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Conserved domains on  [gi|68163543|ref|NP_001020203|]
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T-cell surface protein tactile precursor [Rattus norvegicus]

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 ...
 33-137 9.02e-13

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: 65.16  E-value: 9.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543  33 NVYALPGSDVNLTC--QTMEKDLMVQMQWSKV-TDEIDMIVVYHPQYGFHYmQGVACE--SRVAAVETLKDATkwtLNLR 107
Cdd:cd05718   8 EVTGFLGGSVTLPCslTSPGTTKITQVTWMKIgAGSSQNVAVFHPQYGPSV-PNPYAErvEFLAARLGLRNAT---LRIR 83

                        90       100       110
                ....*....|....*....|....*....|
gi 68163543 108 NISSSLSGKYECSFTMYPTGTKTIVYNLIV 137
Cdd:cd05718  84 NLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 267-343 4.42e-04

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 pfam08205:

Pssm-ID: 472250  Cd Length: 89  Bit Score: 39.32  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68163543   267 ERVFTCLLKNVFPKASITWLIDGRlfqgnEEGIYITNEEKNSSSGFWELKSVLTrmHNRTSQSNNMTVWCMALSPGP 343
Cdd:pfam08205  16 EVVATCSSAGGKPAPRITWYLDGK-----PLEAAETSSEQDPESGLVTVTSELK--LVPSRSDHGQSLTCQVSYGAL 85
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 350-493 9.18e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.21  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543   350 TSSQPITFS--LDSGTAPTKRLPNVTGSTLGAQTFPDAEVSPTRYLATSSMTIVDENVLTP-DPT-----PQTSNSSMTT 421
Cdd:pfam05109 612 TSSTPVVTSppKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSaHPTggeniTQVTPASTST 691

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68163543   422 KDVNYSQPS----SGTDAKNSSRAASSSDGGSRPFPSTSPPKwlslphTSTGPQEPDSAVSWIPTDAYTSGSSDAS 493
Cdd:pfam05109 692 HHVSTSSPAprpgTTSQASGPGNSSTSTKPGEVNVTKGTPPK------NATSPQAPSGQKTAVPTVTSTGGKANST 761
 
Name Accession Description Interval E-value
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 33-137 9.02e-13

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: 65.16  E-value: 9.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543  33 NVYALPGSDVNLTC--QTMEKDLMVQMQWSKV-TDEIDMIVVYHPQYGFHYmQGVACE--SRVAAVETLKDATkwtLNLR 107
Cdd:cd05718   8 EVTGFLGGSVTLPCslTSPGTTKITQVTWMKIgAGSSQNVAVFHPQYGPSV-PNPYAErvEFLAARLGLRNAT---LRIR 83

                        90       100       110
                ....*....|....*....|....*....|
gi 68163543 108 NISSSLSGKYECSFTMYPTGTKTIVYNLIV 137
Cdd:cd05718  84 NLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 267-343 4.42e-04

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 39.32  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68163543   267 ERVFTCLLKNVFPKASITWLIDGRlfqgnEEGIYITNEEKNSSSGFWELKSVLTrmHNRTSQSNNMTVWCMALSPGP 343
Cdd:pfam08205  16 EVVATCSSAGGKPAPRITWYLDGK-----PLEAAETSSEQDPESGLVTVTSELK--LVPSRSDHGQSLTCQVSYGAL 85
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 350-493 9.18e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.21  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543   350 TSSQPITFS--LDSGTAPTKRLPNVTGSTLGAQTFPDAEVSPTRYLATSSMTIVDENVLTP-DPT-----PQTSNSSMTT 421
Cdd:pfam05109 612 TSSTPVVTSppKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSaHPTggeniTQVTPASTST 691

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68163543   422 KDVNYSQPS----SGTDAKNSSRAASSSDGGSRPFPSTSPPKwlslphTSTGPQEPDSAVSWIPTDAYTSGSSDAS 493
Cdd:pfam05109 692 HHVSTSSPAprpgTTSQASGPGNSSTSTKPGEVNVTKGTPPK------NATSPQAPSGQKTAVPTVTSTGGKANST 761
 
