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Conserved domains on  [gi|384475575|ref|NP_001244973|]
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heat shock factor-binding protein 1 [Macaca mulatta]

Protein Classification

heat shock factor-binding 1 family protein( domain architecture ID 10536259)

heat shock factor-binding 1 (HSBP1) family protein similar to human HSBP1, a regulator of heat shock response that negatively affects HSF1 DNA-binding activity and may have a role in the suppression of the activation of the stress response during the aging process

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSBP1 pfam06825
Heat shock factor binding protein 1; Heat shock factor binding protein 1 (HSBP1) appears to be ...
 10-60 4.79e-24

Heat shock factor binding protein 1; Heat shock factor binding protein 1 (HSBP1) appears to be a negative regulator of the heat shock response.


:

Pssm-ID: 429139  Cd Length: 51  Bit Score: 84.87  E-value: 4.79e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384475575  10 QDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAG 60
Cdd:pfam06825  1 QELTAFVENLLQQLQDKFQTMSDQILGRIDEMGSRIDDLEKSIADLMTQAG 51
 
Name Accession Description Interval E-value
HSBP1 pfam06825
Heat shock factor binding protein 1; Heat shock factor binding protein 1 (HSBP1) appears to be ...
 10-60 4.79e-24

Heat shock factor binding protein 1; Heat shock factor binding protein 1 (HSBP1) appears to be a negative regulator of the heat shock response.


Pssm-ID: 429139  Cd Length: 51  Bit Score: 84.87  E-value: 4.79e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384475575  10 QDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAG 60
Cdd:pfam06825  1 QELTAFVENLLQQLQDKFQTMSDQILGRIDEMGSRIDDLEKSIADLMTQAG 51
PRK14559 PRK14559
serine/threonine phosphatase;
6-76 9.09e-03

serine/threonine phosphatase;


Pssm-ID: 237756 [Multi-domain]  Cd Length: 645  Bit Score: 32.72  E-value: 9.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384475575   6 PKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDdmSSRIDDLEKNIADLMTQAGVEELEGENKIPATQKS 76
Cdd:PRK14559 272 PPSLQDLGQVWQQLFTQSQRTQFESLIPLLQDLQ--SGKIQTIAQLRLRLQELATELEAEGEAEFESTEGE 340
 
Name Accession Description Interval E-value
HSBP1 pfam06825
Heat shock factor binding protein 1; Heat shock factor binding protein 1 (HSBP1) appears to be ...
 10-60 4.79e-24

Heat shock factor binding protein 1; Heat shock factor binding protein 1 (HSBP1) appears to be a negative regulator of the heat shock response.


Pssm-ID: 429139  Cd Length: 51  Bit Score: 84.87  E-value: 4.79e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384475575  10 QDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAG 60
Cdd:pfam06825  1 QELTAFVENLLQQLQDKFQTMSDQILGRIDEMGSRIDDLEKSIADLMTQAG 51
PRK14559 PRK14559
serine/threonine phosphatase;
6-76 9.09e-03

serine/threonine phosphatase;


Pssm-ID: 237756 [Multi-domain]  Cd Length: 645  Bit Score: 32.72  E-value: 9.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384475575   6 PKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDdmSSRIDDLEKNIADLMTQAGVEELEGENKIPATQKS 76
Cdd:PRK14559 272 PPSLQDLGQVWQQLFTQSQRTQFESLIPLLQDLQ--SGKIQTIAQLRLRLQELATELEAEGEAEFESTEGE 340
 
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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