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Conserved domains on  [gi|1480722|gb|AAB05768|]
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immunoglobulin heavy and light chain variable region [Mus musculus]

Protein Classification

immunoglobulin heavy chain variable domain-containing protein; immunoglobulin domain-containing family protein( domain architecture ID 10141752)

immunoglobulin heavy chain variable domain-containing protein similar to immunoglobulin heavy chains| 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
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 4-116 8.63e-64

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


:

Pssm-ID: 409370 [Multi-domain]  Cd Length: 118  Bit Score: 194.45  E-value: 8.63e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    4 QLQQSGAELMKPGASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEILPGRGSSKYNEKFKGKATFTSDSSSNTAYMQ 83
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 1480722   84 LSSLTSEDSAVYYCASLRPP-----FAYWGQGTLVTVS 116
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGygysyFDYWGQGTTVTVS 118
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 134-238 4.91e-55

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


:

Pssm-ID: 409369  Cd Length: 106  Bit Score: 171.80  E-value: 4.91e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  134 IVMTQSPSSIYASLGERVTITCKASQDI-KSYLGWFQQKPGKSPKTLIYRANRLVDGVPSRFSGSGSGQDYSLTISSLEY 212
Cdd:cd04980   1 IVMTQSPASLSVSPGERVTISCKASQSIsSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTISSVEP 80

                        90       100
                ....*....|....*....|....*.
gi 1480722  213 EDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:cd04980  81 EDAAVYYCQQGYTFPYTFGGGTKLEI 106
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 4-116 8.63e-64

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


Pssm-ID: 409370 [Multi-domain]  Cd Length: 118  Bit Score: 194.45  E-value: 8.63e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    4 QLQQSGAELMKPGASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEILPGRGSSKYNEKFKGKATFTSDSSSNTAYMQ 83
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 1480722   84 LSSLTSEDSAVYYCASLRPP-----FAYWGQGTLVTVS 116
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGygysyFDYWGQGTTVTVS 118
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 134-238 4.91e-55

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


Pssm-ID: 409369  Cd Length: 106  Bit Score: 171.80  E-value: 4.91e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  134 IVMTQSPSSIYASLGERVTITCKASQDI-KSYLGWFQQKPGKSPKTLIYRANRLVDGVPSRFSGSGSGQDYSLTISSLEY 212
Cdd:cd04980   1 IVMTQSPASLSVSPGERVTISCKASQSIsSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTISSVEP 80

                        90       100
                ....*....|....*....|....*.
gi 1480722  213 EDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:cd04980  81 EDAAVYYCQQGYTFPYTFGGGTKLEI 106
IGv smart00406
Immunoglobulin V-Type;
18-98 2.78e-28

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 102.46  E-value: 2.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722      18 SVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEIlPGRGSSKYNEKFKGKATFTSDSSSNTAYMQLSSLTSEDSAVYYC 97
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYI-GSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   .
gi 1480722      98 A 98
Cdd:smart00406  80 A 80
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 138-238 1.81e-16

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 72.49  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    138 QSPSSIYASLGERVTITC--KASQDIKS-YLGWFQQKPGKSPKTLIYRANRL--VDGVPSRFSGSG--SGQDYSLTISSL 210
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCtySSSMSEAStSVYWYRQPPGKGPTFLIAYYSNGseEGVKKGRFSGRGdpSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*...
gi 1480722    211 EYEDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 140-238 1.59e-15

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.46  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722     140 PSSIYASLGERVTITCKASQDIKSYLGWFQQKPgkspKTLIYranrlvdgvPSRFSGSGSGQDYSLTISSLEYEDMGIYY 219
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGG----KLLAE---------SGRFSVSRSGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*....
gi 1480722     220 CLKYDEFPYTFgGGTKLEI 238
Cdd:smart00410  68 CAATNSSGSAS-SGTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 16-115 4.33e-11

