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Conserved domains on  [gi|2217318168|ref|XP_047293934|]
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serine/threonine-protein phosphatase 4 regulatory subunit 1 isoform X10 [Homo sapiens]

Protein Classification

WW-binding domain-containing protein( domain architecture ID 10633234)

WW-binding domain-containing protein similar to serine/threonine-protein phosphatase 4 regulatory subunit 1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WRNPLPNID pfam15017
Putative WW-binding domain and destruction box; This short conserved region is a putative ...
342-360 4.27e-04

Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain.


:

Pssm-ID: 464448  Cd Length: 56  Bit Score: 38.86  E-value: 4.27e-04
                          10
                  ....*....|....*....
gi 2217318168 342 YNSFHFWRTPLPEIDLDIE 360
Cdd:pfam15017   3 FNSFLFWRNPLPEIDLELE 21
 
Name Accession Description Interval E-value
WRNPLPNID pfam15017
Putative WW-binding domain and destruction box; This short conserved region is a putative ...
342-360 4.27e-04

Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain.


Pssm-ID: 464448  Cd Length: 56  Bit Score: 38.86  E-value: 4.27e-04
                          10
                  ....*....|....*....
gi 2217318168 342 YNSFHFWRTPLPEIDLDIE 360
Cdd:pfam15017   3 FNSFLFWRNPLPEIDLELE 21
 
Name Accession Description Interval E-value
WRNPLPNID pfam15017
Putative WW-binding domain and destruction box; This short conserved region is a putative ...
342-360 4.27e-04

Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain.


Pssm-ID: 464448  Cd Length: 56  Bit Score: 38.86  E-value: 4.27e-04
                          10
                  ....*....|....*....
gi 2217318168 342 YNSFHFWRTPLPEIDLDIE 360
Cdd:pfam15017   3 FNSFLFWRNPLPEIDLELE 21
 
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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