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Conserved domains on  [gi|755561451|ref|XP_011245346|]
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E3 ubiquitin-protein ligase NEDD4-like isoform X18 [Mus musculus]

Protein Classification

WW domain-containing protein( domain architecture ID 11675104)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY; similar to mammalian Yes-associated protein 1 (YAP1) which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
522-851 5.80e-178

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


:

Pssm-ID: 214523  Cd Length: 328  Bit Score: 515.25  E-value: 5.80e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   522 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 601
Cdd:smart00119   1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   602 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 678
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   679 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 758
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   759 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 837
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 755561451   838 REKLLMAVENAQGF 851
Cdd:smart00119 315 REKLLLAINEGKGF 328
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
267-296 2.38e-12

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: 61.75  E-value: 2.38e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  267 LPSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
380-410 1.18e-11

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: 59.85  E-value: 1.18e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755561451 380 PPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 410
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
1-32 2.05e-11

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd04033:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 133  Bit Score: 62.37  E-value: 2.05e-11
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755561451   1 MERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 32
Cdd:cd04033  102 NERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
429-461 5.91e-11

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: 57.61  E-value: 5.91e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 755561451   429 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 461
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
77-103 4.90e-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: 52.12  E-value: 4.90e-09
                          10        20
                  ....*....|....*....|....*..
gi 755561451   77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
522-851 5.80e-178

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 515.25  E-value: 5.80e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   522 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 601
Cdd:smart00119   1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   602 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 678
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   679 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 758
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   759 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 837
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 755561451   838 REKLLMAVENAQGF 851
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
267-851 4.95e-173

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 522.79  E-value: 4.95e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 267 LPSGWEERKDAKGRTYYVNHNNRTTTWTRPImqlaedgASGSATNSNNHLVEPQIRRPRSLSSPTVTLSAPLEgaKDSPI 346
Cdd:COG5021  299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPL-------LEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFL--EAHPE 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 347 RRAVKDTLSNpqspqpspynspkpQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDP-RLKFPVHMRSKASLNPN 425
Cdd:COG5021  370 FSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLrREQLGRESDESFYVASN 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 426 -------DLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPA--ITGPAVPYSREFKQKYDYFRKKLKKPADIPn 496
Cdd:COG5021  436 vqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY- 514
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 497 rFEMKLHRNNIFEESYRRIMSvKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQIN 576
Cdd:COG5021  515 -LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPIN 592
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 577 PNSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILEN--DPTELDLM 654
Cdd:COG5021  593 PLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNdiDETILDLT 671
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 655 FCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 734
Cdd:COG5021  672 FTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGG 751
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 735 LGD-VDVNDWRQHSIYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSP 813
Cdd:COG5021  752 IPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTD 830
                        570       580       590
                 ....*....|....*....|....*....|....*....
gi 755561451 814 -EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGF 851
Cdd:COG5021  831 dDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
498-852 1.42e-169

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 494.78  E-value: 1.42e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 498 FEMKLHRNNIFEESYRRIMSVKRPDvLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 577
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 578 NSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLMF 655
Cdd:cd00078   80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 656 CIDEEN-FGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 734
Cdd:cd00078  159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 735 LGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGSP- 813
Cdd:cd00078  239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 755561451 814 EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 852
Cdd:cd00078  314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
549-852 2.79e-134

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 402.37  E-value: 2.79e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  549 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLN 627
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  628 DMESVDSEYYNSLKWIL---ENDPTELDLMFCIDEenFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQM 704
Cdd:pfam00632  81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  705 NAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 784
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  785 TSRVPMNGFAELygsngpQLFTIEQWGS--PEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 852
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
267-296 2.38e-12

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: 61.75  E-value: 2.38e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  267 LPSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
266-296 5.62e-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: 60.69  E-value: 5.62e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 755561451   266 GLPSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
380-410 1.18e-11

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: 59.85  E-value: 1.18e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755561451 380 PPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 410
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
379-408 1.42e-11

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: 59.44  E-value: 1.42e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  379 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDP 408
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
379-410 1.43e-11

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: 59.54  E-value: 1.43e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 755561451   379 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 410
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
268-296 1.53e-11

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: 59.46  E-value: 1.53e-11
                         10        20
                 ....*....|....*....|....*....
gi 755561451 268 PSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
1-32 2.05e-11

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 62.37  E-value: 2.05e-11
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755561451   1 MERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 32
Cdd:cd04033  102 NERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
429-461 5.91e-11

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: 57.61  E-value: 5.91e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 755561451   429 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 461
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
431-461 2.14e-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: 56.00  E-value: 2.14e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755561451 431 PPGWEERIHLDGRTFYIDHNSKITQWEDPRL 461
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
430-459 3.74e-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: 55.20  E-value: 3.74e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  430 LPPGWEERIHLDGRTFYIDHNSKITQWEDP 459
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
77-103 4.90e-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: 52.12  E-value: 4.90e-09
                          10        20
                  ....*....|....*....|....*..
gi 755561451   77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
77-103 3.33e-08