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 58.24  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722     16 GASVKISCKATGYTFS-NYWIEWVKQRPGHGLEWigEILpgRGSSKYNEKFKGKA-TFTSDSSSNTAYMQLSSLTSEDSA 93
Cdd:pfam07686  11 GGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTF--LIA--YYSNGSEEGVKKGRfSGRGDPSNGDGSLTIQNLTLSDSG 86

                          90       100
                  ....*....|....*....|..
gi 1480722     94 VYYCASLRPPFAYWGQGTLVTV 115
Cdd:pfam07686  87 TYTCAVIPSGEGVFGKGTRLTV 108
 
Name Accession Description Interval E-value
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 4-116 8.63e-64

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


Pssm-ID: 409370 [Multi-domain]  Cd Length: 118  Bit Score: 194.45  E-value: 8.63e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    4 QLQQSGAELMKPGASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEILPGRGSSKYNEKFKGKATFTSDSSSNTAYMQ 83
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 1480722   84 LSSLTSEDSAVYYCASLRPP-----FAYWGQGTLVTVS 116
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGygysyFDYWGQGTTVTVS 118
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 134-238 4.91e-55

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


Pssm-ID: 409369  Cd Length: 106  Bit Score: 171.80  E-value: 4.91e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  134 IVMTQSPSSIYASLGERVTITCKASQDI-KSYLGWFQQKPGKSPKTLIYRANRLVDGVPSRFSGSGSGQDYSLTISSLEY 212
Cdd:cd04980   1 IVMTQSPASLSVSPGERVTISCKASQSIsSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTISSVEP 80

                        90       100
                ....*....|....*....|....*.
gi 1480722  213 EDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:cd04980  81 EDAAVYYCQQGYTFPYTFGGGTKLEI 106
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 135-236 8.00e-35

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. 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 (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409373  Cd Length: 105  Bit Score: 120.26  E-value: 8.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  135 VMTQsPSSIYASLGERVTITCKASQDIKS--YLGWFQQKPGKSPKTLIYRANRLVDGVPSRFSGSGSGQDYSLTISSLEY 212
Cdd:cd04984   1 VLTQ-PSSLSVSPGETVTITCTGSSGNISgnYVNWYQQKPGSAPRYLIYEDKHRPSGIPDRFSGSKSGNTASLTISGAQT 79

                        90       100
                ....*....|....*....|....
gi 1480722  213 EDMGIYYCLKYDEFPYTFGGGTKL 236
Cdd:cd04984  80 EDEADYYCQVWDSNSYVFGGGTKL 103
IGv smart00406
Immunoglobulin V-Type;
18-98 2.78e-28

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 102.46  E-value: 2.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722      18 SVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEIlPGRGSSKYNEKFKGKATFTSDSSSNTAYMQLSSLTSEDSAVYYC 97
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYI-GSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79


                   .
gi 1480722      98 A 98
Cdd:smart00406  80 A 80
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 136-238 4.16e-28

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


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 103.18  E-value: 4.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  136 MTQSPSSIYASLGERVTITCKASQDIKS-YLGWFQQKPGKSPKTLIYRA---NRLVDGVPSRFSGSGSGQ-DYSLTISSL 210
Cdd:cd00099   1 VTQSPRSLSVQEGESVTLSCEVSSSFSStYIYWYRQKPGQGPEFLIYLSsskGKTKGGVPGRFSGSRDGTsSFSLTISNL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 1480722  211 EYEDMGIYYC---LKYDEFPYTFGGGTKLEI 238
Cdd:cd00099  81 QPEDSGTYYCavsESGGTDKLTFGSGTRLTV 111
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 5-115 4.08e-22

