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Conserved domains on  [gi|157818655|ref|NP_001100288|]
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myelin protein zero-like protein 2 precursor [Rattus norvegicus]

Protein Classification

immunoglobulin domain-containing family protein; immunoglobulin domain-containing protein( domain architecture ID 10147193)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 27-142 1.37e-77

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


:

Pssm-ID: 409464  Cd Length: 116  Bit Score: 228.56  E-value: 1.37e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  27 VEIYTSGALEAVNGTDIRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDV 106
Cdd:cd05880    1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDGNIMRRDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157818655 107 SIMLWKLQFDDNGTYTCQVKNPPDVDGLIGTIRLSV 142
Cdd:cd05880   81 SILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
 
Name Accession Description Interval E-value
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 27-142 1.37e-77

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 228.56  E-value: 1.37e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  27 VEIYTSGALEAVNGTDIRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDV 106
Cdd:cd05880    1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDGNIMRRDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157818655 107 SIMLWKLQFDDNGTYTCQVKNPPDVDGLIGTIRLSV 142
Cdd:cd05880   81 SILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 30-143 2.62e-23

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: 89.82  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655   30 YTSGALEAVNGTDIRLKCTFSSFaPVGDALTVTWNFRPRDGGREQFVFYYHmdPFRPMsGRFKDRVVWDGNPERYDVSIM 109
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYS--NGSEE-GVKKGRFSGRGDPSNGDGSLT 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 157818655  110 LWKLQFDDNGTYTCQVkNPPDVDGLIGTIRLSVV 143
Cdd:pfam07686  77 IQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
42-125 1.08e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 53.15  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655    42 DIRLKCTFSSFAPVGdaLTVTWnFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDVSIMLWKLQFDDNGTY 121
Cdd:smart00406   1 SVTLSCKFSGSTFSS--YYVSW-VRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTY 77


                   ....
gi 157818655   122 TCQV 125
Cdd:smart00406  78 YCAV 81
 
Name Accession Description Interval E-value
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 27-142 1.37e-77

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 228.56  E-value: 1.37e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  27 VEIYTSGALEAVNGTDIRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDV 106
Cdd:cd05880    1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDGNIMRRDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157818655 107 SIMLWKLQFDDNGTYTCQVKNPPDVDGLIGTIRLSV 142
Cdd:cd05880   81 SILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 27-142 1.98e-62

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: 189.95  E-value: 1.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  27 VEIYTSGALEAVNGTDIRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYH-MDPFRPMSGRFKDRVVWDGNPERYD 105
Cdd:cd05715    1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSkGKPYILKVGRFKDRVSWAGNPSKKD 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157818655 106 VSIMLWKLQFDDNGTYTCQVKNPPDVDGLIGTIRLSV 142
Cdd:cd05715   81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 27-142 4.77e-28

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: 102.26  E-value: 4.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  27 VEIYTSGALEAVNGTDIRLKCTFSSFAPVGDALTVTWNFRPrDGGREQF-VFYYHM-DPFRPMSGRFKDRVVWDGNPERY 104
Cdd:cd05879    1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQP-DGSRDAIsIFHYGKgQPYIDNVGPFKERIEWVGNPSRK 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157818655 105 DVSIMLWKLQFDDNGTYTCQVKNPPDVDGLIGTIRLSV 142
Cdd:cd05879   80 DGSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 30-143 2.62e-23

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: 89.82  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655   30 YTSGALEAVNGTDIRLKCTFSSFaPVGDALTVTWNFRPRDGGREQFVFYYHmdPFRPMsGRFKDRVVWDGNPERYDVSIM 109
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYS--NGSEE-GVKKGRFSGRGDPSNGDGSLT 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 157818655  110 LWKLQFDDNGTYTCQVkNPPDVDGLIGTIRLSVV 143
Cdd:pfam07686  77 IQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
42-125 1.08e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 53.15  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655    42 DIRLKCTFSSFAPVGdaLTVTWnFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDVSIMLWKLQFDDNGTY 121
Cdd:smart00406   1 SVTLSCKFSGSTFSS--YYVSW-VRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTY 77


                   ....
gi 157818655   122 TCQV 125
Cdd:smart00406  78 YCAV 81
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 34-131 1.63e-07

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


Pssm-ID: 409552  Cd Length: 114  Bit Score: 48.22  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  34 ALEAVNGTDIRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDVSIMLWKL 113
Cdd:cd20960    9 EIKKVAGENVTLPCHHQLGLEDQGTLDIEWLLLPSDKVEKVVITYSGDRVYNHYYPALKGRVAFTSNDLSGDASLNISNL 88

                         90
                 ....*....|....*...
gi 157818655 114 QFDDNGTYTCQVKNPPDV 131
Cdd:cd20960   89 KLSDTGTYQCKVKKAPGY 106
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 32-142 1.00e-06

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: 45.19  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655    32 SGALEAVNGTDIRLKCTFSSFAPVgdalTVTWNfrpRDGGreQFVFYyhmdpfrpmSGRFKdrVVWDGNperyDVSIMLW 111
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPP----EVTWY---KQGG--KLLAE---------SGRFS--VSRSGS----TSTLTIS 56

