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Conserved domains on  [gi|303523511|ref|NP_006097|]
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transcriptional coactivator YAP1 isoform 2 [Homo sapiens]

Protein Classification

WW domain-containing protein( domain architecture ID 10078122)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY

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 cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
174-203 1.74e-10

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: 55.61  E-value: 1.74e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 303523511 174 PAGWEMAKTSSGQRYFLNHIDQTTTWQDPR 203
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
 
Name Accession Description Interval E-value
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
174-203 1.74e-10

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: 55.61  E-value: 1.74e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 303523511 174 PAGWEMAKTSSGQRYFLNHIDQTTTWQDPR 203
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
172-203 2.01e-10

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: 55.30  E-value: 2.01e-10
                           10        20        30
                   ....*....|....*....|....*....|..
gi 303523511   172 PLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPR 203
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
173-202 3.50e-09

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 51.74  E-value: 3.50e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 303523511  173 LPAGWEMAKTSSGQRYFLNHIDQTTTWQDP 202
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
174-203 1.74e-10

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: 55.61  E-value: 1.74e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 303523511 174 PAGWEMAKTSSGQRYFLNHIDQTTTWQDPR 203
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
172-203 2.01e-10

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: 55.30  E-value: 2.01e-10
                           10        20        30
                   ....*....|....*....|....*....|..
gi 303523511   172 PLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPR 203
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
173-202 3.50e-09

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 51.74  E-value: 3.50e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 303523511  173 LPAGWEMAKTSSGQRYFLNHIDQTTTWQDP 202
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
 
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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