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


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 87.39  E-value: 4.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    5 LQQSGAELMK-PGASVKISCKATGyTFSNYWIEWVKQRPGHGLEWIGEILPGrgSSKYNEKFKGKATFTSDSSSnTAYMQ 83
Cdd:cd00099   1 VTQSPRSLSVqEGESVTLSCEVSS-SFSSTYIYWYRQKPGQGPEFLIYLSSS--KGKTKGGVPGRFSGSRDGTS-SFSLT 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1480722   84 LSSLTSEDSAVYYCASLRPPF---AYWGQGTLVTV 115
Cdd:cd00099  77 ISNLQPEDSGTYYCAVSESGGtdkLTFGSGTRLTV 111
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 138-238 1.81e-16

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 72.49  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    138 QSPSSIYASLGERVTITC--KASQDIKS-YLGWFQQKPGKSPKTLIYRANRL--VDGVPSRFSGSG--SGQDYSLTISSL 210
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCtySSSMSEAStSVYWYRQPPGKGPTFLIAYYSNGseEGVKKGRFSGRGdpSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*...
gi 1480722    211 EYEDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 140-238 1.59e-15

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.46  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722     140 PSSIYASLGERVTITCKASQDIKSYLGWFQQKPgkspKTLIYranrlvdgvPSRFSGSGSGQDYSLTISSLEYEDMGIYY 219
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGG----KLLAE---------SGRFSVSRSGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*....
gi 1480722     220 CLKYDEFPYTFgGGTKLEI 238
Cdd:smart00410  68 CAATNSSGSAS-SGTTLTV 85
IGv smart00406
Immunoglobulin V-Type;
151-220 2.07e-15

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 68.95  E-value: 2.07e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1480722     151 VTITCKASQDIKS--YLGWFQQKPGKSPKTLIYRANRLVD----GVPSRFSGSG--SGQDYSLTISSLEYEDMGIYYC 220
Cdd:smart00406   2 VTLSCKFSGSTFSsyYVSWVRQPPGKGLEWLGYIGSNGSSyyqeSYKGRFTISKdtSKNDVSLTISNLRVEDTGTYYC 79
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 137-236 3.91e-15

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


Pssm-ID: 409480  Cd Length: 110  Bit Score: 68.85  E-value: 3.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  137 TQSPSSIYASLGERVTITCkaSQDIK-SYLGWFQQKPGKSPKTLIYRAN---RLVDGVP-SRFSGSGSGQDYS-LTISSL 210
Cdd:cd05899   2 TQSPRYLIKRRGQSVTLRC--SQKSGhDNMYWYRQDPGKGLQLLFYSYGgglNEEGDLPgDRFSASRPSLTRSsLTIKSA 79

                        90       100
                ....*....|....*....|....*....
gi 1480722  211 EYEDMGIYYC---LKYDEFPYTFGGGTKL 236
Cdd:cd05899  80 EPEDSAVYLCassLGGGADEAYFGPGTRL 108
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 5-115 1.84e-14

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. 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 (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409373  Cd Length: 105  Bit Score: 67.10  E-value: 1.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    5 LQQSGAELMKPGASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEILPGRGSSkYNEKFKGKatftsdSSSNTAYMQL 84
Cdd:cd04984   2 LTQPSSLSVSPGETVTITCTGSSGNISGNYVNWYQQKPGSAPRYLIYEDKHRPSG-IPDRFSGS------KSGNTASLTI 74

                        90       100       110
                ....*....|....*....|....*....|.
gi 1480722   85 SSLTSEDSAVYYCASLRPPFAYWGQGTLVTV 115
Cdd:cd04984  75 SGAQTEDEADYYCQVWDSNSYVFGGGTKLTV 105
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 136-236 4.18e-14

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


Pssm-ID: 409371  Cd Length: 117  Bit Score: 66.62  E-value: 4.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  136 MTQSPSSIYASLGERVTITCKAS-QDI-KSYLGWFQQKPGKSPKTLIY-----RANRLVDGVPSRFSGSGSGQD--YSLT 206
Cdd:cd04982   1 LEQPQLSITREESKSVTISCKVSgIDFsTTYIHWYRQKPGQALERLLYvsstsAVRKDSGKTKNKFEARKDVGKstSTLT 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 1480722  207 ISSLEYEDMGIYYCLKYDEFPYT----FGGGTKL 236
Cdd:cd04982  81 ITNLEKEDSATYYCAYWESGSGYyikvFGSGTKL 114
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 16-115 4.08e-13

