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Conserved domains on  [gi|119600066|gb|EAW79660|]
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CD200 receptor 1, isoform CRA_d, 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 ...
44-150 6.48e-44

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: 140.80  E-value: 6.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600066  44 EVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETkETNCTDERITWVSRPDQNSDLQIRTVA 123
Cdd:cd20985    2 EVNTTVSVQMGTKALLCCFSIPLTKAVLITWIIKLRGQPSCTIAYKVDTKET-ETSCLDRNITWASTPDHSPDLQISAVA 80
                         90       100
                 ....*....|....*....|....*..
gi 119600066 124 ITHDGYYRCIMVTPDGNFHRGYHLQVL 150
Cdd:cd20985   81 LQHEGTYSCEIVTPEGNFQKVYDLQVL 107
 
Name Accession Description Interval E-value
IgV_CD200R-like cd20985
Immunoglobulin Variable domain of cell surface glycoprotein CD200 receptor and similar ...
44-150 6.48e-44

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: 140.80  E-value: 6.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600066  44 EVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETkETNCTDERITWVSRPDQNSDLQIRTVA 123
Cdd:cd20985    2 EVNTTVSVQMGTKALLCCFSIPLTKAVLITWIIKLRGQPSCTIAYKVDTKET-ETSCLDRNITWASTPDHSPDLQISAVA 80
                         90       100
                 ....*....|....*....|....*..
gi 119600066 124 ITHDGYYRCIMVTPDGNFHRGYHLQVL 150
Cdd:cd20985   81 LQHEGTYSCEIVTPEGNFQKVYDLQVL 107
 
Name Accession Description Interval E-value
IgV_CD200R-like cd20985
Immunoglobulin Variable domain of cell surface glycoprotein CD200 receptor and similar ...
44-150 6.48e-44

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: 140.80  E-value: 6.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119600066  44 EVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETkETNCTDERITWVSRPDQNSDLQIRTVA 123
Cdd:cd20985    2 EVNTTVSVQMGTKALLCCFSIPLTKAVLITWIIKLRGQPSCTIAYKVDTKET-ETSCLDRNITWASTPDHSPDLQISAVA 80
                         90       100
                 ....*....|....*....|....*..
gi 119600066 124 ITHDGYYRCIMVTPDGNFHRGYHLQVL 150
Cdd:cd20985   81 LQHEGTYSCEIVTPEGNFQKVYDLQVL 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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