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Conserved domains on  [gi|936976299|ref|NP_001301026|]
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programmed cell death protein 1 precursor [Canis lupus familiaris]

Protein Classification

IgV_PD1 domain-containing protein( domain architecture ID 11610716)

IgV_PD1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_PD1 cd16088
Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are ...
 34-145 4.58e-76

Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are composed of the immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1; also known as CD279/cluster of differentiation 279). PD1 is a cell surface receptor that is expressed on T cells and pro-B cells. The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. Activation of CD4+ T cells, CD8+ T cells, NKT cells, B cells, and monocytes induces PD-1 expression, immediately after which it binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274/cluster of differentiation 274) and PD-L2, also known as B7-DC. PD-1 plays an important role in down regulating the immune system by preventing the activation of T-cells, reducing autoimmunity and promoting self-tolerance. The inhibitory effect of PD-1 is accomplished by promoting apoptosis in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells. A class of drugs that target PD-1, known as the PD-1 inhibitors, activate the immune system to attack tumors and treat cancer. Comparisons between the mouse PD-1 (mPD-1) and human PD-1 (hPD-1) reveals that unlike the mPD-1 which has a conventional IgSF V-set domain, hPD-1 lacks a C" strand, and instead the C' and D strands are connected by a long and flexible loop. In addition, the BC loop is not stabilized by disulfide bonding to the F strand of the ligand binding beta sheet. These differences result in different binding affinities of human and mouse PD-1 for their ligands.


:

Pssm-ID: 409509  Cd Length: 112  Bit Score: 227.39  E-value: 4.58e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  34 PLTFSPAQLTVQEGENATFTCSLADIPDSFVLNWYRLSPRNQTDKLAAFQEDRIEPGRDRRFRVTRLPNGRDFHMSIVAA 113
Cdd:cd16088    1 PPTFSPALLVVTEGANATFTCSFSNTSESFVLNWYRLSPSNQTDKLAAFPEDRSQPGQDWRFRVTQLPNGRDFHMSVVRA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 936976299 114 RLNDSGIYLCGAIYLPPNTQINESPRAELSVT 145
Cdd:cd16088   81 RRNDSGTYLCGAISLAPKAQIKESPRAELRVT 112
 
Name Accession Description Interval E-value
IgV_PD1 cd16088
Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are ...
 34-145 4.58e-76

Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are composed of the immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1; also known as CD279/cluster of differentiation 279). PD1 is a cell surface receptor that is expressed on T cells and pro-B cells. The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. Activation of CD4+ T cells, CD8+ T cells, NKT cells, B cells, and monocytes induces PD-1 expression, immediately after which it binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274/cluster of differentiation 274) and PD-L2, also known as B7-DC. PD-1 plays an important role in down regulating the immune system by preventing the activation of T-cells, reducing autoimmunity and promoting self-tolerance. The inhibitory effect of PD-1 is accomplished by promoting apoptosis in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells. A class of drugs that target PD-1, known as the PD-1 inhibitors, activate the immune system to attack tumors and treat cancer. Comparisons between the mouse PD-1 (mPD-1) and human PD-1 (hPD-1) reveals that unlike the mPD-1 which has a conventional IgSF V-set domain, hPD-1 lacks a C" strand, and instead the C' and D strands are connected by a long and flexible loop. In addition, the BC loop is not stabilized by disulfide bonding to the F strand of the ligand binding beta sheet. These differences result in different binding affinities of human and mouse PD-1 for their ligands.


