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Conserved domains on  [gi|1622897446|ref|XP_028695568|]
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poliovirus receptor homolog [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 25-137 7.73e-59

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


The actual alignment was detected with superfamily member cd20989:

Pssm-ID: 472250  Cd Length: 112  Bit Score: 187.40  E-value: 7.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  25 IVVQAPTQVPGFLGDSVTLPCYLQVPGMEeTHVSQLTWSRHGESGSMAIFHPTQGPKYSEPKRLEFVATRLGTELRDASL 104
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMV-THVSQVTWQRHDEHGSVAVFHPKQGPSFPESERLSFVAARLGAELRNASL 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622897446 105 RMFGLRVEDEGSYTCVFFIFPQGKRSVDIWLRV 137
Cdd:cd20989    80 AMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 240-325 2.12e-51

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


:

Pssm-ID: 409524  Cd Length: 86  Bit Score: 167.36  E-value: 2.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 240 PEVSFSGYDNNWYLSQNEATLTCDARSNPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTFICNVTNALGARQA 319
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                  ....*.
gi 1622897446 320 ELTVQV 325
Cdd:cd20930    81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 141-237 4.71e-51

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


:

Pssm-ID: 409500  Cd Length: 97  Bit Score: 166.81  E-value: 4.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 141 PQNTAEVQKVQLTGKPVPVARCVSTGGRPPAHITWHSDLGGMPNTSQAPGFLSGTVTVTSLWILVPSSQVDGKSVTCKVE 220
Cdd:cd07703     1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                          90
                  ....*....|....*..
gi 1622897446 221 HEGFEKPQLLTVNLTVY 237
Cdd:cd07703    81 HETLEEPQLLPVTLSVR 97
 
Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 25-137 7.73e-59

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 187.40  E-value: 7.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  25 IVVQAPTQVPGFLGDSVTLPCYLQVPGMEeTHVSQLTWSRHGESGSMAIFHPTQGPKYSEPKRLEFVATRLGTELRDASL 104
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMV-THVSQVTWQRHDEHGSVAVFHPKQGPSFPESERLSFVAARLGAELRNASL 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622897446 105 RMFGLRVEDEGSYTCVFFIFPQGKRSVDIWLRV 137
Cdd:cd20989    80 AMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 240-325 2.12e-51

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 167.36  E-value: 2.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 240 PEVSFSGYDNNWYLSQNEATLTCDARSNPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTFICNVTNALGARQA 319
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                  ....*.
gi 1622897446 320 ELTVQV 325
Cdd:cd20930    81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 141-237 4.71e-51

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409500  Cd Length: 97  Bit Score: 166.81  E-value: 4.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 141 PQNTAEVQKVQLTGKPVPVARCVSTGGRPPAHITWHSDLGGMPNTSQAPGFLSGTVTVTSLWILVPSSQVDGKSVTCKVE 220
Cdd:cd07703     1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                          90
                  ....*....|....*..
gi 1622897446 221 HEGFEKPQLLTVNLTVY 237
Cdd:cd07703    81 HETLEEPQLLPVTLSVR 97
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 143-228 1.68e-23

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 93.64  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 143 NTAEVQKVQLTGK-PVPVARCVSTGGRPPAHITWHSDLGGM--PNTSQAPGFLSGTVTVTSLWILVPSSQVDGKSVTCKV 219
Cdd:pfam08205   1 PTIEPPASLLEGEgPEVVATCSSAGGKPAPRITWYLDGKPLeaAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQV 80


                  ....*....
gi 1622897446 220 EHEGFEKPQ 228
Cdd:pfam08205  81 SYGALRGSI 89
IGv smart00406
Immunoglobulin V-Type;
40-121 1.16e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 51.61  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446   40 SVTLPCYLQVPGMEETHVSqltWSRH--GESGSMAIFHPTQGPKYSEPK---RLEFVATrlgTELRDASLRMFGLRVEDE 114
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVS---WVRQppGKGLEWLGYIGSNGSSYYQESykgRFTISKD---TSKNDVSLTISNLRVEDT 74


                   ....*..
gi 1622897446  115 GSYTCVF 121
Cdd:smart00406  75 GTYYCAV 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 37-138 3.14e-08

