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Conserved domains on  [gi|1858696887|pdb|6VMS|E]
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Chain E, scFv16

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 ...
 3-119 5.34e-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: 195.61  E-value: 5.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        3 QLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*..
6VMS_E       83 MTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTV 119
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYGYSYFDYWGQGTTVTV 117
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 138-247 1.82e-52

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: 166.03  E-value: 1.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      138 IVMTQATSSVPVTPGESVSISCRSSKSLlhsnGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTIS 217
Cdd:cd04980   1 IVMTQSPASLSVSPGERVTISCKASQSI----SSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTIS 76

                        90       100       110
                ....*....|....*....|....*....|
6VMS_E      218 RLEAEDVGVYYCMQHLEYPLTFGAGTKLEL 247
Cdd:cd04980  77 SVEPEDAAVYYCQQGYTFPYTFGGGTKLEI 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 ...
 3-119 5.34e-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: 195.61  E-value: 5.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        3 QLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*..
6VMS_E       83 MTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTV 119
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYGYSYFDYWGQGTTVTV 117
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 138-247 1.82e-52

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: 166.03  E-value: 1.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      138 IVMTQATSSVPVTPGESVSISCRSSKSLlhsnGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTIS 217
Cdd:cd04980   1 IVMTQSPASLSVSPGERVTISCKASQSI----SSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTIS 76

                        90       100       110
                ....*....|....*....|....*....|
6VMS_E      218 RLEAEDVGVYYCMQHLEYPLTFGAGTKLEL 247
Cdd:cd04980  77 SVEPEDAAVYYCQQGYTFPYTFGGGTKLEI 106
IGv smart00406
Immunoglobulin V-Type;
19-98 2.15e-30

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 108.62  E-value: 2.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E          19 KLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTiYYADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVR 98
Cdd:smart00406   3 TLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSS-YYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
IGv smart00406
Immunoglobulin V-Type;
154-229 1.47e-16

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 72.41  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E         154 SVSISCRSSKSllhSNGNTYLYWFLQRPGQSPQLLIYRMSN----LASGVPDRFSGSG--SGTAFTLTISRLEAEDVGVY 227
Cdd:smart00406   1 SVTLSCKFSGS---TFSSYYVSWVRQPPGKGLEWLGYIGSNgssyYQESYKGRFTISKdtSKNDVSLTISNLRVEDTGTY 77


                   ..
6VMS_E         228 YC 229
Cdd:smart00406  78 YC 79
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 144-245 2.35e-15

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: 70.18  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        144 TSSVPVT--PGESVSISCRSSKSllHSNGNTYLYWFLQRPGQSPQLLIYRMSNLA--SGVPDRFSGSGSGTA--FTLTIS 217
Cdd:pfam07686   1 QTPREVTvaLGGSVTLPCTYSSS--MSEASTSVYWYRQPPGKGPTFLIAYYSNGSeeGVKKGRFSGRGDPSNgdGSLTIQ 78

                          90       100
                  ....*....|....*....|....*...
6VMS_E        218 RLEAEDVGVYYCMQHLEYPLTFGAGTKL 245
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGEGVFGKGTRL 106
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 11-119 2.37e-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: 59.01  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E         11 LVQPGGSRKLSCSASGFAFS-SFGMHWVRQAPEKGLEWVAYISSGSGTIYyadTVKGRFTISRDDPKNTLFLQMTSLRSE 89
Cdd:pfam07686   7 TVALGGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTFLIAYYSNGSEEG---VKKGRFSGRGDPSNGDGSLTIQNLTLS 83

                          90       100       110
                  ....*....|....*....|....*....|
6VMS_E         90 DTAMYYCVrsiyyYGSSPFDFWGQGTTLTV 119
Cdd:pfam07686  84 DSGTYTCA-----VIPSGEGVFGKGTRLTV 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 ...
 3-119 5.34e-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: 195.61  E-value: 5.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        3 QLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQ 82
Cdd:cd04981   1 QLQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIGLIYPGGGDTYYADSFKGRFTITRDTSKSTAYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*..
6VMS_E       83 MTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTV 119
Cdd:cd04981  81 LNSLTSEDTAVYYCARGLGGYGYSYFDYWGQGTTVTV 117
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 138-247 1.82e-52