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: 49.83  E-value: 3.33e-08
                         10        20
                 ....*....|....*....|....*..
gi 755561451  77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:cd00201    3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
77-103 8.71e-08

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: 48.75  E-value: 8.71e-08
                           10        20
                   ....*....|....*....|....*..
gi 755561451    77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:smart00456   5 GWEERKDPDGRPYYYNHETKETQWEKP 31
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
522-851 5.80e-178

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 515.25  E-value: 5.80e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   522 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 601
Cdd:smart00119   1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   602 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 678
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   679 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 758
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451   759 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 837
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                          330
                   ....*....|....
gi 755561451   838 REKLLMAVENAQGF 851
Cdd:smart00119 315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
267-851 4.95e-173

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 522.79  E-value: 4.95e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 267 LPSGWEERKDAKGRTYYVNHNNRTTTWTRPImqlaedgASGSATNSNNHLVEPQIRRPRSLSSPTVTLSAPLEgaKDSPI 346
Cdd:COG5021  299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPL-------LEETLGESTSFLVVNNDDSSSIKDLPHQVGSNPFL--EAHPE 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 347 RRAVKDTLSNpqspqpspynspkpQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDP-RLKFPVHMRSKASLNPN 425
Cdd:COG5021  370 FSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLrREQLGRESDESFYVASN 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 426 -------DLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPA--ITGPAVPYSREFKQKYDYFRKKLKKPADIPn 496
Cdd:COG5021  436 vqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY- 514
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 497 rFEMKLHRNNIFEESYRRIMSvKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQIN 576
Cdd:COG5021  515 -LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPIN 592
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 577 PNSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILEN--DPTELDLM 654
Cdd:COG5021  593 PLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNdiDETILDLT 671
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 655 FCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 734
Cdd:COG5021  672 FTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGG 751
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 735 LGD-VDVNDWRQHSIYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSP 813
Cdd:COG5021  752 IPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTD 830
                        570       580       590
                 ....*....|....*....|....*....|....*....
gi 755561451 814 -EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGF 851
Cdd:COG5021  831 dDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
498-852 1.42e-169

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 494.78  E-value: 1.42e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 498 FEMKLHRNNIFEESYRRIMSVKRPDvLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 577
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 578 NSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLMF 655
Cdd:cd00078   80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 656 CIDEEN-FGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 734
Cdd:cd00078  159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451 735 LGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGSP- 813
Cdd:cd00078  239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 755561451 814 EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 852
Cdd:cd00078  314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
549-852 2.79e-134

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 402.37  E-value: 2.79e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  549 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLN 627
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  628 DMESVDSEYYNSLKWIL---ENDPTELDLMFCIDEenFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQM 704
Cdd:pfam00632  81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  705 NAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 784
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755561451  785 TSRVPMNGFAELygsngpQLFTIEQWGS--PEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 852
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
267-296 2.38e-12

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: 61.75  E-value: 2.38e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  267 LPSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
266-296 5.62e-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: 60.69  E-value: 5.62e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 755561451   266 GLPSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
380-410 1.18e-11

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: 59.85  E-value: 1.18e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755561451 380 PPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 410
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
379-408 1.42e-11

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: 59.44  E-value: 1.42e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  379 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDP 408
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
379-410 1.43e-11

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: 59.54  E-value: 1.43e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 755561451   379 LPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRL 410
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
268-296 1.53e-11

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: 59.46  E-value: 1.53e-11
                         10        20
                 ....*....|....*....|....*....
gi 755561451 268 PSGWEERKDAKGRTYYVNHNNRTTTWTRP 296
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
1-32 2.05e-11

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 62.37  E-value: 2.05e-11
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755561451   1 MERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 32
Cdd:cd04033  102 NERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
429-461 5.91e-11

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: 57.61  E-value: 5.91e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 755561451   429 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 461
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
431-461 2.14e-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: 56.00  E-value: 2.14e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755561451 431 PPGWEERIHLDGRTFYIDHNSKITQWEDPRL 461
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
430-459 3.74e-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: 55.20  E-value: 3.74e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 755561451  430 LPPGWEERIHLDGRTFYIDHNSKITQWEDP 459
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
77-103 4.90e-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: 52.12  E-value: 4.90e-09
                          10        20
                  ....*....|....*....|....*..
gi 755561451   77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
77-103 3.33e-08

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: 49.83  E-value: 3.33e-08
                         10        20
                 ....*....|....*....|....*..
gi 755561451  77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:cd00201    3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
77-103 8.71e-08

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: 48.75  E-value: 8.71e-08
                           10        20
                   ....*....|....*....|....*..
gi 755561451    77 GWEEKVDNLGRTYYVNHNNRSTQWHRP 103
Cdd:smart00456   5 GWEERKDPDGRPYYYNHETKETQWEKP 31
 
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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