                           90       100       110
                   ....*....|....*....|....*....|.
gi 157818655   112 KLQFDDNGTYTCQVKNppDVDGLIGTIRLSV 142
Cdd:smart00410  57 NVTPEDSGTYTCAATN--SSGSASSGTTLTV 85
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 36-131 2.62e-06

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: 44.64  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  36 EAVNGTDIRLKCTFSSfapVGDALTVTWNfRPRDGGREQFVFYYHMDPFRPMsGRFKDRVVWDgNPERYDVSIMLWKLQF 115
Cdd:cd05846    9 RAVLGGNATLSCNLTL---PEEVLQVTWQ-KIKASSPENIVTYSKKYGVKIQ-PSYVRRISFT-SSGLNSTSITIWNVTL 82

                         90
                 ....*....|....*.
gi 157818655 116 DDNGTYTCQVKNPPDV 131
Cdd:cd05846   83 EDEGCYKCLFNTFPDG 98
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 40-142 3.46e-05

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: 41.55  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  40 GTDIRLKCTFSSFAPVGdalTVTWnFRPRDGGREQFVFYYHMDpFRPMSGRFKDRVVWDGNPERyDVSIMLWKLQFDDNG 119
Cdd:cd00099   13 GESVTLSCEVSSSFSST---YIYW-YRQKPGQGPEFLIYLSSS-KGKTKGGVPGRFSGSRDGTS-SFSLTISNLQPEDSG 86

                         90       100
                 ....*....|....*....|....*.
gi 157818655 120 TYTCQVKNPPDVDGLI---GTiRLSV 142
Cdd:cd00099   87 TYYCAVSESGGTDKLTfgsGT-RLTV 111
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 40-129 4.66e-05

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: 41.49  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  40 GTDIRLKCTFSSFAPVGDALTVTWnfRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDgNPERYDVSIMLWKLQFDDNG 119
Cdd:cd05886   14 GTDVVLHCSFANPLPSVKITQVTW--QKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFL-NPSFTDGTIRLSRLELEDEG 90

                         90
                 ....*....|
gi 157818655 120 TYTCQVKNPP 129
Cdd:cd05886   91 VYICEFATFP 100
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 37-125 6.51e-04

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


Pssm-ID: 409383  Cd Length: 113  Bit Score: 38.20  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  37 AVNGTDIRLKCTFSSfaPVGDALT-VTWnFRPrDGGREQFVFYYH----MDPFRPMSGRFKDRVvwdGNPERYDVSIMLW 111
Cdd:cd05718   11 GFLGGSVTLPCSLTS--PGTTKITqVTW-MKI-GAGSSQNVAVFHpqygPSVPNPYAERVEFLA---ARLGLRNATLRIR 83

                         90
                 ....*....|....
gi 157818655 112 KLQFDDNGTYTCQV 125
Cdd:cd05718   84 NLRVEDEGNYICEF 97
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 94-132 9.75e-04

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.17  E-value: 9.75e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 157818655   94 RVVWDGNPERYDVSIMLWKLQFDDNGTYTCQVKNPPDVD 132
Cdd:pfam00047  42 LKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 31-125 2.77e-03

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409483  Cd Length: 121  Bit Score: 36.35  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  31 TSGALEAVNGTDIRLKCTFS---SFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPE-RYDV 106
Cdd:cd05902    3 TAPPVRRPLSSSVLLPCVFTlppSASSPPEGPRIKWTKLSTSGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKnRYNA 82

                         90
                 ....*....|....*....
gi 157818655 107 SIMLWKLQFDDNGTYTCQV 125
Cdd:cd05902   83 SLVLSRLRYSDSGTYRCEV 101
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 23-134 6.53e-03

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 35.38  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  23 PTTAVEIYtsgaleAVNGTDIRLKCTF----SSFAPVGdaLTVTWNFRPRDGGREQFVFY---YHMDPFrpmsGRFKDRV 95
Cdd:cd05877    1 ETVQAKVF------SHRGGNVTLPCRYhyepELSAPRK--IRVKWTKLEVDYAKEEDVLVaigTRHKSY----GSYQGRV 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157818655  96 VWDGNPERyDVSIMLWKLQFDDNGTYTCQVknppdVDGL 134
Cdd:cd05877   69 FLRRADDL-DASLVITDLRLEDYGRYRCEV-----IDGL 101
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 37-130 6.95e-03

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 34.82  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818655  37 AVNGTDIRLKCTFSSFApvgDALTVTWNFRPRDggrEQFVFYYHMDpfrpMSGRFKDRVVWDGnperydVSIMLWKLQFD 116
Cdd:cd20946   11 VVENQEVILSCKTPKKT---SSPRVEWKKLQRD---VTFVVFQNNK----IQGDYKGRAEILG------TNITIKNVTRS 74

                         90
                 ....*....|....
gi 157818655 117 DNGTYTCQVKNPPD 130
Cdd:cd20946   75 DSGKYRCEVSARSD 88
 
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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