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: 166.03  E-value: 1.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      138 IVMTQATSSVPVTPGESVSISCRSSKSLlhsnGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTIS 217
Cdd:cd04980   1 IVMTQSPASLSVSPGERVTISCKASQSI----SSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTIS 76

                        90       100       110
                ....*....|....*....|....*....|
6VMS_E      218 RLEAEDVGVYYCMQHLEYPLTFGAGTKLEL 247
Cdd:cd04980  77 SVEPEDAAVYYCQQGYTFPYTFGGGTKLEI 106
IGv smart00406
Immunoglobulin V-Type;
19-98 2.15e-30

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 108.62  E-value: 2.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E          19 KLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTiYYADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVR 98
Cdd:smart00406   3 TLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSS-YYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 140-246 3.13e-29

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: 106.65  E-value: 3.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      140 MTQATSSVPVTPGESVSISCRSSKSllhsNGNTYLYWFLQRPGQSPQLLIYRMSNLAS---GVPDRFSGSGSG-TAFTLT 215
Cdd:cd00099   1 VTQSPRSLSVQEGESVTLSCEVSSS----FSSTYIYWYRQKPGQGPEFLIYLSSSKGKtkgGVPGRFSGSRDGtSSFSLT 76

                        90       100       110
                ....*....|....*....|....*....|....
6VMS_E      216 ISRLEAEDVGVYYCMQHL---EYPLTFGAGTKLE 246
Cdd:cd00099  77 ISNLQPEDSGTYYCAVSEsggTDKLTFGSGTRLT 110
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 139-245 3.46e-29

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: 106.01  E-value: 3.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      139 VMTQAtSSVPVTPGESVSISCRSSKSLLHSNgntYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISR 218
Cdd:cd04984   1 VLTQP-SSLSVSPGETVTITCTGSSGNISGN---YVNWYQQKPGSAPRYLIYEDKHRPSGIPDRFSGSKSGNTASLTISG 76

                        90       100
                ....*....|....*....|....*..
6VMS_E      219 LEAEDVGVYYCMQHLEYPLTFGAGTKL 245
Cdd:cd04984  77 AQTEDEADYYCQVWDSNSYVFGGGTKL 103
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 11-119 1.90e-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: 88.93  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       11 LVQPGGSRKLSCSASGFaFSSFGMHWVRQAPEKGLEWVAYISSGSGTiyYADTVKGRFTISRDDpKNTLFLQMTSLRSED 90
Cdd:cd00099   9 SVQEGESVTLSCEVSSS-FSSTYIYWYRQKPGQGPEFLIYLSSSKGK--TKGGVPGRFSGSRDG-TSSFSLTISNLQPED 84

                        90       100
                ....*....|....*....|....*....
6VMS_E       91 TAMYYCVRSiyYYGSSPFDFWGQGTTLTV 119
Cdd:cd00099  85 SGTYYCAVS--ESGGTDKLTFGSGTRLTV 111
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 141-245 2.51e-19

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: 80.39  E-value: 2.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      141 TQATSSVPVTPGESVSISCRSSKSllhsnGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGS--GSGTAFTLTISR 218
Cdd:cd04983   2 TQSPQSLSVQEGENVTLNCNYSTS-----TFYYLFWYRQYPGQGPQFLIYISSDSGNKKKGRFSATldKSRKSSSLHISA 76

                        90       100       110
                ....*....|....*....|....*....|
6VMS_E      219 LEAEDVGVYYCM---QHLEYPLTFGAGTKL 245
Cdd:cd04983  77 AQLSDSAVYFCAlseSGGTGKLTFGKGTRL 106
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 141-245 1.85e-18

