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Conserved domains on  [gi|194328798|ref|NP_001123664|]
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proline-rich nuclear receptor coactivator 2 [Danio rerio]

Protein Classification

proline-rich nuclear receptor coactivator motif-containing protein( domain architecture ID 10634043)

proline-rich nuclear receptor coactivator (PNRC) motif-containing protein; the PNRC family is composed of co-regulatory proteins for nuclear receptors

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PNRC pfam15365
Proline-rich nuclear receptor coactivator motif; The PNRC family, proline-rich nuclear ...
103-121 3.85e-04

Proline-rich nuclear receptor coactivator motif; The PNRC family, proline-rich nuclear receptor coactivator, is found in eukaryotes. Studies in S. pombe show that the proteins carrying this motif are mRNA decapping proteins. In addition, this motif is found in Saccharomyces cerevisiae two intrinsically disordered decapping enhancers Edc1 and Edc2, which show limited sequence conservation with human PNRC2. This motif in the N-terminal domain serves two purposes: it enhances the activity of the catalytic domain by recognizing part of the mRNA cap structure (i.e. activation motif), and secondly, it directly interacts with the decapping activator Dcp1. Mutation in the (YAG) sequence led to los of activity of activate the decapping complex. Hence the activity of the family members involved in mRNA processing mechanisms depends on YAG activation motif that is 11-13 residues N-terminal of a conserved LPxP Dcp1 interaction motif.


:

Pssm-ID: 464675  Cd Length: 19  Bit Score: 35.81  E-value: 3.85e-04
                          10
                  ....*....|....*....
gi 194328798  103 YAGAKFSEPPSPSVLPKPP 121
Cdd:pfam15365   1 YAGPAFSNSPEPSSLPIPS 19
 
Name Accession Description Interval E-value
PNRC pfam15365
Proline-rich nuclear receptor coactivator motif; The PNRC family, proline-rich nuclear ...
103-121 3.85e-04

Proline-rich nuclear receptor coactivator motif; The PNRC family, proline-rich nuclear receptor coactivator, is found in eukaryotes. Studies in S. pombe show that the proteins carrying this motif are mRNA decapping proteins. In addition, this motif is found in Saccharomyces cerevisiae two intrinsically disordered decapping enhancers Edc1 and Edc2, which show limited sequence conservation with human PNRC2. This motif in the N-terminal domain serves two purposes: it enhances the activity of the catalytic domain by recognizing part of the mRNA cap structure (i.e. activation motif), and secondly, it directly interacts with the decapping activator Dcp1. Mutation in the (YAG) sequence led to los of activity of activate the decapping complex. Hence the activity of the family members involved in mRNA processing mechanisms depends on YAG activation motif that is 11-13 residues N-terminal of a conserved LPxP Dcp1 interaction motif.


Pssm-ID: 464675  Cd Length: 19  Bit Score: 35.81  E-value: 3.85e-04
                          10
                  ....*....|....*....
gi 194328798  103 YAGAKFSEPPSPSVLPKPP 121
Cdd:pfam15365   1 YAGPAFSNSPEPSSLPIPS 19
 
Name Accession Description Interval E-value
PNRC pfam15365
Proline-rich nuclear receptor coactivator motif; The PNRC family, proline-rich nuclear ...
103-121 3.85e-04

Proline-rich nuclear receptor coactivator motif; The PNRC family, proline-rich nuclear receptor coactivator, is found in eukaryotes. Studies in S. pombe show that the proteins carrying this motif are mRNA decapping proteins. In addition, this motif is found in Saccharomyces cerevisiae two intrinsically disordered decapping enhancers Edc1 and Edc2, which show limited sequence conservation with human PNRC2. This motif in the N-terminal domain serves two purposes: it enhances the activity of the catalytic domain by recognizing part of the mRNA cap structure (i.e. activation motif), and secondly, it directly interacts with the decapping activator Dcp1. Mutation in the (YAG) sequence led to los of activity of activate the decapping complex. Hence the activity of the family members involved in mRNA processing mechanisms depends on YAG activation motif that is 11-13 residues N-terminal of a conserved LPxP Dcp1 interaction motif.


Pssm-ID: 464675  Cd Length: 19  Bit Score: 35.81  E-value: 3.85e-04
                          10
                  ....*....|....*....
gi 194328798  103 YAGAKFSEPPSPSVLPKPP 121
Cdd:pfam15365   1 YAGPAFSNSPEPSSLPIPS 19
 
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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