Pssm-ID: 409509  Cd Length: 112  Bit Score: 227.39  E-value: 4.58e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  34 PLTFSPAQLTVQEGENATFTCSLADIPDSFVLNWYRLSPRNQTDKLAAFQEDRIEPGRDRRFRVTRLPNGRDFHMSIVAA 113
Cdd:cd16088    1 PPTFSPALLVVTEGANATFTCSFSNTSESFVLNWYRLSPSNQTDKLAAFPEDRSQPGQDWRFRVTQLPNGRDFHMSVVRA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 936976299 114 RLNDSGIYLCGAIYLPPNTQINESPRAELSVT 145
Cdd:cd16088   81 RRNDSGTYLCGAISLAPKAQIKESPRAELRVT 112
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 38-145 2.14e-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: 70.56  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299   38 SPAQLTVQEGENATFTCSLAD--IPDSFVLNWYRLSPRNQTDKL-AAFQEDRIEPGRDRRFRVTRLPNGRDFHMSIVAAR 114
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSsmSEASTSVYWYRQPPGKGPTFLiAYYSNGSEEGVKKGRFSGRGDPSNGDGSLTIQNLT 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 936976299  115 LNDSGIYLCGAIylpPNTQINESPRAELSVT 145
Cdd:pfam07686  82 LSDSGTYTCAVI---PSGEGVFGKGTRLTVL 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 39-144 9.00e-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: 57.13  E-value: 9.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299    39 PAQLTVQEGENATFTCSLADIPDSFVlNWYRlsprnqtdklaafqEDRIEPGRDRRFRVTRlpNGRDFHMSIVAARLNDS 118
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEV-TWYK--------------QGGKLLAESGRFSVSR--SGSTSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|....*.
gi 936976299   119 GIYLCGAIylppNTQINESPRAELSV 144
Cdd:smart00410  64 GTYTCAAT----NSSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
IgV_PD1 cd16088
Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are ...
 34-145 4.58e-76

Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are composed of the immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1; also known as CD279/cluster of differentiation 279). PD1 is a cell surface receptor that is expressed on T cells and pro-B cells. The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. Activation of CD4+ T cells, CD8+ T cells, NKT cells, B cells, and monocytes induces PD-1 expression, immediately after which it binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274/cluster of differentiation 274) and PD-L2, also known as B7-DC. PD-1 plays an important role in down regulating the immune system by preventing the activation of T-cells, reducing autoimmunity and promoting self-tolerance. The inhibitory effect of PD-1 is accomplished by promoting apoptosis in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells. A class of drugs that target PD-1, known as the PD-1 inhibitors, activate the immune system to attack tumors and treat cancer. Comparisons between the mouse PD-1 (mPD-1) and human PD-1 (hPD-1) reveals that unlike the mPD-1 which has a conventional IgSF V-set domain, hPD-1 lacks a C" strand, and instead the C' and D strands are connected by a long and flexible loop. In addition, the BC loop is not stabilized by disulfide bonding to the F strand of the ligand binding beta sheet. These differences result in different binding affinities of human and mouse PD-1 for their ligands.


Pssm-ID: 409509  Cd Length: 112  Bit Score: 227.39  E-value: 4.58e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  34 PLTFSPAQLTVQEGENATFTCSLADIPDSFVLNWYRLSPRNQTDKLAAFQEDRIEPGRDRRFRVTRLPNGRDFHMSIVAA 113
Cdd:cd16088    1 PPTFSPALLVVTEGANATFTCSFSNTSESFVLNWYRLSPSNQTDKLAAFPEDRSQPGQDWRFRVTQLPNGRDFHMSVVRA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 936976299 114 RLNDSGIYLCGAIYLPPNTQINESPRAELSVT 145
Cdd:cd16088   81 RRNDSGTYLCGAISLAPKAQIKESPRAELRVT 112
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 38-145 2.14e-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: 70.56  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299   38 SPAQLTVQEGENATFTCSLAD--IPDSFVLNWYRLSPRNQTDKL-AAFQEDRIEPGRDRRFRVTRLPNGRDFHMSIVAAR 114
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSSsmSEASTSVYWYRQPPGKGPTFLiAYYSNGSEEGVKKGRFSGRGDPSNGDGSLTIQNLT 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 936976299  115 LNDSGIYLCGAIylpPNTQINESPRAELSVT 145
Cdd:pfam07686  82 LSDSGTYTCAVI---PSGEGVFGKGTRLTVL 109
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 35-123 8.96e-13

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: 63.51  E-value: 8.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  35 LTFSPAQLTVQEGENATFTCSLADIPDSFVLNWYRLSPrNQTDKLAAFQE---DRIEPGRDRRFRVTRlPNGRDFHMSIV 111
Cdd:cd00099    1 VTQSPRSLSVQEGESVTLSCEVSSSFSSTYIYWYRQKP-GQGPEFLIYLSsskGKTKGGVPGRFSGSR-DGTSSFSLTIS 78

