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Conserved domains on  [gi|270265874|ref|NP_001161753|]
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WW domain-containing transcription regulator protein 1 isoform 1 [Mus musculus]

Protein Classification

WW domain-containing protein( domain architecture ID 10648633)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY; similar to mammalian polyglutamine-binding protein 1, an intrinsically disordered protein that acts as a scaffold and is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development

CATH:  2.20.70.10
Gene Ontology:  GO:0005515
PubMed:  22201747|9029943
SCOP:  3001621

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
182-213 1.15e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 53.37  E-value: 1.15e-09
                           10        20        30
                   ....*....|....*....|....*....|..
gi 270265874   182 PLPPGWEMTFTATGQRYFLNHIEKITTWQDPR 213
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
 
Name Accession Description Interval E-value
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
182-213 1.15e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 53.37  E-value: 1.15e-09
                           10        20        30
                   ....*....|....*....|....*....|..
gi 270265874   182 PLPPGWEMTFTATGQRYFLNHIEKITTWQDPR 213
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
184-213 1.84e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 52.53  E-value: 1.84e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 270265874 184 PPGWEMTFTATGQRYFLNHIEKITTWQDPR 213
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
183-212 1.58e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 49.81  E-value: 1.58e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 270265874  183 LPPGWEMTFTATGQRYFLNHIEKITTWQDP 212
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
182-213 1.15e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 53.37  E-value: 1.15e-09
                           10        20        30
                   ....*....|....*....|....*....|..
gi 270265874   182 PLPPGWEMTFTATGQRYFLNHIEKITTWQDPR 213
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
184-213 1.84e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 52.53  E-value: 1.84e-09
                         10        20        30
                 ....*....|....*....|....*....|
gi 270265874 184 PPGWEMTFTATGQRYFLNHIEKITTWQDPR 213
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
183-212 1.58e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 49.81  E-value: 1.58e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 270265874  183 LPPGWEMTFTATGQRYFLNHIEKITTWQDP 212
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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