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: 51.30  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  37 LGDSVTLPCylQVPGMEETHVSQLTWSRHGESGS----MAIFHPTQGPkYSEPKRLEFvatRLGTELRDASLRMFGLRVE 112
Cdd:pfam07686  10 LGGSVTLPC--TYSSSMSEASTSVYWYRQPPGKGptflIAYYSNGSEE-GVKKGRFSG---RGDPSNGDGSLTIQNLTLS 83

                          90       100
                  ....*....|....*....|....*.
gi 1622897446 113 DEGSYTCVFFIFPQGKRSVDIWLRVL 138
Cdd:pfam07686  84 DSGTYTCAVIPSGEGVFGKGTRLTVL 109
 
Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 25-137 7.73e-59

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 187.40  E-value: 7.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  25 IVVQAPTQVPGFLGDSVTLPCYLQVPGMEeTHVSQLTWSRHGESGSMAIFHPTQGPKYSEPKRLEFVATRLGTELRDASL 104
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMV-THVSQVTWQRHDEHGSVAVFHPKQGPSFPESERLSFVAARLGAELRNASL 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622897446 105 RMFGLRVEDEGSYTCVFFIFPQGKRSVDIWLRV 137
Cdd:cd20989    80 AMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 240-325 2.12e-51

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 167.36  E-value: 2.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 240 PEVSFSGYDNNWYLSQNEATLTCDARSNPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTFICNVTNALGARQA 319
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                  ....*.
gi 1622897446 320 ELTVQV 325
Cdd:cd20930    81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 141-237 4.71e-51

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409500  Cd Length: 97  Bit Score: 166.81  E-value: 4.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 141 PQNTAEVQKVQLTGKPVPVARCVSTGGRPPAHITWHSDLGGMPNTSQAPGFLSGTVTVTSLWILVPSSQVDGKSVTCKVE 220
Cdd:cd07703     1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                          90
                  ....*....|....*..
gi 1622897446 221 HEGFEKPQLLTVNLTVY 237
Cdd:cd07703    81 HETLEEPQLLPVTLSVR 97
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 25-137 2.06e-43

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: 147.59  E-value: 2.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  25 IVVQAPTQVPGFLGDSVTLPCYLQVPGMeeTHVSQLTWSRHG--ESGSMAIFHPTQGPKYSEP--KRLEFVATRLGteLR 100
Cdd:cd05718     1 QRVQVPTEVTGFLGGSVTLPCSLTSPGT--TKITQVTWMKIGagSSQNVAVFHPQYGPSVPNPyaERVEFLAARLG--LR 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622897446 101 DASLRMFGLRVEDEGSYTCVFFIFPQGKRSVDIWLRV 137
Cdd:cd05718    77 NATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 141-236 3.76e-43

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. 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), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while 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" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 146.10  E-value: 3.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 141 PQNTAEVQKVQL-TGKPVPVARCVSTGGRPPAHITWHSDLGGMPNTSQAPGFlSGTVTVTSLWILVPSSQVDGKSVTCKV 219
Cdd:cd05719     1 PTNSLEGGPALLiGGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGS-NGTVTVTSRYRLVPSREADGQPLTCVV 79

                          90
                  ....*....|....*..
gi 1622897446 220 EHEGFEKPQLLTVNLTV 236
Cdd:cd05719    80 EHPSLEKDQRISVTLNV 96
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 143-228 1.68e-23

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 93.64  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 143 NTAEVQKVQLTGK-PVPVARCVSTGGRPPAHITWHSDLGGM--PNTSQAPGFLSGTVTVTSLWILVPSSQVDGKSVTCKV 219
Cdd:pfam08205   1 PTIEPPASLLEGEgPEVVATCSSAGGKPAPRITWYLDGKPLeaAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQV 80


                  ....*....
gi 1622897446 220 EHEGFEKPQ 228
Cdd:pfam08205  81 SYGALRGSI 89
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 159-236 8.99e-14

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 66.77  E-value: 8.99e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897446 159 VARCVSTGGRPPAHITWHSDLGGMPNTSQApgFLSGTVTVTSLWILVPSSQVDGKSVTCKVEHEGFEKPQLLTVNLTV 236
Cdd:cd07704    21 AASCTAETGKPAASVTWETDLGGMESSRTF--EHNRTATVTSEYHLVPTRFANGRPLTCVVSHPALQQDIRITHILDV 96
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 26-138 5.87e-12

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 62.29  E-value: 5.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  26 VVQAPTQVPGFLGDSVTLPCYLQVPgMEETHVSQLTWSR--HGESGSMAIFHPTQG----PKYSEpkRLEFvatrLGTEL 99
Cdd:cd05886     2 TVQVNDSMSGFIGTDVVLHCSFANP-LPSVKITQVTWQKstNGSKQNVAIYNPSMGvsvlPPYRE--RVTF----LNPSF 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622897446 100 RDASLRMFGLRVEDEGSYTCVFFIFPQGKRSVDIWLRVL 138
Cdd:cd05886    75 TDGTIRLSRLELEDEGVYICEFATFPTGNRESQLNLTVM 113
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 144-232 1.44e-10

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other strands by G, F, C, and C'.


