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Conserved domains on  [gi|568965387|ref|XP_006512792|]
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interleukin-20 receptor subunit alpha isoform X2 [Mus musculus]

Protein Classification

Interfer-bind domain-containing protein( domain architecture ID 10558174)

Interfer-bind domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Interfer-bind pfam09294
Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary ...
4-108 1.06e-21

Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary structure consisting of seven beta-strands arranged in an immunoglobulin-like beta-sandwich, in a Greek-key topology. They are required for binding to interferon-alpha.


:

Pssm-ID: 462746  Cd Length: 103  Bit Score: 88.94  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965387    4 AQVSPPEVALTTGEKSISIALTAPEKWKRNPqdhtVSMQQIYPNLKYNVSVYNTKS-RRTWSQCVTNSTLVLSWLEPNTL 82
Cdd:pfam09294   1 TIIGPPEVELEVEGGSLNVTVKDPETREGKN----LSLRDLYGSLQYRVSYWKNSSnGEKKNTTSTNSFVVLSDLEPGTT 76
                          90       100
                  ....*....|....*....|....*.
gi 568965387   83 YCVHVESLVPGPPRLPMPSQKQCIST 108
Cdd:pfam09294  77 YCVSVQAFSPLDNKSSQRSPPQCIRT 102
 
Name Accession Description Interval E-value
Interfer-bind pfam09294
Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary ...
4-108 1.06e-21

Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary structure consisting of seven beta-strands arranged in an immunoglobulin-like beta-sandwich, in a Greek-key topology. They are required for binding to interferon-alpha.


Pssm-ID: 462746  Cd Length: 103  Bit Score: 88.94  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965387    4 AQVSPPEVALTTGEKSISIALTAPEKWKRNPqdhtVSMQQIYPNLKYNVSVYNTKS-RRTWSQCVTNSTLVLSWLEPNTL 82
Cdd:pfam09294   1 TIIGPPEVELEVEGGSLNVTVKDPETREGKN----LSLRDLYGSLQYRVSYWKNSSnGEKKNTTSTNSFVVLSDLEPGTT 76
                          90       100
                  ....*....|....*....|....*.
gi 568965387   83 YCVHVESLVPGPPRLPMPSQKQCIST 108
Cdd:pfam09294  77 YCVSVQAFSPLDNKSSQRSPPQCIRT 102
 
Name Accession Description Interval E-value
Interfer-bind pfam09294
Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary ...
4-108 1.06e-21

Interferon-alpha/beta receptor, fibronectin type III; Members of this family adopt a secondary structure consisting of seven beta-strands arranged in an immunoglobulin-like beta-sandwich, in a Greek-key topology. They are required for binding to interferon-alpha.


Pssm-ID: 462746  Cd Length: 103  Bit Score: 88.94  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965387    4 AQVSPPEVALTTGEKSISIALTAPEKWKRNPqdhtVSMQQIYPNLKYNVSVYNTKS-RRTWSQCVTNSTLVLSWLEPNTL 82
Cdd:pfam09294   1 TIIGPPEVELEVEGGSLNVTVKDPETREGKN----LSLRDLYGSLQYRVSYWKNSSnGEKKNTTSTNSFVVLSDLEPGTT 76
                          90       100
                  ....*....|....*....|....*.
gi 568965387   83 YCVHVESLVPGPPRLPMPSQKQCIST 108
Cdd:pfam09294  77 YCVSVQAFSPLDNKSSQRSPPQCIRT 102
 
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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