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: 78.09  E-value: 1.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      141 TQATSSVPVTPGESVSISCRssksllHSNGNTYLYWFLQRPGQSPQLLIYRMSNLA---SGVP-DRFSGSG-SGTAFTLT 215
Cdd:cd05899   2 TQSPRYLIKRRGQSVTLRCS------QKSGHDNMYWYRQDPGKGLQLLFYSYGGGLneeGDLPgDRFSASRpSLTRSSLT 75

                        90       100       110
                ....*....|....*....|....*....|...
6VMS_E      216 ISRLEAEDVGVYYC---MQHLEYPLTFGAGTKL 245
Cdd:cd05899  76 IKSAEPEDSAVYLCassLGGGADEAYFGPGTRL 108
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 13-119 7.37e-18

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: 77.02  E-value: 7.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       13 QPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQMTSLRSEDTA 92
Cdd:cd04982  11 EESKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYVSSTSAVRKDSGKTKNKFEARKDVGKSTSTLTITNLEKEDSA 90

                        90       100       110
                ....*....|....*....|....*....|.
6VMS_E       93 MYYC----VRSIYYYgsspfDFWGQGTTLTV 119
Cdd:cd04982  91 TYYCayweSGSGYYI-----KVFGSGTKLIV 116
IGv smart00406
Immunoglobulin V-Type;
154-229 1.47e-16

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 72.41  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E         154 SVSISCRSSKSllhSNGNTYLYWFLQRPGQSPQLLIYRMSN----LASGVPDRFSGSG--SGTAFTLTISRLEAEDVGVY 227
Cdd:smart00406   1 SVTLSCKFSGS---TFSSYYVSWVRQPPGKGLEWLGYIGSNgssyYQESYKGRFTISKdtSKNDVSLTISNLRVEDTGTY 77


                   ..
6VMS_E         228 YC 229
Cdd:smart00406  78 YC 79
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 3-119 5.11e-16

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: 71.82  E-value: 5.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        3 QLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSgtiyyADTVKGRFTISRDDPKNTLFLQ 82
Cdd:cd16095   3 QLEESGGGSHPAGKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSLDHIS-----TKVSEDRITSSREDTNSQIFLQ 77

                        90       100       110
                ....*....|....*....|....*....|....*..
6VMS_E       83 MTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTV 119
Cdd:cd16095  78 IKGLGLRDSGQYHCARRVGYGDDTDKLIFGPGTDVIV 114
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 140-245 5.74e-16

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: 72.01  E-value: 5.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      140 MTQATSSVPVTPGESVSISCRSSkslLHSNGNTYLYWFLQRPGQSPQLLIY-----RMSNLASGVPDRFSGS--GSGTAF 212
Cdd:cd04982   1 LEQPQLSITREESKSVTISCKVS---GIDFSTTYIHWYRQKPGQALERLLYvsstsAVRKDSGKTKNKFEARkdVGKSTS 77

                        90       100       110
                ....*....|....*....|....*....|....*..
6VMS_E      213 TLTISRLEAEDVGVYYC----MQHLEYPLTFGAGTKL 245
Cdd:cd04982  78 TLTITNLEKEDSATYYCayweSGSGYYIKVFGSGTKL 114
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 144-245 2.35e-15

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: 70.18  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        144 TSSVPVT--PGESVSISCRSSKSllHSNGNTYLYWFLQRPGQSPQLLIYRMSNLA--SGVPDRFSGSGSGTA--FTLTIS 217
Cdd:pfam07686   1 QTPREVTvaLGGSVTLPCTYSSS--MSEASTSVYWYRQPPGKGPTFLIAYYSNGSeeGVKKGRFSGRGDPSNgdGSLTIQ 78

                          90       100
                  ....*....|....*....|....*...
6VMS_E        218 RLEAEDVGVYYCMQHLEYPLTFGAGTKL 245
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGEGVFGKGTRL 106
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 145-246 3.49e-14