Pssm-ID: 409354  Cd Length: 95  Bit Score: 57.47  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 144 TAEVQKVQLTGKPVPVARCVSTGGRPP-AHITWHSD----LGGMPNTSQAPGFlSGTVTVTSLWILVPSSQVDGKSVTCK 218
Cdd:cd00098     3 TLLPPSPEEKGGGKVTLVCLVSGFYPKdITVTWLKNgvplTSGVSTSSPVEPN-DGTYSVTSSLTVPPSDWDEGATYTCV 81

                          90
                  ....*....|....
gi 1622897446 219 VEHEGFEKPQLLTV 232
Cdd:cd00098    82 VTHESLKSPLSKTW 95
IgC1_2_Nectin-1_like cd05890
Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig ...
 157-234 6.62e-09

Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1, or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 143298  Cd Length: 98  Bit Score: 53.07  E-value: 6.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622897446 157 VPVARCVSTGGRPPAHITWHSDLGGMPnTSQAPGFLSGTVTVTSLWILVPSSQVDGKSVTCKVEHEGFEKPQLLTVNL 234
Cdd:cd05890    22 VLVATCTSANGKPPSVVSWDTRLKGEA-EFQEIRNPNGTVTVISRYRLVPSREAHQQSLACIVNYHMDRFTDSLTLNV 98
IGv smart00406
Immunoglobulin V-Type;
40-121 1.16e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 51.61  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446   40 SVTLPCYLQVPGMEETHVSqltWSRH--GESGSMAIFHPTQGPKYSEPK---RLEFVATrlgTELRDASLRMFGLRVEDE 114
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVS---WVRQppGKGLEWLGYIGSNGSSYYQESykgRFTISKD---TSKNDVSLTISNLRVEDT 74


                   ....*..
gi 1622897446  115 GSYTCVF 121
Cdd:smart00406  75 GTYYCAV 81
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 37-130 2.43e-08

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: 51.58  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  37 LGDSVTLPCYLQVPgMEethVSQLTWSRHGESGS--MAIFHPTQGPKYSEPKRLEFVATRLGteLRDASLRMFGLRVEDE 114
Cdd:cd05846    12 LGGNATLSCNLTLP-EE---VLQVTWQKIKASSPenIVTYSKKYGVKIQPSYVRRISFTSSG--LNSTSITIWNVTLEDE 85

                          90
                  ....*....|....*.
gi 1622897446 115 GSYTCVFFIFPQGKRS 130
Cdd:cd05846    86 GCYKCLFNTFPDGIKS 101
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 37-138 3.14e-08

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: 51.30  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  37 LGDSVTLPCylQVPGMEETHVSQLTWSRHGESGS----MAIFHPTQGPkYSEPKRLEFvatRLGTELRDASLRMFGLRVE 112
Cdd:pfam07686  10 LGGSVTLPC--TYSSSMSEASTSVYWYRQPPGKGptflIAYYSNGSEE-GVKKGRFSG---RGDPSNGDGSLTIQNLTLS 83

                          90       100
                  ....*....|....*....|....*.
gi 1622897446 113 DEGSYTCVFFIFPQGKRSVDIWLRVL 138
Cdd:pfam07686  84 DSGTYTCAVIPSGEGVFGKGTRLTVL 109
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 59-133 3.69e-06

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.