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


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 63.44  E-value: 4.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722   16 GASVKISCKATgyTFSNYWIEWVKQRPGHGLEWIGeilpgRGSSKYNEKFKGKATFTSDSSSNTAYMQLSSLTSEDSAVY 95
Cdd:cd04983  13 GENVTLNCNYS--TSTFYYLFWYRQYPGQGPQFLI-----YISSDSGNKKKGRFSATLDKSRKSSSLHISAAQLSDSAVY 85

                        90       100
                ....*....|....*....|....
gi 1480722   96 YCAsLRPPFAYW----GQGTLVTV 115
Cdd:cd04983  86 FCA-LSESGGTGkltfGKGTRLTV 108
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 137-239 5.74e-13

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


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 63.06  E-value: 5.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  137 TQSPSSIYASLGERVTITCKASQDIKSYLGWFQQKPGKSPKTLIYR---ANRLVDGvpsRFSGS--GSGQDYSLTISSLE 211
Cdd:cd04983   2 TQSPQSLSVQEGENVTLNCNYSTSTFYYLFWYRQYPGQGPQFLIYIssdSGNKKKG---RFSATldKSRKSSSLHISAAQ 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 1480722  212 YEDMGIYYC---LKYDEFPYTFGGGTKLEIK 239
Cdd:cd04983  79 LSDSAVYFCalsESGGTGKLTFGKGTRLTVE 109
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 12-115 1.19e-12

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


Pssm-ID: 409480  Cd Length: 110  Bit Score: 62.30  E-value: 1.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722   12 LMKPGASVKISCKAT-GYtfsnYWIEWVKQRPGHGLEWIGEILpgRGSSKYNEKFKGKATFTSDSSSNTAYMQLSSLTSE 90
Cdd:cd05899   9 IKRRGQSVTLRCSQKsGH----DNMYWYRQDPGKGLQLLFYSY--GGGLNEEGDLPGDRFSASRPSLTRSSLTIKSAEPE 82

                        90       100
                ....*....|....*....|....*...
gi 1480722   91 DSAVYYCASLRPPF---AYWGQGTLVTV 115
Cdd:cd05899  83 DSAVYLCASSLGGGadeAYFGPGTRLTV 110
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 5-116 2.61e-12

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


Pssm-ID: 409371  Cd Length: 117  Bit Score: 61.61  E-value: 2.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    5 LQQSGAELMKP-GASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEILPGRGSSKYNEKFKGKATFTSDSSSNTAYMQ 83
Cdd:cd04982   1 LEQPQLSITREeSKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYVSSTSAVRKDSGKTKNKFEARKDVGKSTSTLT 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 1480722   84 LSSLTSEDSAVYYCASLRPPFAYW----GQGTLVTVS 116
Cdd:cd04982  81 ITNLEKEDSATYYCAYWESGSGYYikvfGSGTKLIVT 117
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 12-115 5.64e-12

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.83  E-value: 5.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722      12 LMKPGASVKISCKATGytFSNYWIEWVKQrpghGLEWIGEilpgrgsskynekfkgKATFTSDSSSNTAYMQLSSLTSED 91
Cdd:smart00410   5 TVKEGESVTLSCEASG--SPPPEVTWYKQ----GGKLLAE----------------SGRFSVSRSGSTSTLTISNVTPED 62

                           90       100
                   ....*....|....*....|....
gi 1480722      92 SAVYYCASLRPPFAYWGqGTLVTV 115
Cdd:smart00410  63 SGTYTCAATNSSGSASS-GTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 16-115 4.33e-11

