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Conserved domains on  [gi|256600228|ref|NP_776160|]
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T-cell immunoreceptor with Ig and ITIM domains precursor [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 38-126 1.09e-12

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 cd05718:

Pssm-ID: 472250  Cd Length: 113  Bit Score: 62.85  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  38 GGSIILQCHL-SSTTAQVTQVNWEQQD----QLLAICNADLGWHISPSFKDRV---APGPGL---GLTLQSLTVNDTGEY 106
Cdd:cd05718   14 GGSVTLPCSLtSPGTTKITQVTWMKIGagssQNVAVFHPQYGPSVPNPYAERVeflAARLGLrnaTLRIRNLRVEDEGNY 93

                         90       100
                 ....*....|....*....|
gi 256600228 107 FCIYHTYPDGTYTGRIFLEV 126
Cdd:cd05718   94 ICEFATFPQGNRQGTTWLRV 113
 
Name Accession Description Interval E-value
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 38-126 1.09e-12

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: 62.85  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  38 GGSIILQCHL-SSTTAQVTQVNWEQQD----QLLAICNADLGWHISPSFKDRV---APGPGL---GLTLQSLTVNDTGEY 106
Cdd:cd05718   14 GGSVTLPCSLtSPGTTKITQVTWMKIGagssQNVAVFHPQYGPSVPNPYAERVeflAARLGLrnaTLRIRNLRVEDEGNY 93

                         90       100
                 ....*....|....*....|
gi 256600228 107 FCIYHTYPDGTYTGRIFLEV 126
Cdd:cd05718   94 ICEFATFPQGNRQGTTWLRV 113
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 33-127 1.99e-07

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: 48.22  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228   33 ISAEKGGSIILQCHL-SSTTAQVTQVNWEQQDQLLAICNADLGWHIS---PSFKDRV----APGPGLG-LTLQSLTVNDT 103
Cdd:pfam07686   6 VTVALGGSVTLPCTYsSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGseeGVKKGRFsgrgDPSNGDGsLTIQNLTLSDS 85

                          90       100
                  ....*....|....*....|....
gi 256600228  104 GEYFCIYHTYPDGTYTGRIFLEVL 127
Cdd:pfam07686  86 GTYTCAVIPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
40-108 2.03e-07

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 47.38  E-value: 2.03e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256600228    40 SIILQCHLSSTTAQVTQVNWEQQDQ-----LLAICNADLGWHISPSFKDRVA----PGPGLG-LTLQSLTVNDTGEYFC 108
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPgkgleWLGYIGSNGSSYYQESYKGRFTiskdTSKNDVsLTISNLRVEDTGTYYC 79
 
Name Accession Description Interval E-value
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 38-126 1.09e-12

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: 62.85  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  38 GGSIILQCHL-SSTTAQVTQVNWEQQD----QLLAICNADLGWHISPSFKDRV---APGPGL---GLTLQSLTVNDTGEY 106
Cdd:cd05718   14 GGSVTLPCSLtSPGTTKITQVTWMKIGagssQNVAVFHPQYGPSVPNPYAERVeflAARLGLrnaTLRIRNLRVEDEGNY 93

                         90       100
                 ....*....|....*....|
gi 256600228 107 FCIYHTYPDGTYTGRIFLEV 126
Cdd:cd05718   94 ICEFATFPQGNRQGTTWLRV 113
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 30-126 3.19e-10

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: 55.81  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  30 TGNISAEKGGSIILQCHLSsTTAQVTQVNW----EQQDQLLAICNADLGWHISPSFKDRVA-PGPGLG---LTLQSLTVN 101
Cdd:cd05846    5 TGDTRAVLGGNATLSCNLT-LPEEVLQVTWqkikASSPENIVTYSKKYGVKIQPSYVRRISfTSSGLNstsITIWNVTLE 83

                         90       100
                 ....*....|....*....|....*
gi 256600228 102 DTGEYFCIYHTYPDGTYTGRIFLEV 126
Cdd:cd05846   84 DEGCYKCLFNTFPDGIKSGTACLTV 108
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 38-126 2.05e-09

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: 53.74  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  38 GGSIILQCHLSS--TTAQVTQVNWEQQD--QLLAICNADLGwhisPSFK--DRVA-----PGPGL---GLTLQSLTVNDT 103
Cdd:cd20989   14 GGSVTLPCHLLPpnMVTHVSQVTWQRHDehGSVAVFHPKQG----PSFPesERLSfvaarLGAELrnaSLAMFGLRVEDE 89

                         90       100
                 ....*....|....*....|...
gi 256600228 104 GEYFCIYHTYPDGTYTGRIFLEV 126
Cdd:cd20989   90 GNYTCEFATFPQGSRSGDTWLRV 112
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 26-127 1.04e-08

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: 51.89  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  26 TIETTGNISAEKGGSIILQCHL--SSTTAQVTQVNWEQ----QDQLLAICNADLGWHISPSFKDRVA-PGPGL---GLTL 95
Cdd:cd05886    2 TVQVNDSMSGFIGTDVVLHCSFanPLPSVKITQVTWQKstngSKQNVAIYNPSMGVSVLPPYRERVTfLNPSFtdgTIRL 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 256600228  96 QSLTVNDTGEYFCIYHTYPDGTYTGRIFLEVL 127
Cdd:cd05886   82 SRLELEDEGVYICEFATFPTGNRESQLNLTVM 113
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 33-127 6.42e-08

