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Conserved domains on  [gi|1207160885|ref|XP_021324693|]
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E3 ubiquitin-protein ligase NEDD4-like isoform X7 [Danio rerio]

Protein Classification

WW domain-containing protein( domain architecture ID 11675138)

WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY; similar to Mus musculus membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2

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 ...
941-1270 1.52e-177

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: 526.80  E-value: 1.52e-177
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885   941 DSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1020
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1021 YHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLRFCIDEDN-FGQTYQVDLKPSGSDMV 1097
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1098 VTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHP 1177
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1178 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGTPD-KLPRAHTCFNRLDLPMYETFEDL 1256
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDeRLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1207160885  1257 REKLLMAVENAQGF 1270
Cdd:smart00119  315 REKLLLAINEGKGF 328
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
374-430 4.10e-25

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: 102.05  E-value: 4.10e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160885  374 NGQTRDDFLGQVDVPLTHLPTEDPAMERPYTFKDFLLRPRSHKSRVKGYLRLKMAYL 430
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
669-698 4.81e-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: 64.06  E-value: 4.81e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  669 LPPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
848-880 1.05e-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: 63.00  E-value: 1.05e-12
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1207160885   848 PLPPGWEERVHADGRTFYIDHNNKKTQWEDPRL 880
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
798-829 5.43e-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: 58.38  E-value: 5.43e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1207160885   798 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 829
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
473-499 3.16e-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: 53.28  E-value: 3.16e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160885  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
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 ...
941-1270 1.52e-177

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: 526.80  E-value: 1.52e-177
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885   941 DSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1020
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1021 YHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLRFCIDEDN-FGQTYQVDLKPSGSDMV 1097
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1098 VTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHP 1177
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1178 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGTPD-KLPRAHTCFNRLDLPMYETFEDL 1256
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDeRLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1207160885  1257 REKLLMAVENAQGF 1270
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
669-1270 1.59e-172

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.96  E-value: 1.59e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  669 LPPGWEERKDPKGRTYYVNHNNRSTTWTRPILQQhtEDGASTSVAAVGGataatppastpSTSSGHLSEP-QVRRPRSLS 747
Cdd:COG5021    299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEE--TLGESTSFLVVNN-----------DDSSSIKDLPhQVGSNPFLE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  748 SptvtlssplegannVPIRRAVKDTFSNpqspqpspysspktQHKANQSFLPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 827
Cdd:COG5021    366 A--------------HPEFSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  828 -RLKYPVHMR---TKASLD----PGDLGPLPPGWEERVHADGRTFYIDHNNKKTQWEDPRLQSPA--ITGPAVPYSREFK 897
Cdd:COG5021    418 rREQLGRESDesfYVASNVqqqrASREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKR 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  898 QKYDYFRKKLKKPADIPnrFEMKLHRNNIFEESYRRIMSlKRPDSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNP 977
Cdd:COG5021    498 RKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNP 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  978 YYGLFEYSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYN 1057
Cdd:COG5021    575 DYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYR 653
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1058 SLKWILEN--DPTELDLRFCIDEDNFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIP 1135
Cdd:COG5021    654 SLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIP 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1136 IDLIKIFDENELELLMCGLGD-VDVNDWRQHTVYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAE 1214
Cdd:COG5021    734 PDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKD 812
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160885 1215 LYGSNGPQLFTIEQWGTPDK-LPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGF 1270
Cdd:COG5021    813 LQGSDGVRKFTIEKGGTDDDrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
917-1271 3.79e-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: 505.95  E-value: 3.79e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  917 FEMKLHRNNIFEESYRRIMSLKRPDsLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 996
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  997 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLRF 1074
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1075 CIDEDN-FGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCG 1153
Cdd:cd00078    159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1154 LGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGTPD 1233
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPD 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1207160885 1234 -KLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1271
Cdd:cd00078    314 dRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
968-1271 4.45e-133

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 409.31  E-value: 4.45e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  968 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLN 1046
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1047 DMESVDSEYYNSLKWIL---ENDPTELDLRFCIDEdnFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQM 1123
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1124 NAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1203
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1204 TSRVPMNGFAELygsngpQLFTIEQWGT--PDKLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1271
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
374-430 4.10e-25

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: 102.05  E-value: 4.10e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160885  374 NGQTRDDFLGQVDVPLTHLPTEDPAMERPYTFKDFLLRPRSHKSRVKGYLRLKMAYL 430
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
669-698 4.81e-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: 64.06  E-value: 4.81e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  669 LPPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
848-880 1.05e-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: 63.00  E-value: 1.05e-12
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1207160885   848 PLPPGWEERVHADGRTFYIDHNNKKTQWEDPRL 880
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
668-698 3.93e-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: 61.46  E-value: 3.93e-12
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1207160885   668 GLPPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
850-880 5.10e-12