Name Accession Description Interval E-value
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 33-137 9.02e-13

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: 65.16  E-value: 9.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543  33 NVYALPGSDVNLTC--QTMEKDLMVQMQWSKV-TDEIDMIVVYHPQYGFHYmQGVACE--SRVAAVETLKDATkwtLNLR 107
Cdd:cd05718   8 EVTGFLGGSVTLPCslTSPGTTKITQVTWMKIgAGSSQNVAVFHPQYGPSV-PNPYAErvEFLAARLGLRNAT---LRIR 83

                        90       100       110
                ....*....|....*....|....*....|
gi 68163543 108 NISSSLSGKYECSFTMYPTGTKTIVYNLIV 137
Cdd:cd05718  84 NLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 44-128 3.39e-08

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: 51.79  E-value: 3.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543  44 LTCQTMEKDLMVQMQWSKVTDEIDMIVVYHPQYGFHYmqGVACESRVAAVETLKDATKWTLNLRNISSSLSGKYECSFTM 123
Cdd:cd05889  19 LECVYPSTGILTQVEWTKIGGQKDNIAVYHPTHGMHI--RKPYAGRVYFLNSTMASNNMSLSFRNASEDDVGYYSCSLYT 96


                ....*
gi 68163543 124 YPTGT 128
Cdd:cd05889  97 YPQGS 101
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 31-127 3.23e-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: 43.39  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543  31 DNNVYALPGSDVNLTCQTMEKDLMVQMQWSKVTDEI-DMIVVYHPQYGFHyMQGvACESRVAAVE-TLKDATkwtLNLRN 108
Cdd:cd05887   6 EPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSsQTVAVHHPQYGIS-IQG-EYQGRVSFKNySLNDAT---ITLHN 80

                        90
                ....*....|....*....
gi 68163543 109 ISSSLSGKYECSFTMYPTG 127
Cdd:cd05887  81 VGFSDSGKYICKAVTFPLG 99
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 267-343 4.42e-04

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 39.32  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68163543   267 ERVFTCLLKNVFPKASITWLIDGRlfqgnEEGIYITNEEKNSSSGFWELKSVLTrmHNRTSQSNNMTVWCMALSPGP 343
Cdd:pfam08205  16 EVVATCSSAGGKPAPRITWYLDGK-----PLEAAETSSEQDPESGLVTVTSELK--LVPSRSDHGQSLTCQVSYGAL 85
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 350-493 9.18e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.21  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543   350 TSSQPITFS--LDSGTAPTKRLPNVTGSTLGAQTFPDAEVSPTRYLATSSMTIVDENVLTP-DPT-----PQTSNSSMTT 421
Cdd:pfam05109 612 TSSTPVVTSppKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSaHPTggeniTQVTPASTST 691

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68163543   422 KDVNYSQPS----SGTDAKNSSRAASSSDGGSRPFPSTSPPKwlslphTSTGPQEPDSAVSWIPTDAYTSGSSDAS 493
Cdd:pfam05109 692 HHVSTSSPAprpgTTSQASGPGNSSTSTKPGEVNVTKGTPPK------NATSPQAPSGQKTAVPTVTSTGGKANST 761
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 33-132 3.19e-03

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: 37.56  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163543  33 NVYALPGSDVNLTCQTMEKDLMV---QMQWSKvTDEIDMIVVYHPQYGFHYMQGVACESRVAAVET-LKDATkwtLNLRN 108
Cdd:cd20989   8 EVRGFLGGSVTLPCHLLPPNMVThvsQVTWQR-HDEHGSVAVFHPKQGPSFPESERLSFVAARLGAeLRNAS---LAMFG 83

                        90       100
                ....*....|....*....|....
gi 68163543 109 ISSSLSGKYECSFTMYPTGTKTIV 132
Cdd:cd20989  84 LRVEDEGNYTCEFATFPQGSRSGD 107
 
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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