                         90
                 ....*....|..
gi 936976299 112 AARLNDSGIYLC 123
Cdd:cd00099   79 NLQPEDSGTYYC 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 39-144 9.00e-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: 57.13  E-value: 9.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299    39 PAQLTVQEGENATFTCSLADIPDSFVlNWYRlsprnqtdklaafqEDRIEPGRDRRFRVTRlpNGRDFHMSIVAARLNDS 118
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEV-TWYK--------------QGGKLLAESGRFSVSR--SGSTSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|....*.
gi 936976299   119 GIYLCGAIylppNTQINESPRAELSV 144
Cdd:smart00410  64 GTYTCAAT----NSSGSASSGTTLTV 85
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 38-123 2.07e-08

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: 51.12  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  38 SPAQLTVQEGENATFTCSLADIPDSFVLnWYRLSPrNQTDKLAAFQEDRIEPGRDRRFRVTRLPNGRDFHMSIVAARLND 117
Cdd:cd04983    4 SPQSLSVQEGENVTLNCNYSTSTFYYLF-WYRQYP-GQGPQFLIYISSDSGNKKKGRFSATLDKSRKSSSLHISAAQLSD 81


                 ....*.
gi 936976299 118 SGIYLC 123
Cdd:cd04983   82 SAVYFC 87
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 35-132 3.18e-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: 47.77  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  35 LTFSPAQLTVQEGENATFTCSLADIPDSFVLNWYRLSPrNQTDKLAAFQEDRIEPGRDRRFRVTrlPNGRDFHMSIVAAR 114
Cdd:cd04980    3 MTQSPASLSVSPGERVTISCKASQSISSNYLAWYQQKP-GQAPKLLIYYASTLHSGVPSRFSGS--GSGTDFTLTISSVE 79

                         90
                 ....*....|....*...
gi 936976299 115 LNDSGIYLCGAIYLPPNT 132
Cdd:cd04980   80 PEDAAVYYCQQGYTFPYT 97
IGv smart00406
Immunoglobulin V-Type;
49-123 3.72e-06

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 44.30  E-value: 3.72e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 936976299    49 NATFTCSLADIPDS-FVLNWYRLSPRNQTDKLAAFQEDR---IEPGRDRRFRVTRLPNGRDFHMSIVAARLNDSGIYLC 123
Cdd:smart00406   1 SVTLSCKFSGSTFSsYYVSWVRQPPGKGLEWLGYIGSNGssyYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 38-123 2.07e-05

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.18  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299   38 SPAQLTVQEGENATFTCSLADIPDSFVLNWYRLSPRNQTdklaafqEDRIEPGRDRRFRVTRLpngrdfhmsIVAARLND 117
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIE-------SLKVKHDNGRTTQSSLL---------ISNVTKED 65


                  ....*.
gi 936976299  118 SGIYLC 123
Cdd:pfam00047  66 AGTYTC 71
IgV_1_Necl_like cd05717
First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the ...
 42-132 3.74e-05

First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells.


Pssm-ID: 409382  Cd Length: 94  Bit Score: 41.73  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  42 LTVQEGENATFTCSLADIPDSfVLNWyrLSPRNQTdklAAFQEDRiePGRDRRFRVTRLpNGRDFHMSIVAARLNDSGIY 121
Cdd:cd05717    6 VTVVEGETLTLKCQVSLRDDS-SLQW--LNPNGQT---IYFNDKR--ALRDSRYQLLNH-SASELSISVSNVTLSDEGVY 76

                         90
                 ....*....|.
gi 936976299 122 LCGAIYLPPNT 132
Cdd:cd05717   77 TCLHYTDPVST 87
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 38-125 3.25e-04

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: 39.57  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  38 SPAQLTVQEGENATFTCSLADipDSFVLNWYRLSPRNQTDKLAAFQED---RIEPGRDRRFRVTRlPNGRDFHMSIVAAR 114
Cdd:cd05899    4 SPRYLIKRRGQSVTLRCSQKS--GHDNMYWYRQDPGKGLQLLFYSYGGglnEEGDLPGDRFSASR-PSLTRSSLTIKSAE 80

                         90
                 ....*....|.
gi 936976299 115 LNDSGIYLCGA 125
Cdd:cd05899   81 PEDSAVYLCAS 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 35-125 7.63e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 7.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299   35 LTFSPAQLTVQEGENATFTCSLADIPDSFVLnWYRlsprnqtdklaafqEDRIEPGRDRRFRVTRLPNGRdfhMSIVAAR 114
Cdd:pfam13927   4 ITVSPSSVTVREGETVTLTCEATGSPPPTIT-WYK--------------NGEPISSGSTRSRSLSGSNST---LTISNVT 65

                          90
                  ....*....|.
gi 936976299  115 LNDSGIYLCGA 125
Cdd:pfam13927  66 RSDAGTYTCVA 76
IgV_1_Necl-3 cd07701
First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3; member of the ...
 34-132 9.07e-04

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-3; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-3, Necl-3 (also known as cell adhesion molecule 2 (CADM2), SynCAM2, IGSF4D). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region, belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-3 accumulates in central and peripheral nervous system tissue, and has been shown to selectively interact with oligodendrocytes.


