chain H, Allogeneic H-2Kb MHC Class I Molecule

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MHC_I pfam00129
Class I Histocompatibility antigen, domains alpha 1 and 2.
2-179 7.74e-121

Class I Histocompatibility antigen, domains alpha 1 and 2.


:

Pssm-ID: 365893  Cd Length: 178  Bit Score: 342.45  E-value: 7.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H          2 PHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTL 81
Cdd:pfam00129   1 SHSLRYFYTAVSRPGLGEPRFIAVGYVDDTQFVRFDSDAENPRMEPRAPWIEQEGPEYWERETQIAKGNEQIFRENLRTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H         82 LGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLE 161
Cdd:pfam00129  81 LGYYNQSEGGSHTLQWMYGCDVGPDGRLLRGYEQFAYDGKDYIALNEDLRSWTAADPAAQITKRKWEAAGEAERRRAYLE 160
                         170
                  ....*....|....*...
1KJ2_H        162 GTCVEWLRRYLKNGNATL 179
Cdd:pfam00129 161 GECVEWLRRYLENGKETL 178
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain. ...
183-275 4.07e-43

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: 142.04  E-value: 4.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      183 DSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVY 262
Cdd:cd07698   1 VPPEVRVTRKRAPDGSLTLSCHATGFYPRDIEVTWLRDGEDSVDDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCRVE 80
                        90
                ....*....|...
1KJ2_H      263 HQGLPEPLTLRWE 275
Cdd:cd07698  81 HSGLKEPLIVPWE 93
 
Name Accession Description Interval E-value
MHC_I pfam00129
Class I Histocompatibility antigen, domains alpha 1 and 2.
2-179 7.74e-121

Class I Histocompatibility antigen, domains alpha 1 and 2.


Pssm-ID: 365893  Cd Length: 178  Bit Score: 342.45  E-value: 7.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H          2 PHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTL 81
Cdd:pfam00129   1 SHSLRYFYTAVSRPGLGEPRFIAVGYVDDTQFVRFDSDAENPRMEPRAPWIEQEGPEYWERETQIAKGNEQIFRENLRTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H         82 LGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLE 161
Cdd:pfam00129  81 LGYYNQSEGGSHTLQWMYGCDVGPDGRLLRGYEQFAYDGKDYIALNEDLRSWTAADPAAQITKRKWEAAGEAERRRAYLE 160
                         170
                  ....*....|....*...
1KJ2_H        162 GTCVEWLRRYLKNGNATL 179
Cdd:pfam00129 161 GECVEWLRRYLENGKETL 178
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain. ...
183-275 4.07e-43

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: 142.04  E-value: 4.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      183 DSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVY 262
Cdd:cd07698   1 VPPEVRVTRKRAPDGSLTLSCHATGFYPRDIEVTWLRDGEDSVDDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCRVE 80
                        90
                ....*....|...
1KJ2_H      263 HQGLPEPLTLRWE 275
Cdd:cd07698  81 HSGLKEPLIVPWE 93
IGc1 smart00407
Immunoglobulin C-Type;
198-269 3.22e-21

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 84.67  E-value: 3.22e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1KJ2_H         198 KVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPL---GKEQYYTCHVYHQGLPEP 269
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPAstwESGDVYTCQVTHEGLKEP 75
C1-set pfam07654
Immunoglobulin C1-set domain.
197-266 5.74e-19

Immunoglobulin C1-set domain.


Pssm-ID: 369453  Cd Length: 85  Bit Score: 79.21  E-value: 5.74e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1KJ2_H        197 DKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVP---LGKEQYYTCHVYHQGL 266
Cdd:pfam07654  13 KPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVTTTPPSPNSDWTYQLSSYLTVTpsdWESGDTYTCRVEHEGL 85
 
Name Accession Description Interval E-value
MHC_I pfam00129
Class I Histocompatibility antigen, domains alpha 1 and 2.
2-179 7.74e-121

Class I Histocompatibility antigen, domains alpha 1 and 2.


Pssm-ID: 365893  Cd Length: 178  Bit Score: 342.45  E-value: 7.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H          2 PHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTL 81
Cdd:pfam00129   1 SHSLRYFYTAVSRPGLGEPRFIAVGYVDDTQFVRFDSDAENPRMEPRAPWIEQEGPEYWERETQIAKGNEQIFRENLRTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H         82 LGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLE 161
Cdd:pfam00129  81 LGYYNQSEGGSHTLQWMYGCDVGPDGRLLRGYEQFAYDGKDYIALNEDLRSWTAADPAAQITKRKWEAAGEAERRRAYLE 160
                         170
                  ....*....|....*...
1KJ2_H        162 GTCVEWLRRYLKNGNATL 179
Cdd:pfam00129 161 GECVEWLRRYLENGKETL 178
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain. ...
183-275 4.07e-43