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 58.24  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722     16 GASVKISCKATGYTFS-NYWIEWVKQRPGHGLEWigEILpgRGSSKYNEKFKGKA-TFTSDSSSNTAYMQLSSLTSEDSA 93
Cdd:pfam07686  11 GGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTF--LIA--YYSNGSEEGVKKGRfSGRGDPSNGDGSLTIQNLTLSDSG 86

                          90       100
                  ....*....|....*....|..
gi 1480722     94 VYYCASLRPPFAYWGQGTLVTV 115
Cdd:pfam07686  87 TYTCAVIPSGEGVFGKGTRLTV 108
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 5-115 5.19e-09

Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409497  Cd Length: 116  Bit Score: 52.84  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    5 LQQSGAELM-KPGASVKISCKATGYTfSNYWIEWVKQRPGHGLEWIGEILPGRGSSK---YNEKFKG-KATFTSDSSSNT 79
Cdd:cd07700   1 LLQTPGSLLvQTNQTVKMSCEAKTSP-KNTRIYWLRQRQAPSKDSHFEFLASWDPSKgivYGEGVDQeKLIILSDSDSSR 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 1480722   80 AYMQLSSLTSEDSAVYYCASLRPPFAYWGQGTLVTV 115
Cdd:cd07700  80 YILSLMSVKPEDSGTYFCMTVGSPELIFGTGTKLSV 115
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 137-238 3.45e-08

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta 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. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409503  Cd Length: 112  Bit Score: 50.21  E-value: 3.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  137 TQSPSSIYASLGERVTITCK-ASQDIKSYLGWFQQKPGKSPKTLIYRANRLVDGVPSRFSGS--GSGQDYSLTISSLEYE 213
Cdd:cd07706   3 TQAQPDVSVQVGEEVTLNCRyETSWTNYYLFWYKQLPSGEMTFLIRQDSSEQNAKSGRYSVNfqKAQKSISLTISALQLE 82

                        90       100
                ....*....|....*....|....*...
gi 1480722  214 DMGIYYC---LKYDEFPYTFGGGTKLEI 238
Cdd:cd07706  83 DSAKYFCalsLPYDTDKLIFGKGTRLTV 110
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 2-98 7.22e-07

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


Pssm-ID: 409514  Cd Length: 115  Bit Score: 46.79  E-value: 7.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    2 QVQLQQSGAELMKPGASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIGEIlpgrgSSKYNEKFKGKATFTSDSSSNTAY 81
Cdd:cd16095   1 ETQLEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSL-----DHISTKVSEDRITSSREDTNSQIF 75

                        90
                ....*....|....*..
gi 1480722   82 MQLSSLTSEDSAVYYCA 98
Cdd:cd16095  76 LQIKGLGLRDSGQYHCA 92
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 3-111 8.42e-07

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


Pssm-ID: 409369  Cd Length: 106  Bit Score: 46.23  E-value: 8.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    3 VQLQQSGAELM-KPGASVKISCKATGYTFSNYwIEWVKQRPGHGlewigeilPGRGSSKYNEKFKGKATFTSDSSSNTAY 81
Cdd:cd04980   1 IVMTQSPASLSvSPGERVTISCKASQSISSNY-LAWYQQKPGQA--------PKLLIYYASTLHSGVPSRFSGSGSGTDF 71

                        90       100       110
                ....*....|....*....|....*....|.
gi 1480722   82 -MQLSSLTSEDSAVYYCASLRPPFAYWGQGT 111
Cdd:cd04980  72 tLTISSVEPEDAAVYYCQQGYTFPYTFGGGT 102
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 135-220 2.60e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.09  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    135 VMTQSPSSIYASLGERVTITCKASQdiksylgwfqqkpGKSPKTLIYRANRLVDGVPSRFSGSGSGQdYSLTISSLEYED 214
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATG-------------SPPPTITWYKNGEPISSGSTRSRSLSGSN-STLTISNVTRSD 68


                  ....*.
gi 1480722    215 MGIYYC 220
Cdd:pfam13927  69 AGTYTC 74
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 16-115 2.70e-06