Pssm-ID: 409472  Cd Length: 111  Bit Score: 45.62  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  59 QLTWSRH-GESGSMAIFHPTQG----PKYSEpkRLEFVATRLGTelRDASLRMFGLRVEDEGSYTCVFFIFPQGKRSVDI 133
Cdd:cd05889    31 QVEWTKIgGQKDNIAVYHPTHGmhirKPYAG--RVYFLNSTMAS--NNMSLSFRNASEDDVGYYSCSLYTYPQGSWEKVI 106
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 37-138 5.48e-06

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 44.89  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  37 LGDSVTLPCYLQVPGMEEthVSQLTWSRHGESG---SMAIFHPTQG----PKYSepKRLEFVATrlgTELRDASLRMFGL 109
Cdd:cd05888     7 LGQDAKLPCFYRGDSGEQ--VGQVAWARVDAGEgaqEIALLHSKYGlhvfPAYE--GRVEQPPP---PRPADGSVLLRNA 79

                          90       100
                  ....*....|....*....|....*....
gi 1622897446 110 RVEDEGSYTCVFFIFPQGKRSVDIWLRVL 138
Cdd:cd05888    80 VQADEGEYECRVSTFPAGNFQAELRLRVL 108
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 23-138 6.27e-06

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 44.93  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  23 GDIVVqaPTQVPGFLGDSVTLPCYLQVpgmeETHVSQLTWSR-HGESG-SMAIFHPTQG----PKYSepKRLEFVATrlg 96
Cdd:cd05887     1 GPIIV--EPHVTAVWGKNVSLKCLIEV----NETITQISWEKiHGKSSqTVAVHHPQYGisiqGEYQ--GRVSFKNY--- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622897446  97 tELRDASLRMFGLRVEDEGSYTCVFFIFPQGKRSVDIWLRVL 138
Cdd:cd05887    70 -SLNDATITLHNVGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgI_2_Necl-1 cd07705
Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set ...
 135-222 9.43e-06

Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1; also known as cell adhesion molecule3 (CADM3)). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one 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 and Necl-2 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. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409502  Cd Length: 103  Bit Score: 44.19  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 135 LRVLAKPQNTAEVQKVQLTGKPVpvARCVSTGGRPPAHITWH---SDLGGMPNTSQAPGFlSGTVTVTSLWILVPSSQVD 211
Cdd:cd07705     1 LGIPQKPQITGYESAFKEKDKAK--LRCTSSGSKPAANIKWRkgdQELEGAPTSVQEDGN-GKTFTVSSSVEFQVTREDD 77

                          90
                  ....*....|.
gi 1622897446 212 GKSVTCKVEHE 222
Cdd:cd07705    78 GAEITCSVGHE 88
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 146-222 1.37e-05

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one 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 and Necl-2 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 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 409418  Cd Length: 102  Bit Score: 43.57  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 146 EVQKVQLTgkpvpvarCVSTGGRPPAHITW---HSDLGGMPNTSQAPGflSGTVTVTSLWILVPSSQVDGKSVTCKVEHE 222
Cdd:cd05761    18 EGDEITLT--------CTTSGSKPAADIRWfknDKELKGVKEVQESGA--GKTFTVTSTLRFRVDRDDDGVAVICRVDHE 87
Ig_SLAM-like_N cd16842
N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule ...
 31-117 7.08e-05

N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family and similar proteins. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. Members of this group include proteins such as CD84, SLAM (CD150), Ly-9 (CD229), NTB-A (ly-108, SLAM6), 19A (CRACC), and SLAMF9. The genes coding for the SLAM family are nested on chromosome 1, in humans at 1q23, and in mice at 1H2. The SLAM family is a subset of the CD2 family, which also includes CD2 and CD58 located on chromosome 1 at 1p13 in humans. In mice, CD2 is located on chromosome 3, and there is no CD58 homolog. The SLAM family proteins are organized as an extracellular domain with either two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.


Pssm-ID: 409517  Cd Length: 102  Bit Score: 41.54  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  31 TQVPGFLGDSVTLPcyLQVPgmEETHVSQLTWSRHGESGSMAIFHPTQG------PKYSEpkRLEFVAtrlgtelRDASL 104
Cdd:cd16842     1 KEVNGILGGSVTFP--LNIS--DGQEIENITWSFKTSLAVIAPGEGGAPeiiitdKSYKE--RLNISQ-------NDYSL 67

                          90
                  ....*....|...
gi 1622897446 105 RMFGLRVEDEGSY 117
Cdd:cd16842    68 QISNLTMEDAGSY 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 30-137 7.93e-05

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: 40.95  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446   30 PTQVPGFLGDSVTLPCylQVPGMEETHVsqlTWSRHGesgsmaifhptqGPKYSEPKRleFVATRLGTelrDASLRMFGL 109
Cdd:smart00410   1 PPSVTVKEGESVTLSC--EASGSPPPEV---TWYKQG------------GKLLAESGR--FSVSRSGS---TSTLTISNV 58

