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Conserved domains on  [gi|221468529|ref|NP_726414|]
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yorkie, isoform G [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 ...
 243-272 4.63e-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: 4.63e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 221468529  243 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 312-341 5.96e-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: 5.96e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 221468529  312 LPDGWEQAVTESGDLYFINHIDRTTSWNDP 341
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
HUL4 super family cl34867
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
238-381 4.65e-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: 48.61  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468529 238 RQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIqyrqqqqilmAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWE 317
Cdd:COG5021  383 RDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRR----------EQLGRESDESFYVASNVQQQRASREGPLLSGWK 452

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221468529 318 QAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPdnlvsSLQIEDNLCSNLFN---DAQAIVNPP 381
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 ...
 243-272 4.63e-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: 4.63e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 221468529  243 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 244-272 5.85e-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: 5.85e-13
                         10        20
                 ....*....|....*....|....*....
gi 221468529 244 PPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 243-272 1.70e-12

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: 61.08  E-value: 1.70e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 221468529   243 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 312-341 5.96e-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: 5.96e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 221468529  312 LPDGWEQAVTESGDLYFINHIDRTTSWNDP 341
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 313-343 2.46e-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: 2.46e-09
                         10        20        30
                 ....*....|....*....|....*....|.
gi 221468529 313 PDGWEQAVTESGDLYFINHIDRTTSWNDPRM 343
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 311-343 9.12e-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: 50.68  E-value: 9.12e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 221468529   311 PLPDGWEQAVTESGDLYFINHIDRTTSWNDPRM 343
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PRP40 COG5104
Splicing factor [RNA processing and modification];
247-341 3.81e-07

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 52.00  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468529 247 WEQAKTNDGQIYYLNHTTKSTQWEDPRiqyrqqqqilmaERIKQNDVLQTTkqtttstiannlgplpDGWEQAVTESGDL 326
Cdd:COG5104   17 WEELKAPDGRIYYYNKRTGKSSWEKPK------------ELLKGSEEDLDV----------------DPWKECRTADGKV 68

                         90
                 ....*....|....*
gi 221468529 327 YFINHIDRTTSWNDP 341
Cdd:COG5104   69 YYYNSITRESRWKIP 83
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
238-381 4.65e-06

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 48.61  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468529 238 RQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIqyrqqqqilmAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWE 317
Cdd:COG5021  383 RDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRR----------EQLGRESDESFYVASNVQQQRASREGPLLSGWK 452

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221468529 318 QAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPdnlvsSLQIEDNLCSNLFN---DAQAIVNPP 381
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 ...
 243-272 4.63e-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: 4.63e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 221468529  243 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 244-272 5.85e-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: 5.85e-13
                         10        20
                 ....*....|....*....|....*....
gi 221468529 244 PPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 243-272 1.70e-12

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: 61.08  E-value: 1.70e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 221468529   243 LPPGWEQAKTNDGQIYYLNHTTKSTQWEDP 272
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 312-341 5.96e-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: 5.96e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 221468529  312 LPDGWEQAVTESGDLYFINHIDRTTSWNDP 341
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 313-343 2.46e-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: 2.46e-09
                         10        20        30
                 ....*....|....*....|....*....|.
gi 221468529 313 PDGWEQAVTESGDLYFINHIDRTTSWNDPRM 343
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 311-343 9.12e-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: 50.68  E-value: 9.12e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 221468529   311 PLPDGWEQAVTESGDLYFINHIDRTTSWNDPRM 343
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PRP40 COG5104
Splicing factor [RNA processing and modification];
247-341 3.81e-07

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 52.00  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468529 247 WEQAKTNDGQIYYLNHTTKSTQWEDPRiqyrqqqqilmaERIKQNDVLQTTkqtttstiannlgplpDGWEQAVTESGDL 326
Cdd:COG5104   17 WEELKAPDGRIYYYNKRTGKSSWEKPK------------ELLKGSEEDLDV----------------DPWKECRTADGKV 68

                         90
                 ....*....|....*
gi 221468529 327 YFINHIDRTTSWNDP 341
Cdd:COG5104   69 YYYNSITRESRWKIP 83
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
238-381 4.65e-06

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 48.61  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468529 238 RQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIqyrqqqqilmAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWE 317
Cdd:COG5021  383 RDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRR----------EQLGRESDESFYVASNVQQQRASREGPLLSGWK 452

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221468529 318 QAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPdnlvsSLQIEDNLCSNLFN---DAQAIVNPP 381
Cdd:COG5021  453 TRLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLD-----IRRIKEDKRRKLFYslkQKAKIFDPY 514
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
239-363 8.55e-05

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 44.76  E-value: 8.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468529 239 QLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIQYrqqqqiLMAERIKQNDVLQTTKQTTTSTIANNLGP------- 311
Cdd:COG5021  295 SLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEE------TLGESTSFLVVNNDDSSSIKDLPHQVGSNpfleahp 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221468529 312 -------------------LPDGWEQAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPDNLVSSLQIE 363
Cdd:COG5021  369 efsellknqsrgttrdfrnKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLGRESDESFYVASNVQQQ 439
 
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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