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


Pssm-ID: 409580  Cd Length: 114  Bit Score: 45.24  E-value: 2.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722   16 GASVKISCKATGYTFSNYWIEWVKQRPGHGLEWIgeilpGRGSSKYNEKFKGKATFTSDSSSNTAYMQLSSLTSEDSAVY 95
Cdd:cd20988  13 GKPVTLKCSMKGEAISNYYINWYRKTQGNTMTFI-----YREGGIYGPGFKDNFRGDIDSSNNLAVLKILEASERDEGSY 87

                        90       100
                ....*....|....*....|....*..
gi 1480722   96 YCAS-------LRPPFAYwGQGTLVTV 115
Cdd:cd20988  88 YCASdtpgggrEYDPLIF-GKGTYLTV 113
IgV_CD8_alpha cd05720
Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; ...
 139-220 4.89e-06

Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; The members here are composed of the immunoglobulin (Ig)-like variable domain of the Cluster of Differentiation (CD) 8 alpha. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. The Ig domain of CD8 alpha binds to antibodies. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409385  Cd Length: 110  Bit Score: 44.40  E-value: 4.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  139 SPSSIYASLGERVTITCKASQDIKSYLGWFQQKPG--KSPKTLIYRANRLVDGVP-----SRFSGSGSGQDYSLTISSLE 211
Cdd:cd05720   4 SPRKRDAQLGQKVELVCEVLNSVPQGCSWLFQPRGsaPQPTFLLYLSSSNKTKWAegldsKRFSGSRSGSSYVLTLKDFR 83


                ....*....
gi 1480722  212 YEDMGIYYC 220
Cdd:cd05720  84 KEDEGYYFC 92
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 2-115 1.13e-05

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta 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. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409503  Cd Length: 112  Bit Score: 43.28  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    2 QVQLQQSGAElmkpGASVKISCK-ATGYTfsNYWIEWVKQRPGHGLEWIGeilpgRGSSKYNEKFKGKATFTSDSSSNTA 80
Cdd:cd07706   4 QAQPDVSVQV----GEEVTLNCRyETSWT--NYYLFWYKQLPSGEMTFLI-----RQDSSEQNAKSGRYSVNFQKAQKSI 72

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 1480722   81 YMQLSSLTSEDSAVYYCA-SLRPPF--AYWGQGTLVTV 115
Cdd:cd07706  73 SLTISALQLEDSAKYFCAlSLPYDTdkLIFGKGTRLTV 110
I-set pfam07679
Immunoglobulin I-set domain;
135-220 1.18e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 42.63  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722    135 VMTQSPSSIYASLGERVTITCKASQDIKSYLGWFqqKPGKSPKTliyranrlvdgvPSRFSGSGSGQDYSLTISSLEYED 214
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWF--KDGQPLRS------------SDRFKVTYEGGTYTLTISNVQPDD 67


                  ....*.
gi 1480722    215 MGIYYC 220
Cdd:pfam07679  68 SGKYTC 73
IgV_CD79b_beta cd16096
Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are ...
 138-220 1.88e-05

Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are composed of the immunoglobulin variable domain (IgV) of the Cluster of Differentiation (CD) 79B (also known as CD79b molecule, immunoglobulin-associated beta (Ig-beta), and B29). The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-beta protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409515  Cd Length: 96  Bit Score: 42.25  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  138 QSPSSIYASLGERVTITCKAsqDIKSYLGWFQQKPGKSPKTLIYRANRLVDgvpsrfsgSGSGQDYSLTISSLEYEDMGI 217
Cdd:cd16096   3 QHPRFAAKKRSSMVKFHCYT--NYSGVMTWFRKKGNQRPQELFPEDGRISQ--------TQNGSVYTLTIQNIQYEDNGI 72


                ...
gi 1480722  218 YYC 220
Cdd:cd16096  73 YFC 75
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 138-238 1.48e-04

Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409497  Cd Length: 116  Bit Score: 40.12  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  138 QSPSSIYASLGERVTITCKASQDIKS---YlgWFQQKPGKSP-------------KTLIYRANrlVDGVPSRFSGSGSGQ 201
Cdd:cd07700   3 QTPGSLLVQTNQTVKMSCEAKTSPKNtriY--WLRQRQAPSKdshfeflaswdpsKGIVYGEG--VDQEKLIILSDSDSS 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 1480722  202 DYSLTISSLEYEDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:cd07700  79 RYILSLMSVKPEDSGTYFCMTVGSPELIFGTGTKLSV 115
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 134-220 2.80e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 39.03  E-value: 2.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  134 IVMTQSPSSIYASLGERVTITCKASQDIKSYLGWFQQkpGKSPKTLIyranrlvdgvpSRFSGSGSGQDysLTISSLEYE 213
Cdd:cd20970   3 ISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTRN--GNLIIEFN-----------TRYIVRENGTT--LTIRNIRRS 67


                ....*..
gi 1480722  214 DMGIYYC 220
Cdd:cd20970  68 DMGIYLC 74
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 138-220 6.70e-04

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 38.15  E-value: 6.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  138 QSPSSIYASLGERVTITCKASQDIKSYLGWFQQKPGKSPKTLIyraNRLVDGVPSRFSGSGSGQD--YSLTISSLEYEDM 215
Cdd:cd05716   2 VGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSEGCQTLV---SSEGVVPGGRISLTDDPDNgvFTVTLNQLRKEDA 78


                ....*
gi 1480722  216 GIYYC 220
Cdd:cd05716  79 GWYWC 83
IgV_SIRP cd16097
Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The ...
 136-239 7.56e-04

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


Pssm-ID: 409516  Cd Length: 111  Bit Score: 37.92  E-value: 7.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  136 MTQSPSSIYASLGERVTITCKASQDIK-SYLGWFQqkpGKSP-KTLIYraNRLVDGVPSRFSGSGSGQ----DYSLTISS 209
Cdd:cd16097   2 VIQPEKSVSVAAGESATLHCTVTSLIPvGPIQWFR---GAGPgRELIY--NQKEGHFPRVTTVSDLTKrnnmDFSIRISN 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1480722  210 LEYEDMGIYYCLKY-----DEFPYTFGGGTKLEIK 239
Cdd:cd16097  77 ITPADAGTYYCVKFrkgspDDVEFKSGAGTELSVR 111
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 35-97 1.26e-03

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 37.43  E-value: 1.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1480722   35 IEWVKQRPGHGLEWIGEILPGRGSSKYNEKFKGKATFTSDSSSNTAYMQLSSLTSEDSAVYYC 97
Cdd:cd20960  36 IEWLLLPSDKVEKVVITYSGDRVYNHYYPALKGRVAFTSNDLSGDASLNISNLKLSDTGTYQC 98
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 151-220 1.70e-03

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 36.15  E-value: 1.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  151 VTITCKASQDIKSYLGWFqqKPGKSPKTLIYRANRLVDGvpsrfsgsgsgqDYSLTISSLEYEDMGIYYC 220
Cdd:cd00096   1 VTLTCSASGNPPPTITWY--KNGKPLPPSSRDSRRSELG------------NGTLTISNVTLEDSGTYTC 56
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 139-238 3.39e-03

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 36.08  E-value: 3.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1480722  139 SPSSIYASLGERVTITCKASQDIKSyLGWFqqkpgkSP---KTLIYRANRLV---DGVPSRfsgsgsgqdysLTISSLEY 212
Cdd:cd04977   6 IPSYAEISVGESKFFLCKVSGDAKN-INWV------SPngeKVLTKHGNLKVvnhGSVLSS-----------LTIYNANI 67

                        90       100
                ....*....|....*....|....*.
gi 1480722  213 EDMGIYYCLKYDEFPYTFGGGTKLEI 238
Cdd:cd04977  68 NDAGIYKCVATNGKGTESEATVKLDI 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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