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: 65.99  E-value: 3.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E         145 SSVPVTPGESVSISCRSSksllhSNGNTYLYWFLQRPgqspQLLIYrmsnlasgvPDRFSGSGSGTAFTLTISRLEAEDV 224
Cdd:smart00410   2 PSVTVKEGESVTLSCEAS-----GSPPPEVTWYKQGG----KLLAE---------SGRFSVSRSGSTSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|..
6VMS_E         225 GVYYCMQHLEYPLTFGaGTKLE 246
Cdd:smart00410  64 GTYTCAATNSSGSASS-GTTLT 84
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 141-245 9.11e-14

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: 66.00  E-value: 9.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      141 TQATSSVPVTPGESVSISCRSSKSllhsNGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGS--GSGTAFTLTISR 218
Cdd:cd07706   3 TQAQPDVSVQVGEEVTLNCRYETS----WTNYYLFWYKQLPSGEMTFLIRQDSSEQNAKSGRYSVNfqKAQKSISLTISA 78

                        90       100       110
                ....*....|....*....|....*....|
6VMS_E      219 LEAEDVGVYYCMQHLEYP---LTFGAGTKL 245
Cdd:cd07706  79 LQLEDSAKYFCALSLPYDtdkLIFGKGTRL 108
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 11-119 4.72e-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: 61.14  E-value: 4.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       11 LVQPGGSRKLSCS-ASGFAFssfgMHWVRQAPEKGLEWVAYiSSGSGTIYYADTVKGRFTISRddPKNTLF-LQMTSLRS 88
Cdd:cd05899   9 IKRRGQSVTLRCSqKSGHDN----MYWYRQDPGKGLQLLFY-SYGGGLNEEGDLPGDRFSASR--PSLTRSsLTIKSAEP 81

                        90       100       110
                ....*....|....*....|....*....|....*.
6VMS_E       89 EDTAMYYCvrsiyyyGSSPFD-----FWGQGTTLTV 119
Cdd:cd05899  82 EDSAVYLC-------ASSLGGgadeaYFGPGTRLTV 110
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 7-119 2.33e-11

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: 58.67  E-value: 2.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E           7 SGGGLVQPGGSRKLSCSASGFafSSFGMHWVRQapekGLEWVAYissgsgtiyyadtvKGRFTISRDdpKNTLFLQMTSL 86
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGS--PPPEVTWYKQ----GGKLLAE--------------SGRFSVSRS--GSTSTLTISNV 58

                           90       100       110
                   ....*....|....*....|....*....|...
6VMS_E          87 RSEDTAMYYCVRSIYYYGSSpfdfwgQGTTLTV 119
Cdd:smart00410  59 TPEDSGTYTCAATNSSGSAS------SGTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 11-119 2.37e-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: 59.01  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E         11 LVQPGGSRKLSCSASGFAFS-SFGMHWVRQAPEKGLEWVAYISSGSGTIYyadTVKGRFTISRDDPKNTLFLQMTSLRSE 89
Cdd:pfam07686   7 TVALGGSVTLPCTYSSSMSEaSTSVYWYRQPPGKGPTFLIAYYSNGSEEG---VKKGRFSGRGDPSNGDGSLTIQNLTLS 83

                          90       100       110
                  ....*....|....*....|....*....|
6VMS_E         90 DTAMYYCVrsiyyYGSSPFDFWGQGTTLTV 119
Cdd:pfam07686  84 DSGTYTCA-----VIPSGEGVFGKGTRLTV 108
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 12-119 1.38e-10

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: 57.09  E-value: 1.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       12 VQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGtiyyaDTVKGRFTISRDdpKNTLFLQMTSLRSEDT 91
Cdd:cd04984  10 VSPGETVTITCTGSSGNISGNYVNWYQQKPGSAPRYLIYEDKHRP-----SGIPDRFSGSKS--GNTASLTISGAQTEDE 82