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: 142.04  E-value: 4.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      183 DSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVY 262
Cdd:cd07698   1 VPPEVRVTRKRAPDGSLTLSCHATGFYPRDIEVTWLRDGEDSVDDVESGEILPNGDGTYQLWVTLEVPPEDKARYSCRVE 80
                        90
                ....*....|...
1KJ2_H      263 HQGLPEPLTLRWE 275
Cdd:cd07698  81 HSGLKEPLIVPWE 93
IGc1 smart00407
Immunoglobulin C-Type;
198-269 3.22e-21

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 84.67  E-value: 3.22e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1KJ2_H         198 KVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPL---GKEQYYTCHVYHQGLPEP 269
Cdd:smart00407   1 KATLVCLVSGFYPPDITVTWLRNGQEVTEGVSTTDPLKNSDGTYFLSSYLTVPAstwESGDVYTCQVTHEGLKEP 75
C1-set pfam07654
Immunoglobulin C1-set domain.
197-266 5.74e-19

Immunoglobulin C1-set domain.


Pssm-ID: 369453  Cd Length: 85  Bit Score: 79.21  E-value: 5.74e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1KJ2_H        197 DKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVP---LGKEQYYTCHVYHQGL 266
Cdd:pfam07654  13 KPNTLTCLVTGFYPPDITVTWLKNGQEVTEGVTTTPPSPNSDWTYQLSSYLTVTpsdWESGDTYTCRVEHEGL 85
IgC_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain. ...
195-276 7.90e-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: 73.59  E-value: 7.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      195 PEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRW 274
Cdd:cd05766  13 LSHPHLLVCHVWGFYPPEITVKWFKNGQEETEGVVSTELIPNGDWTYQILVMLETTPSRGDTYTCVVEHSSLQEPLTVDW 92

                ..
1KJ2_H      275 EP 276
Cdd:cd05766  93 RP 94
IgC cd00098
Immunoglobulin Constant (IgC) domain. Members of the IgC family are components of ...
193-275 8.48e-17

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: 73.63  E-value: 8.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      193 SRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQY---YTCHVYHQGLPEP 269
Cdd:cd00098  10 EKLGGTVTLVCLVSGFYPKDITVTWLKNGKEVTSGVSTTPPTKNSDGTFSVTSYLTVPPSDWDEgttYTCEVSHESLSQP 89

                ....*.
1KJ2_H      270 LTLRWE 275
Cdd:cd00098  90 VSKSLN 95
IgC_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain. IgC_Tapasin_R: Immunoglobulin-like domain on Tapasin-R. ...
154-272 2.45e-10

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: 57.15  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      154 ERLRAYLEGT--CVEWLRRYLKNGNATLLRTDSPKAHV--THHSRPEDKVTLRCWALGFYPADITLTWQL----NGEELI 225
Cdd:cd05771   6 PGLTVLDEGTyiCSVSTPPFQAQQIIQLSVSEPPRVRLslEKTVSIEEPQTLICHIAGYYPLDVQVEWTReppgDSPPRV 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1KJ2_H      226 QDME--LVETRPAGDGTFQKWASVVVPLGKEQY---YTCHVYHQGLPEPLTL 272
Cdd:cd05771  86 SVSNvsFSSHRQHADGTYSLSSALTLEPGTPHPgatYTCRVTHVALETPVSV 137
IgC_MHC_II_alpha cd05767
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain. ...
200-275 4.91e-10

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: 55.04  E-value: 4.91e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1KJ2_H      200 TLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWE 275
Cdd:cd05767  19 TLICFVDNFFPPVLNVTWLKNGVPVTDGVSETRYYPRQDLSFQKFSYLNFTPEEGDIYSCIVEHWGLETPATRYWE 94
IgC_CH3_IgAGD_CH4_IgAEM cd05768
CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin. ...
196-273 6.86e-10

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: 55.01  E-value: 6.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      196 EDKVTLRCWALGFYPADITLTWQLNGEELIQDmELVETRPA---GDGTF----------QKWASVVVplgkeqyYTCHVY 262
Cdd:cd05768  15 LNTVTLTCLVKGFSPEDIFVRWLQNGQPLPEE-DYKTTTPVkeeSDGSFfvyskltvtaSDWKSGDV-------FSCVVG 86
                        90
                ....*....|.
1KJ2_H      263 HQGLPEPLTLR 273
Cdd:cd05768  87 HEALPLQFTQK 97
IgC_beta2m cd05770
Class I major histocompatibility complex (MHC) beta2-microglobulin. IgC_beta2m: ...
185-275 1.04e-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: 54.41  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      185 PKAHV-THHSRPEDKV-TLRCWALGFYPADITLTWQLNGEElIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVY 262
Cdd:cd05770   2 PKVQVySRFPAENGKPnVLNCYVTGFHPPDIEIRLLKNGVK-IPKVEQSDLSFSKDWTFYLLKSTEFTPTKGDEYACRVR 80
                        90
                ....*....|...
1KJ2_H      263 HQGLPEPLTLRWE 275
Cdd:cd05770  81 HNSMSEPKKYKWD 93
IgC_SIRP_domain_2 cd05772
Signal-regulatory protein (SIRP) immunoglobulin-like domain 2. IgC: immunoglobulin (Ig)-like ...
184-271 3.91e-09

Signal-regulatory protein (SIRP) immunoglobulin-like domain 2. IgC: immunoglobulin (Ig)-like domain in Signal-Regulatory Protein (SIRP), domain 2 (C1 repeat 1). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three Immunoglobulin superfamily domains a single V-set and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions that have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs but also binds CD47, but with much less affinity.