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: 61.00  E-value: 5.10e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207160885  850 PPGWEERVHADGRTFYIDHNNKKTQWEDPRL 880
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
849-878 7.77e-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: 60.60  E-value: 7.77e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  849 LPPGWEERVHADGRTFYIDHNNKKTQWEDP 878
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
670-698 1.25e-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: 60.23  E-value: 1.25e-11
                           10        20
                   ....*....|....*....|....*....
gi 1207160885  670 PPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
798-829 5.43e-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: 58.38  E-value: 5.43e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1207160885   798 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 829
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
799-829 5.69e-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: 58.31  E-value: 5.69e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207160885  799 PPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 829
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
798-827 1.15e-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: 57.13  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  798 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 827
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
473-499 3.16e-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: 53.28  E-value: 3.16e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160885  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
473-499 6.58e-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: 6.58e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160885  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
473-501 6.03e-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: 49.52  E-value: 6.03e-08
                            10        20
                    ....*....|....*....|....*....
gi 1207160885   473 GWEEKVDNLGRTYYVNHNNRTTQWKRPSS 501
Cdd:smart00456    5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
941-1270 1.52e-177

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: 526.80  E-value: 1.52e-177
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885   941 DSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1020
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1021 YHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLRFCIDEDN-FGQTYQVDLKPSGSDMV 1097
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1098 VTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHP 1177
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  1178 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGTPD-KLPRAHTCFNRLDLPMYETFEDL 1256
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDeRLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1207160885  1257 REKLLMAVENAQGF 1270
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
669-1270 1.59e-172

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.96  E-value: 1.59e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  669 LPPGWEERKDPKGRTYYVNHNNRSTTWTRPILQQhtEDGASTSVAAVGGataatppastpSTSSGHLSEP-QVRRPRSLS 747
Cdd:COG5021    299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEE--TLGESTSFLVVNN-----------DDSSSIKDLPhQVGSNPFLE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  748 SptvtlssplegannVPIRRAVKDTFSNpqspqpspysspktQHKANQSFLPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 827
Cdd:COG5021    366 A--------------HPEFSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  828 -RLKYPVHMR---TKASLD----PGDLGPLPPGWEERVHADGRTFYIDHNNKKTQWEDPRLQSPA--ITGPAVPYSREFK 897
Cdd:COG5021    418 rREQLGRESDesfYVASNVqqqrASREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKR 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  898 QKYDYFRKKLKKPADIPnrFEMKLHRNNIFEESYRRIMSlKRPDSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNP 977
Cdd:COG5021    498 RKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNP 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  978 YYGLFEYSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYN 1057
Cdd:COG5021    575 DYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYR 653
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1058 SLKWILEN--DPTELDLRFCIDEDNFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIP 1135
Cdd:COG5021    654 SLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIP 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1136 IDLIKIFDENELELLMCGLGD-VDVNDWRQHTVYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAE 1214
Cdd:COG5021    734 PDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKD 812
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160885 1215 LYGSNGPQLFTIEQWGTPDK-LPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGF 1270
Cdd:COG5021    813 LQGSDGVRKFTIEKGGTDDDrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
917-1271 3.79e-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: 505.95  E-value: 3.79e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  917 FEMKLHRNNIFEESYRRIMSLKRPDsLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 996
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  997 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLRF 1074
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1075 CIDEDN-FGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCG 1153
Cdd:cd00078    159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1154 LGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGTPD 1233
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPD 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1207160885 1234 -KLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1271
Cdd:cd00078    314 dRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
968-1271 4.45e-133

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 409.31  E-value: 4.45e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885  968 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLN 1046
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1047 DMESVDSEYYNSLKWIL---ENDPTELDLRFCIDEdnFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQM 1123
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1124 NAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1203
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160885 1204 TSRVPMNGFAELygsngpQLFTIEQWGT--PDKLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1271
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
374-430 4.10e-25

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: 102.05  E-value: 4.10e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160885  374 NGQTRDDFLGQVDVPLTHLPTEDPAMERPYTFKDFLLRPRSHKSRVKGYLRLKMAYL 430
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
669-698 4.81e-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: 64.06  E-value: 4.81e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  669 LPPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
848-880 1.05e-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: 63.00  E-value: 1.05e-12
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1207160885   848 PLPPGWEERVHADGRTFYIDHNNKKTQWEDPRL 880
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
668-698 3.93e-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: 61.46  E-value: 3.93e-12
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1207160885   668 GLPPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
850-880 5.10e-12

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: 61.00  E-value: 5.10e-12
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207160885  850 PPGWEERVHADGRTFYIDHNNKKTQWEDPRL 880
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
849-878 7.77e-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: 60.60  E-value: 7.77e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  849 LPPGWEERVHADGRTFYIDHNNKKTQWEDP 878
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
670-698 1.25e-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: 60.23  E-value: 1.25e-11
                           10        20
                   ....*....|....*....|....*....
gi 1207160885  670 PPGWEERKDPKGRTYYVNHNNRSTTWTRP 698
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
798-829 5.43e-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: 58.38  E-value: 5.43e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1207160885   798 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 829
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
799-829 5.69e-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: 58.31  E-value: 5.69e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207160885  799 PPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 829
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
798-827 1.15e-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: 57.13  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160885  798 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 827
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
473-499 3.16e-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: 53.28  E-value: 3.16e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160885  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
473-499 6.58e-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: 6.58e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160885  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
473-501 6.03e-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: 49.52  E-value: 6.03e-08
                            10        20
                    ....*....|....*....|....*....
gi 1207160885   473 GWEEKVDNLGRTYYVNHNNRTTQWKRPSS 501
Cdd:smart00456    5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
 
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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