                        90       100
                ....*....|....*....|....*...
6VMS_E       92 AMYYCvrSIYYYGSSPFdfwGQGTTLTV 119
Cdd:cd04984  83 ADYYC--QVWDSNSYVF---GGGTKLTV 105
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 11-119 5.88e-10

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: 55.53  E-value: 5.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       11 LVQPGGSRKLSCSASGFAfSSFGMHWVRQ----APEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQMTSL 86
Cdd:cd07700   9 LVQTNQTVKMSCEAKTSP-KNTRIYWLRQrqapSKDSHFEFLASWDPSKGIVYGEGVDQEKLIILSDSDSSRYILSLMSV 87

                        90       100       110
                ....*....|....*....|....*....|...
6VMS_E       87 RSEDTAMYYCVrsiyYYGSSPFDFwGQGTTLTV 119
Cdd:cd07700  88 KPEDSGTYFCM----TVGSPELIF-GTGTKLSV 115
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 12-119 1.23e-09

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: 54.58  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       12 VQPGGSRKLSCSASGFAFSSFgmHWVRQAPEKGLEWVAYISSGSGTiyyadTVKGRFTISRDDPKNTLFLQMTSLRSEDT 91
Cdd:cd04983  10 VQEGENVTLNCNYSTSTFYYL--FWYRQYPGQGPQFLIYISSDSGN-----KKKGRFSATLDKSRKSSSLHISAAQLSDS 82

                        90       100
                ....*....|....*....|....*...
6VMS_E       92 AMYYCVRSIYYYGSSPfdFWGQGTTLTV 119
Cdd:cd04983  83 AVYFCALSESGGTGKL--TFGKGTRLTV 108
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 142-245 1.77e-07

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: 48.60  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      142 QATSSVPVTPGESVSISCRSSKSLlhsnGNTYLYWFLQRPGQSP----QLLIYrmSNLASGV-------PDRFS--GSGS 208
Cdd:cd07700   3 QTPGSLLVQTNQTVKMSCEAKTSP----KNTRIYWLRQRQAPSKdshfEFLAS--WDPSKGIvygegvdQEKLIilSDSD 76

                        90       100       110
                ....*....|....*....|....*....|....*..
6VMS_E      209 GTAFTLTISRLEAEDVGVYYCMQHLEYPLTFGAGTKL 245
Cdd:cd07700  77 SSRYILSLMSVKPEDSGTYFCMTVGSPELIFGTGTKL 113
IgV_CD79b_beta cd16096
Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are ...
 167-245 6.27e-07

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: 46.48  E-value: 6.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      167 HSNGNTYLYWFLQRPGQSPQLLIyrmsnLASGvpdRFSGSGSGTAFTLTISRLEAEDVGVYYCMQ---HLEYPLTFGAGT 243
Cdd:cd16096  21 YTNYSGVMTWFRKKGNQRPQELF-----PEDG---RISQTQNGSVYTLTIQNIQYEDNGIYFCQQkcnSTEPDVTDGCGT 92


                ..
6VMS_E      244 KL 245
Cdd:cd16096  93 EL 94
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 2-119 3.87e-06

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: 44.69  E-value: 3.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        2 VQLVESGGGL-VQPGGSRKLSCSASGfAFSSFGMHWVRQAPEKGLEWVayissgsgtIYYADT----VKGRFTISRDDPK 76
Cdd:cd04980   1 IVMTQSPASLsVSPGERVTISCKASQ-SISSNYLAWYQQKPGQAPKLL---------IYYASTlhsgVPSRFSGSGSGTD 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
6VMS_E       77 NTLflQMTSLRSEDTAMYYCVRsiyyYGSSPFDFwGQGTTLTV 119
Cdd:cd04980  71 FTL--TISSVEPEDAAVYYCQQ----GYTFPYTF-GGGTKLEI 106
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 152-230 1.48e-05

