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Conserved domains on  [gi|1394193569|ref|NP_001350857|]
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yorkie, isoform H [Drosophila melanogaster]

Protein Classification

WW domain-containing protein( domain architecture ID 10449603)

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|7641887

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 266-295 4.96e-13

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: 62.52  E-value: 4.96e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1394193569 266 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 335-364 6.31e-10

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: 54.05  E-value: 6.31e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 1394193569 335 LPDGWEQAVTESGDLYFINHIDRTTSWNDP 364
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
HUL4 super family cl34867
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
261-404 5.12e-06

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5021:

Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 48.99  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394193569 261 RQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPriqyrqqqqiLMAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWE 340
Cdd:COG5021   383 RDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL----------RREQLGRESDESFYVASNVQQQRASREGPLLSGWK 452

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394193569 341 QAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPdnlvsSLQIEDNLCSNLFN---DAQAIVNPP 404
Cdd:COG5021   453 TRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLD-----IRRIKEDKRRKLFYslkQKAKIFDPY 514
 
Name Accession Description Interval E-value
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 266-295 4.96e-13

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: 62.52  E-value: 4.96e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1394193569 266 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 267-295 5.90e-13

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: 62.55  E-value: 5.90e-13
                          10        20
                  ....*....|....*....|....*....
gi 1394193569 267 PPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 266-295 9.43e-13

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: 61.85  E-value: 9.43e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1394193569  266 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 335-364 6.31e-10

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: 54.05  E-value: 6.31e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 1394193569 335 LPDGWEQAVTESGDLYFINHIDRTTSWNDP 364
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 336-366 2.55e-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: 52.14  E-value: 2.55e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1394193569 336 PDGWEQAVTESGDLYFINHIDRTTSWNDPRM 366
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 334-366 5.57e-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: 51.45  E-value: 5.57e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1394193569  334 PLPDGWEQAVTESGDLYFINHIDRTTSWNDPRM 366
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PRP40 COG5104
Splicing factor [RNA processing and modification];
270-364 2.41e-07

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 52.78  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394193569 270 WEQAKTNDGQIYYLNHTTKSTQWEDPRiqyrqqqqilmaERIKQNDVLQTTkqtttstiannlgplpDGWEQAVTESGDL 349
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPK------------ELLKGSEEDLDV----------------DPWKECRTADGKV 68

                          90
                  ....*....|....*
gi 1394193569 350 YFINHIDRTTSWNDP 364
Cdd:COG5104    69 YYYNSITRESRWKIP 83
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
261-404 5.12e-06

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 48.99  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394193569 261 RQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPriqyrqqqqiLMAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWE 340
Cdd:COG5021   383 RDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL----------RREQLGRESDESFYVASNVQQQRASREGPLLSGWK 452

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394193569 341 QAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPdnlvsSLQIEDNLCSNLFN---DAQAIVNPP 404
Cdd:COG5021   453 TRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLD-----IRRIKEDKRRKLFYslkQKAKIFDPY 514
 
Name Accession Description Interval E-value
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 266-295 4.96e-13

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: 62.52  E-value: 4.96e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1394193569 266 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 267-295 5.90e-13

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: 62.55  E-value: 5.90e-13
                          10        20
                  ....*....|....*....|....*....
gi 1394193569 267 PPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 266-295 9.43e-13

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: 61.85  E-value: 9.43e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1394193569  266 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 335-364 6.31e-10

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: 54.05  E-value: 6.31e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 1394193569 335 LPDGWEQAVTESGDLYFINHIDRTTSWNDP 364
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 336-366 2.55e-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: 52.14  E-value: 2.55e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1394193569 336 PDGWEQAVTESGDLYFINHIDRTTSWNDPRM 366
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 334-366 5.57e-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: 51.45  E-value: 5.57e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1394193569  334 PLPDGWEQAVTESGDLYFINHIDRTTSWNDPRM 366
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PRP40 COG5104
Splicing factor [RNA processing and modification];
270-364 2.41e-07

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 52.78  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394193569 270 WEQAKTNDGQIYYLNHTTKSTQWEDPRiqyrqqqqilmaERIKQNDVLQTTkqtttstiannlgplpDGWEQAVTESGDL 349
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPK------------ELLKGSEEDLDV----------------DPWKECRTADGKV 68

                          90
                  ....*....|....*
gi 1394193569 350 YFINHIDRTTSWNDP 364
Cdd:COG5104    69 YYYNSITRESRWKIP 83
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
261-404 5.12e-06

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 48.99  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394193569 261 RQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPriqyrqqqqiLMAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWE 340
Cdd:COG5021   383 RDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL----------RREQLGRESDESFYVASNVQQQRASREGPLLSGWK 452

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394193569 341 QAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPdnlvsSLQIEDNLCSNLFN---DAQAIVNPP 404
Cdd:COG5021   453 TRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLD-----IRRIKEDKRRKLFYslkQKAKIFDPY 514
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
262-386 1.01e-04

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 44.76  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394193569 262 QLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIQYrqqqqiLMAERIKQNDVLQTTKQTTTSTIANNLGP------- 334
Cdd:COG5021   295 SLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEE------TLGESTSFLVVNNDDSSSIKDLPHQVGSNpfleahp 368

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394193569 335 -------------------LPDGWEQAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPDNLVSSLQIE 386
Cdd:COG5021   369 efsellknqsrgttrdfrnKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLGRESDESFYVASNVQQQ 439
PRP40 COG5104
Splicing factor [RNA processing and modification];
269-295 8.48e-03

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 38.52  E-value: 8.48e-03
                          10        20
                  ....*....|....*....|....*..
gi 1394193569 269 GWEQAKTNDGQIYYLNHTTKSTQWEDP 295
Cdd:COG5104    57 PWKECRTADGKVYYYNSITRESRWKIP 83
 
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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