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: 49.51  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  33 ISAEKGGSIILQCHLS-STTAQVTQVNWEQQD-----QLLAICNADLGWHISPSFKDRV---APGPGL--GLTLQSLTVN 101
Cdd:cd05888    3 VTVVLGQDAKLPCFYRgDSGEQVGQVAWARVDagegaQEIALLHSKYGLHVFPAYEGRVeqpPPPRPAdgSVLLRNAVQA 82

                         90       100
                 ....*....|....*....|....*.
gi 256600228 102 DTGEYFCIYHTYPDGTYTGRIFLEVL 127
Cdd:cd05888   83 DEGEYECRVSTFPAGNFQAELRLRVL 108
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 33-127 1.99e-07

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: 48.22  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228   33 ISAEKGGSIILQCHL-SSTTAQVTQVNWEQQDQLLAICNADLGWHIS---PSFKDRV----APGPGLG-LTLQSLTVNDT 103
Cdd:pfam07686   6 VTVALGGSVTLPCTYsSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGseeGVKKGRFsgrgDPSNGDGsLTIQNLTLSDS 85

                          90       100
                  ....*....|....*....|....
gi 256600228  104 GEYFCIYHTYPDGTYTGRIFLEVL 127
Cdd:pfam07686  86 GTYTCAVIPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
40-108 2.03e-07

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 47.38  E-value: 2.03e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256600228    40 SIILQCHLSSTTAQVTQVNWEQQDQ-----LLAICNADLGWHISPSFKDRVA----PGPGLG-LTLQSLTVNDTGEYFC 108
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPgkgleWLGYIGSNGSSYYQESYKGRFTiskdTSKNDVsLTISNLRVEDTGTYYC 79
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 43-124 4.37e-07

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: 47.16  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  43 LQChLSSTTAQVTQVNWEQ---QDQLLAICNADLGWHISPSFKDRV------APGPGLGLTLQSLTVNDTGEYFCIYHTY 113
Cdd:cd05889   19 LEC-VYPSTGILTQVEWTKiggQKDNIAVYHPTHGMHIRKPYAGRVyflnstMASNNMSLSFRNASEDDVGYYSCSLYTY 97

                         90
                 ....*....|.
gi 256600228 114 PDGTYTGRIFL 124
Cdd:cd05889   98 PQGSWEKVIQV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 31-126 4.86e-07

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: 46.34  E-value: 4.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228    31 GNISAEKGGSIILQCHLSSTTaqVTQVNWEQQDqllaicnadLGWHISPSFKDRVAPGPGLGLTLQSLTVNDTGEYFCIy 110
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSP--PPEVTWYKQG---------GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCA- 69

                           90
                   ....*....|....*.
gi 256600228   111 HTYPDGTYTGRIFLEV 126
Cdd:smart00410  70 ATNSSGSASSGTTLTV 85
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 33-127 9.27e-05

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: 40.69  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  33 ISAEKGGSIILQCHLSSTTAqVTQVNWEQQ----DQLLAICNADLGWHISPSFKDRVA-PGPGL---GLTLQSLTVNDTG 104
Cdd:cd05887    9 VTAVWGKNVSLKCLIEVNET-ITQISWEKIhgksSQTVAVHHPQYGISIQGEYQGRVSfKNYSLndaTITLHNVGFSDSG 87

                         90       100
                 ....*....|....*....|...
gi 256600228 105 EYFCIYHTYPDGTYTGRIFLEVL 127
Cdd:cd05887   88 KYICKAVTFPLGNAQSSTTVTVL 110
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 29-123 1.24e-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: 39.87  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228   29 TTGNISAEKGGSIILQCHLSSTTAQVtQVNWEQQDQLLaicnaDLGWHISPSFKDRVapgpGLGLTLQSLTVNDTGEYFC 108
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSASTGSPGP-DVTWSKEGGTL-----IESLKVKHDNGRTT----QSSLLISNVTKEDAGTYTC 71

                          90
                  ....*....|....*
gi 256600228  109 IYHTYPDGTYTGRIF 123
Cdd:pfam00047  72 VVNNPGGSATLSTSL 86
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 33-108 4.28e-04

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: 38.85  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  33 ISAEKGGSIILQCHLSSTTAqVTQVNWEQQD-----QLLAICNADLGwHISPSFKDR-VAPGPGLG---LTLQSLTVNDT 103
Cdd:cd00099    8 LSVQEGESVTLSCEVSSSFS-STYIYWYRQKpgqgpEFLIYLSSSKG-KTKGGVPGRfSGSRDGTSsfsLTISNLQPEDS 85


                 ....*
gi 256600228 104 GEYFC 108
Cdd:cd00099   86 GTYYC 90
IgV_CEACAM_like cd05741
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
 29-106 7.06e-04

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and related domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface. This family corresponds to the D1 Ig-like domain. Also belonging to this group is the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family, CD84-like family. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. SLAM family proteins are organized as an extracellular domain with having 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: 409403  Cd Length: 102  Bit Score: 37.88  E-value: 7.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256600228  29 TTGNISAEKGGSIILqcHLSSTTAQVTQVNWEQQ------DQLLAICNADLGWHISPSFKDRVAPGPGLGLTLQSLTVND 102
Cdd:cd05741    1 SSEQFYGAEGKNVLL--LVPNLQTPLKSVSWYKGkqvsrnDEIAEYENSSDEFRAGSAFSGREYIYTNGSLLIQNITLSD 78


                 ....
gi 256600228 103 TGEY 106
Cdd:cd05741   79 TGFY 82
 
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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