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: 42.77  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      152 GESVSISCRSSKSLLHSNgntyLYWFLQRPGqSPQLLIyrmSNLASGVPDRFSGSGSGTA--FTLTISRLEAEDVGVYYC 229
Cdd:cd05716  12 GGSVTIQCPYPPKYASSR----KYWCKWGSE-GCQTLV---SSEGVVPGGRISLTDDPDNgvFTVTLNQLRKEDAGWYWC 83


                .
6VMS_E      230 M 230
Cdd:cd05716  84 G 84
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 146-248 6.19e-05

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: 41.39  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      146 SVPVTPGESVSISCrSSKSllHSNGNTYLYWFLQRPGqSPQLLIYRMSNL-ASGVPDRFSGS--GSGTAFTLTISRLEAE 222
Cdd:cd20988   7 TVTVSVGKPVTLKC-SMKG--EAISNYYINWYRKTQG-NTMTFIYREGGIyGPGFKDNFRGDidSSNNLAVLKILEASER 82

                        90       100       110
                ....*....|....*....|....*....|..
6VMS_E      223 DVGVYYC------MQHLEYPLTFGAGTKLELK 248
Cdd:cd20988  83 DEGSYYCasdtpgGGREYDPLIFGKGTYLTVE 114
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 142-229 1.95e-04

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 40.12  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      142 QATSSVPVTPGESVSISCrssksLLHSNGNTYL---YWFLQRPGQSPQLLIYRMS---NLASGVPDRFSGSGSGTAF--- 212
Cdd:cd05718   4 QVPTEVTGFLGGSVTLPC-----SLTSPGTTKItqvTWMKIGAGSSQNVAVFHPQygpSVPNPYAERVEFLAARLGLrna 78

                        90
                ....*....|....*..
6VMS_E      213 TLTISRLEAEDVGVYYC 229
Cdd:cd05718  79 TLRIRNLRVEDEGNYIC 95
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 139-229 3.19e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.32  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E        139 VMTQATSSVPVTPGESVSISCRSSKsllhsngntylywflqrpGQSPQLLIYRMSNLASGVPDRFSGSGSGTAfTLTISR 218
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATG------------------SPPPTITWYKNGEPISSGSTRSRSLSGSNS-TLTISN 63

                          90
                  ....*....|.
6VMS_E        219 LEAEDVGVYYC 229
Cdd:pfam13927  64 VTRSDAGTYTC 74
IgV_CD8_alpha cd05720
Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; ...
 176-229 4.00e-04

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: 39.01  E-value: 4.00e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
6VMS_E      176 WFLQRPGQSPQL--LIYRMSNLASGVPD-----RFSGSGSGTAFTLTISRLEAEDVGVYYC 229
Cdd:cd05720  32 WLFQPRGSAPQPtfLLYLSSSNKTKWAEgldskRFSGSRSGSSYVLTLKDFRKEDEGYYFC 92
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 29-119 6.65e-04

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: 38.27  E-value: 6.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E       29 FSSFGMHWVRQAPEKGLEWVAYISSgsgtiYYADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYygssPF 108
Cdd:cd07706  27 WTNYYLFWYKQLPSGEMTFLIRQDS-----SEQNAKSGRYSVNFQKAQKSISLTISALQLEDSAKYFCALSLPY----DT 97

                        90
                ....*....|...
6VMS_E      109 D--FWGQGTTLTV 119
Cdd:cd07706  98 DklIFGKGTRLTV 110
IgV_H_TCR_mu cd16095
T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the ...
 152-243 1.69e-03

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: 37.16  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      152 GESVSISCRSSKSLLHSngnTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGS--GSGTAFTLTISRLEAEDVGVYYC 229
Cdd:cd16095  15 GKTLSLKCQTSGFQFNT---SQLSWYLWVPGHAPLWLTSLDHISTKVSEDRITSSreDTNSQIFLQIKGLGLRDSGQYHC 91