                           90       100
                   ....*....|....*....|....*...
gi 1622897446  110 RVEDEGSYTCVfFIFPQGKRSVDIWLRV 137
Cdd:smart00410  59 TPEDSGTYTCA-ATNSSGSASSGTTLTV 85
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 27-121 1.22e-04

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 41.41  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  27 VQAPTQ-VPGFLGDSVTLPCYLQvPGMEETHVsQLTWSRhgESGSMAIFHPTQGPKYSEPKRLEFvatRLGTEL-RDA-- 102
Cdd:cd05713     3 VIGPTEpILALVGEDAELPCHLS-PKMSAEHM-EVRWFR--SQFSPVVHLYRDGQDQEEEQMPEY---RGRTELlKDAia 75

                          90       100
                  ....*....|....*....|...
gi 1622897446 103 ----SLRMFGLRVEDEGSYTCVF 121
Cdd:cd05713    76 egsvALRIHNVRPSDEGQYTCFF 98
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 25-119 7.36e-04

Immunoglobulin (Ig)-like domain of protein zero (P0); 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 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.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 39.09  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446  25 IVVQAPTQVPGFLGDSVTLPCYLQVPGMEETHVSqLTWSRHGESG--SMAIFHPTQGPKYSEPK-----RLEFVATrlgT 97
Cdd:cd05879     1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDIS-FTWHYQPDGSrdAISIFHYGKGQPYIDNVgpfkeRIEWVGN---P 76

                          90       100
                  ....*....|....*....|..
gi 1622897446  98 ELRDASLRMFGLRVEDEGSYTC 119
Cdd:cd05879    77 SRKDGSIVIHNLDYTDNGTFTC 98
IgI_2_Necl-3 cd05884
Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set ...
 148-222 3.70e-03

Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3; also known as cell adhesion molecule 2 (CADM2)). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409467  Cd Length: 104  Bit Score: 36.83  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897446 148 QKVQLTGKPVPVAR-------CVSTGGRPPAHITWHSDLGGMPNTS--QAPGFLSGTVTVTSLWILVPSSQVDGKSVTCK 218
Cdd:cd05884     6 EKPQISGFTSPVMEgdhiqltCKTSGSKPAADIRWFKNDKEVKDVKylKAEDANRKTFTVSSSLDFHVDRDDDGVAITCR 85


                  ....
gi 1622897446 219 VEHE 222
Cdd:cd05884    86 VDHE 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 258-315 4.03e-03

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 35.77  E-value: 4.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897446 258 ATLTCDARSNPEPTgYNWSTTMGPLPPFAVAQ------GAQLLIRPVDKPINTTFICNVTNALG 315
Cdd:cd00096     1 VTLTCSASGNPPPT-ITWYKNGKPLPPSSRDSrrselgNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 257-325 7.51e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. 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. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 35.45  E-value: 7.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897446 257 EATLTCDARSNPEPT---GYNWSTTMGPLPPFAVAQGAqLLIRPVDKPINTTFICNVTNALGARQAELTVQV 325
Cdd:cd20978    18 DVTLPCQVTGVPQPKitwLHNGKPLQGPMERATVEDGT-LTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgC1_CH1_IgEG cd21817
CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and ...
 162-221 8.12e-03

CH1 domain (first constant Ig domain of the heavy chain) in immunoglobulin heavy epsilon and gamma chain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin constant-1 set domain of epsilon and gamma chains. It belongs to a family composed of the first immunoglobulin constant-1 set domain of alpha, delta, epsilon, gamma, and mu heavy chains. This domain is found on the Fab antigen-binding fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. This group belongs to the C1-set of IgSF domains, which are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and heavy chains, in the major histocompatibility complex (MHC) class I and II complex molecules, and in various T-cell receptors.


Pssm-ID: 409622  Cd Length: 94  Bit Score: 35.50  E-value: 8.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897446 162 CVSTGGRP-PAHITWHSD-LGGMPNTSQAPGFLSGTVTVTSLwILVPSSQVDGKSVTCKVEH 221
Cdd:cd21817    23 CLVTGYFPePVTVTWNSGsLTSGVKTFPAVLQSSGLYTTSSQ-VTVPSSSWGSQTFTCNVEH 83
 
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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