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Conserved domains on  [gi|119600065|gb|EAW79659|]
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CD200 receptor 1, isoform CRA_c, partial [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 ...
 67-173 3.27e-42

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 cd20985:

Pssm-ID: 472250  Cd Length: 107  Bit Score: 140.03  E-value: 3.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600065  67 EVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETkETNCTDERITWVSRPDQNSDLQIRTVA 146
Cdd:cd20985    2 EVNTTVSVQMGTKALLCCFSIPLTKAVLITWIIKLRGQPSCTIAYKVDTKET-ETSCLDRNITWASTPDHSPDLQISAVA 80

                         90       100
                 ....*....|....*....|....*..
gi 119600065 147 ITHDGYYRCIMVTPDGNFHRGYHLQVL 173
Cdd:cd20985   81 LQHEGTYSCEIVTPEGNFQKVYDLQVL 107
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 174-225 4.21e-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 cd05719:

Pssm-ID: 472250  Cd Length: 96  Bit Score: 38.63  E-value: 4.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119600065 174 VTPEVTLFQNRNRTAVCKAVAGKPAAHISWIPE--GDCATKQEYWSNGTVTVKS 225
Cdd:cd05719    7 GGPALLIGGEPTLVATCISANGKPPASVTWETDlkGEASTTQVRGSNGTVTVTS 60
 
Name Accession Description Interval E-value
IgV_CD200R-like cd20985
Immunoglobulin Variable domain of cell surface glycoprotein CD200 receptor and similar ...
 67-173 3.27e-42

Immunoglobulin Variable domain of cell surface glycoprotein CD200 receptor and similar proteins; The members here are composed of the immunoglobulin variable (IgV) domain of cell surface glycoprotein CD200 receptor and similar proteins. CD200 (also known as OX2) is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R). CD200-CD200R interactions are involved in the control of myeloid cellular function. In the mouse, several CD200R-related genes have been identified, including CD200RL (for receptor like), CD200R1, and CD200R2. While CD200 gives good binding to CD200R, it does not bind CD200RLa, CD200RLb, CD200RLc, or CD200RLe. For instance, CD200RLa has a 50-fold lower binding affinity to CD200, although CD200RLa shares a high amino acid sequence identity with CD200R in the V-like domain. Furthermore, the CD200-CD200R regulatory interactions provide an attractive target for immunomodulation, because its manipulation can provoke either immune tolerance or autoimmune diseases.


Pssm-ID: 409577  Cd Length: 107  Bit Score: 140.03  E-value: 3.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600065  67 EVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETkETNCTDERITWVSRPDQNSDLQIRTVA 146
Cdd:cd20985    2 EVNTTVSVQMGTKALLCCFSIPLTKAVLITWIIKLRGQPSCTIAYKVDTKET-ETSCLDRNITWASTPDHSPDLQISAVA 80

                         90       100
                 ....*....|....*....|....*..
gi 119600065 147 ITHDGYYRCIMVTPDGNFHRGYHLQVL 173
Cdd:cd20985   81 LQHEGTYSCEIVTPEGNFQKVYDLQVL 107
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 174-225 4.21e-04

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: 38.63  E-value: 4.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119600065 174 VTPEVTLFQNRNRTAVCKAVAGKPAAHISWIPE--GDCATKQEYWSNGTVTVKS 225
Cdd:cd05719    7 GGPALLIGGEPTLVATCISANGKPPASVTWETDlkGEASTTQVRGSNGTVTVTS 60
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 174-229 9.25e-03

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 34.70  E-value: 9.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600065  174 VTPEVTLF--QNRNRTAVCKAVAGKPAAHISWI----PEGDCATKQEYWS-NGTVTVKSTCHW 229
Cdd:pfam08205   3 IEPPASLLegEGPEVVATCSSAGGKPAPRITWYldgkPLEAAETSSEQDPeSGLVTVTSELKL 65
 
Name Accession Description Interval E-value
IgV_CD200R-like cd20985
Immunoglobulin Variable domain of cell surface glycoprotein CD200 receptor and similar ...
 67-173 3.27e-42

Immunoglobulin Variable domain of cell surface glycoprotein CD200 receptor and similar proteins; The members here are composed of the immunoglobulin variable (IgV) domain of cell surface glycoprotein CD200 receptor and similar proteins. CD200 (also known as OX2) is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R). CD200-CD200R interactions are involved in the control of myeloid cellular function. In the mouse, several CD200R-related genes have been identified, including CD200RL (for receptor like), CD200R1, and CD200R2. While CD200 gives good binding to CD200R, it does not bind CD200RLa, CD200RLb, CD200RLc, or CD200RLe. For instance, CD200RLa has a 50-fold lower binding affinity to CD200, although CD200RLa shares a high amino acid sequence identity with CD200R in the V-like domain. Furthermore, the CD200-CD200R regulatory interactions provide an attractive target for immunomodulation, because its manipulation can provoke either immune tolerance or autoimmune diseases.


Pssm-ID: 409577  Cd Length: 107  Bit Score: 140.03  E-value: 3.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600065  67 EVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETkETNCTDERITWVSRPDQNSDLQIRTVA 146
Cdd:cd20985    2 EVNTTVSVQMGTKALLCCFSIPLTKAVLITWIIKLRGQPSCTIAYKVDTKET-ETSCLDRNITWASTPDHSPDLQISAVA 80

                         90       100
                 ....*....|....*....|....*..
gi 119600065 147 ITHDGYYRCIMVTPDGNFHRGYHLQVL 173
Cdd:cd20985   81 LQHEGTYSCEIVTPEGNFQKVYDLQVL 107
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 174-225 4.21e-04

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: 38.63  E-value: 4.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119600065 174 VTPEVTLFQNRNRTAVCKAVAGKPAAHISWIPE--GDCATKQEYWSNGTVTVKS 225
Cdd:cd05719    7 GGPALLIGGEPTLVATCISANGKPPASVTWETDlkGEASTTQVRGSNGTVTVTS 60
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 182-229 1.62e-03

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: 37.11  E-value: 1.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119600065 182 QNRNRTAVCKAVAGKPAAHISWipEGDC---ATKQEYWSNGTVTVKSTCHW 229
Cdd:cd07704   16 GNETLAASCTAETGKPAASVTW--ETDLggmESSRTFEHNRTATVTSEYHL 64
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 174-229 9.25e-03

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 34.70  E-value: 9.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119600065  174 VTPEVTLF--QNRNRTAVCKAVAGKPAAHISWI----PEGDCATKQEYWS-NGTVTVKSTCHW 229
Cdd:pfam08205   3 IEPPASLLegEGPEVVATCSSAGGKPAPRITWYldgkPLEAAETSSEQDPeSGLVTVTSELKL 65
 
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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