Pssm-ID: 409498  Cd Length: 96  Bit Score: 37.76  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  34 PLTfspAQLTVQEGENATFTCSLaDIPDSFVLNWYrlSPRNQT---DKLAAFQEDRIEPGRdrrfrvtrlPNGRDFHMSI 110
Cdd:cd07701    2 PLT---QNVTVVEGGTANLTCRV-DQNDNTSLQWS--NPAQQTlyfDDKKALRDNRIELVR---------ASWHELSISI 66

                         90       100
                 ....*....|....*....|..
gi 936976299 111 VAARLNDSGIYLCGAIYLPPNT 132
Cdd:cd07701   67 SDVSLSDEGQYTCSLFTMPVKT 88
I-set pfam07679
Immunoglobulin I-set domain;
39-125 1.15e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 37.24  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299   39 PAQLTVQEGENATFTCSLADIPDsFVLNWYRlsprnqtdklaafqeDRIEPGRDRRFRVTRlpNGRDFHMSIVAARLNDS 118
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPD-PEVSWFK---------------DGQPLRSSDRFKVTY--EGGTYTLTISNVQPDDS 68


                  ....*..
gi 936976299  119 GIYLCGA 125
Cdd:pfam07679  69 GKYTCVA 75
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 35-123 1.49e-03

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: 37.73  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  35 LTFSPAQLTVQEGENATFTCSLADIP-DSFVLNWYRLSP------------RNQTDKLAAFQEDRIEPGRDRRFRVTRLp 101
Cdd:cd04982    1 LEQPQLSITREESKSVTISCKVSGIDfSTTYIHWYRQKPgqalerllyvssTSAVRKDSGKTKNKFEARKDVGKSTSTL- 79

                         90       100
                 ....*....|....*....|..
gi 936976299 102 ngrdfhmSIVAARLNDSGIYLC 123
Cdd:cd04982   80 -------TITNLEKEDSATYYC 94
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 41-123 1.97e-03

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 36.94  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  41 QLTVQEGENATFTCSLADIPDSFVLNWYRLSPRNQTDkLAAFQE---DRIEPGRDRRFRVTRLPNGRDFhMSIVAARLND 117
Cdd:cd05846    7 DTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPEN-IVTYSKkygVKIQPSYVRRISFTSSGLNSTS-ITIWNVTLED 84


                 ....*.
gi 936976299 118 SGIYLC 123
Cdd:cd05846   85 EGCYKC 90
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 37-123 2.45e-03

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 37.02  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  37 FSPAQLTVQEGENATFTC---SLADIPDSFVLNWyRLSPRNQTDKLAAFQEDRIEP--GRDRRF--RVTRL--PNGRDFH 107
Cdd:cd05715    4 YTPRELNVLNGSDVRLTCtftSCYTVGDAFSVTW-TYQPEGGNTTESMFHYSKGKPyiLKVGRFkdRVSWAgnPSKKDAS 82

                         90
                 ....*....|....*.
gi 936976299 108 MSIVAARLNDSGIYLC 123
Cdd:cd05715   83 IVISNLQFSDNGTYTC 98
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 35-125 3.50e-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: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 936976299  35 LTFSPAQLTVQEGENATFTCSLADIPDSfvLNWYrlSPrnqtdklaafQEDRIEPGRDRRFRVTRlpNGRDFHMSIVAAR 114
Cdd:cd04977    3 VKIIPSYAEISVGESKFFLCKVSGDAKN--INWV--SP----------NGEKVLTKHGNLKVVNH--GSVLSSLTIYNAN 66

                         90
                 ....*....|.
gi 936976299 115 LNDSGIYLCGA 125
Cdd:cd04977   67 INDAGIYKCVA 77
 
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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