                        90
                ....*....|....*....
6VMS_E      230 MQHLEY-----PLTFGAGT 243
Cdd:cd16095  92 ARRVGYgddtdKLIFGPGT 110
IgV_CTLA-4 cd05721
Immunoglobulin Variable (IgV) domain of cytotoxic T lymphocyte-associated antigen 4 (CTLA-4); ...
 190-245 3.29e-03

Immunoglobulin Variable (IgV) domain of cytotoxic T lymphocyte-associated antigen 4 (CTLA-4); The members here are composed of the variable(v)-type immunoglobulin (Ig) domain found in cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). CTLA-4 is involved in the regulation of T cell response, acting as an inhibitor of intracellular signaling. CTLA-4 is similar to CD28, a T cell co-receptor protein that recognizes the B7 proteins (CD80 and CD86). CD28 binding of the B7 proteins occurs after the presentation of antigen to the T cell receptor (TCR) via the peptide-MHC complex on the surface of an antigen presenting cell (APC). CTLA-4 also binds the B7 molecules with a higher affinity than does CD28. The B7/CTLA-4 interaction generates inhibitory signals down-regulating the response, and may prevent T cell activation by weak TCR signals. CD28 and CTLA-4 then elicit opposing signals in the regulation of T cell responsiveness and homeostasis. T cell activation leads to increased CTLA-4 gene expression and trafficking of CTLA-4 protein to the cell surface. CTLA-4 is not detected on the T-cell surface until 24 hours after activation. Covalent dimerization of CTLA-4 has been shown to be required for its high binding avidity, although each CTLA-4 monomer contains a binding site for CD80 and CD86.


Pssm-ID: 409386  Cd Length: 115  Bit Score: 36.52  E-value: 3.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
6VMS_E      190 YRMSNLASGVPDRF-SGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYP----LTFGAGTKL 245
Cdd:cd05721  51 YTMGNELTFLDDSIcTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPppyyVGMGNGTQI 111
CD19_protodomain_3_4 cd23998
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 3 ...
 149-229 8.21e-03

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 3 and 4; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding. This group contains the protodomains 3 and 4 of the CD19 double Ig domain.


Pssm-ID: 467825  Cd Length: 95  Bit Score: 34.77  E-value: 8.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6VMS_E      149 VTPGESVSISCRSSKSllhSNGNTYLYWFLQRPGQSPQLLIYRmsNLASGVPDR----FSGSGSGTafTLTISRLEAEDV 224
Cdd:cd23998   5 VAPGSTLWLSCGVPPD---SGTRGPISWTHVHPKPSNTSLLSL--ELKEDRPARekwvLGTLRGGA--LLLLPRATAQDA 77


                ....*
6VMS_E      225 GVYYC 229
Cdd:cd23998  78 GIYHC 82
IgC1_MHC-like_ZAG cd21010
Immunoglobulin domain of Zn-alpha2-glycoprotein (ZAG); member of the C1-set of Ig superfamily ...
 12-57 8.38e-03

Immunoglobulin domain of Zn-alpha2-glycoprotein (ZAG); member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin domain of Zn-alpha2-glycoprotein (ZAG). ZAG is a soluble protein that is present in serum and other body fluids. ZAG stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. The 2.8 angstrom crystal structure of ZAG resembles a class I major histocompatibility complex (MHC) heavy chain, but ZAG does not bind the class I light chain beta-2-microglobulin. The ZAG structure includes a large groove analogous to class I MHC peptide binding grooves. Instead of a peptide, the ZAG groove contains a nonpeptidic compound that may be implicated in lipid catabolism under normal or pathological conditions. 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 beta-2-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: 409601  Cd Length: 93  Bit Score: 34.99  E-value: 8.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
6VMS_E       12 VQPGGSRKLSCSASGFAFSSFGMHWVR----QAPEkglEWVAYISSGSGT 57
Cdd:cd21010  13 VAPGKNRTLKCLAYDFYPRGISLHWTRagkvQESE---SGGDVLPSGNGT 59
 
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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