Pssm-ID: 319314  Cd Length: 103  Bit Score: 53.09  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      184 SPKAHVThhsrPEDKVTLRCWALGFYPADITLTWQLNGEELiqDMELVETRPAGDG-TFQKWASVVVPLGKE---QYYTC 259
Cdd:cd05772   9 GPAARAT----PGQTVSFTCKSHGFSPRDITLKWFKNGNEL--SALQTTVLPEGDSvSYSVSSTVQVVLTKDdvhSQLTC 82
                        90
                ....*....|..
1KJ2_H      260 HVYHQGLPEPLT 271
Cdd:cd05772  83 EVAHVTLQAPLR 94
IgC_L cd07699
Immunoglobulin Constant domain. IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. ...
197-271 8.05e-07

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: 46.29  E-value: 8.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      197 DKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQkwASVVVPLGKEQY-----YTCHVYHQGLPEPLT 271
Cdd:cd07699  17 GKATLVCLINKFYPGFATVTWKVDGSTVSSGVTTSKTEQQSDNTYS--MSSYLTLSSSDWnkhkvYTCEVTHEGLSSTIT 94
IgC_TCR_beta cd05769
T cell receptor (TCR) beta chain constant immunoglobulin domain. IgC_TCR_beta: Constant ...
198-223 3.76e-05

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: 41.98  E-value: 3.76e-05
                        10        20
                ....*....|....*....|....*.
1KJ2_H      198 KVTLRCWALGFYPADITLTWQLNGEE 223
Cdd:cd05769  20 KATLVCLATGFYPDHVSLSWKVNGKE 45
IgC_CH1_IgAEGM cd04985
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin. IgC_CH2: The ...
193-267 1.42e-04

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: 39.97  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      193 SRPEDKVTLRCWALGFYPADITLTWQLNGEELIQdmelVETRPA---GDGTFQKWASVVVP---LGKEQYYTCHVYHQGL 266
Cdd:cd04985  13 SSSSDSVTLGCLATGFFPEPVTFTWNSGSNSTSG----VKTFPAvlqSGGLYTASSQLTVPaseWKSKKSFYCKVEHPPT 88

                .
1KJ2_H      267 P 267
Cdd:cd04985  89 T 89
ig pfam00047
Immunoglobulin domain. Members of the immunoglobulin superfamily are found in hundreds of ...
186-271 1.79e-04

Immunoglobulin domain. Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 365836  Cd Length: 86  Bit Score: 39.48  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H        186 KAHVTHHSRPEDKVTLRCWALGFYPaDITLTWQLNGEELIQDMELVETRpagDGTFQkwASV-VVPLGKEQ--YYTCHVY 262
Cdd:pfam00047   1 SAPPTVTVLEGESATLTCSASTGSP-LPDVTWSKEGGTLIESLRVKHDN---GRTTQ--SSLlISNVTLEDagTYTCVVN 74

                  ....*....
1KJ2_H        263 HQGLPEPLT 271
Cdd:pfam00047  75 NPGGPATLS 83
IgC_CH2_IgE cd05847
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin E (IgE). ...
197-266 2.48e-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: 39.31  E-value: 2.48e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1KJ2_H      197 DKVTLRCWALGFYPADITLTWQLNGeeliQDMELV--ETRPAGD--GTFQKWASVVVPlgKEQY-----YTCHVYHQGL 266
Cdd:cd05847  15 ETIQLLCLISGYTPGTIEVEWLVDG----QVATLVaaSTAPQKEegSTFSTTSELNVT--QEDWksgktYTCKVTHQGT 87
IgC_CH2_Mu cd16093
CH2 domain (second constant Ig domain of the heavy chain) in immunoglobulin. IgC_CH2: The ...
195-266 1.07e-03

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: 37.68  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KJ2_H      195 PEDKVTLRCWALGFYPADITLTWQLNGEE----LIQDMELVETRPAGDGTFQKWASVVVP----LGKEQyYTCHVYHQGL 266
Cdd:cd16093  15 PRRTSKLICQATGFSPRQISVSWLREGKQvgsgVTTDAVEAEAKESGPTTFRVTSTLTITesewLSQSM-FTCRVDHRGL 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
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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