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Conserved domains on  [gi|547234945|ref|NP_001271267|]
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E3 ubiquitin-protein ligase NEDD4 isoform 3 [Homo sapiens]

Protein Classification

WW domain-containing protein( domain architecture ID 11675221)

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 ...
986-1315 0e+00

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: 554.54  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945    986 DFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1065
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1066 YHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWI-LENDPTE-LDLRF-IIDEELFGQTHQHELKNGGSEIV 1142
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1143 VTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQ 1222
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1223 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGsngpqSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEEL 1301
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 547234945   1302 WDKLQMAIENTQGF 1315
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 ...
517-570 2.09e-24

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: 100.12  E-value: 2.09e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 547234945  517 TRDDFLGQVDVPLYPLPTENPRLERPYTFKDFVLHPRSHKSRVKGYLRLKMTYL 570
Cdd:cd04033    80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
893-925 2.47e-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: 62.23  E-value: 2.47e-12
                            10        20        30
                    ....*....|....*....|....*....|...
gi 547234945    893 PLPPGWEERTHTDGRIFYINHNIKRTQWEDPRL 925
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
769-798 1.49e-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: 59.83  E-value: 1.49e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   769 LPPGWEEKQDERGRSYYVDHNSRTTTWTKP 798
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
611-643 2.08e-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: 2.08e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 547234945    611 PLPPGWEERQDILGRTYYVNHESRRTQWKRPTP 643
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
842-871 4.85e-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: 58.29  E-value: 4.85e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   842 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 871
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
986-1315 0e+00

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: 554.54  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945    986 DFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1065
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1066 YHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWI-LENDPTE-LDLRF-IIDEELFGQTHQHELKNGGSEIV 1142
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1143 VTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQ 1222
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1223 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGsngpqSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEEL 1301
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 547234945   1302 WDKLQMAIENTQGF 1315
Cdd:smart00119  315 REKLLLAINEGKGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
962-1316 6.13e-172

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: 514.42  E-value: 6.13e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  962 FEMKLRRATVLEDSYRRIMGVKRADfLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINP 1041
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1042 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWILENDPT--ELDLRF 1119
Cdd:cd00078    80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1120 IID-EELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCG 1198
Cdd:cd00078   159 TIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1199 LGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELygsngPQSFTVEQWGTP- 1277
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 547234945 1278 EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1316
Cdd:cd00078   314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
737-1316 4.06e-165

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 515.86  E-value: 4.06e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  737 SSSNHSSRRGSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNSRTTTWTKPTVQatvETSQLTSSQSSA 816
Cdd:COG5021   267 ISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLE---ETLGESTSFLVV 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  817 GPQSQASTSDSGQQVTQPSEIE-----------QGFL--------PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPA 877
Cdd:COG5021   344 NNDDSSSIKDLPHQVGSNPFLEahpefsellknQSRGttrdfrnkPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLG 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  878 HLRGKTSLDTSN-------DLGPLPPGWEERTHTDGRIFYINHNIKRTQWEDPRLENVA--ITGPAVPYSRDYKRKYeFF 948
Cdd:COG5021   424 RESDESFYVASNvqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKL-FY 502
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  949 RRKLKKQNdIPNKFEMKLRRATVLEDSYRRIMGvKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFE 1028
Cdd:COG5021   503 SLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1029 YSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWIL 1108
Cdd:COG5021   581 YITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL 659
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1109 EN--DPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKI 1186
Cdd:COG5021   660 NNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1187 FDENELELLMCGLGD-VDVNDWREHTKYKnGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNG 1265
Cdd:COG5021   740 FDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDG 818
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 547234945 1266 PQSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1316
Cdd:COG5021   819 VRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFG 870
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1013-1316 3.13e-132

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 407.77  E-value: 3.13e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1013 FLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLH 1091
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1092 DMESVDSEYYNSLRWIL---ENDPTELDLRFIIDEelFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQM 1168
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1169 AAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTG 1248
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1249 TSRVPMNGFAELygsngpQSFTVEQWGT--PEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1316
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
517-570 2.09e-24

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: 100.12  E-value: 2.09e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 547234945  517 TRDDFLGQVDVPLYPLPTENPRLERPYTFKDFVLHPRSHKSRVKGYLRLKMTYL 570
Cdd:cd04033    80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
893-925 2.47e-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: 62.23  E-value: 2.47e-12
                            10        20        30
                    ....*....|....*....|....*....|...
gi 547234945    893 PLPPGWEERTHTDGRIFYINHNIKRTQWEDPRL 925
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
895-925 1.05e-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: 1.05e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547234945  895 PPGWEERTHTDGRIFYINHNIKRTQWEDPRL 925
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
769-798 1.49e-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: 59.83  E-value: 1.49e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   769 LPPGWEEKQDERGRSYYVDHNSRTTTWTKP 798
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
611-643 2.08e-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: 2.08e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 547234945    611 PLPPGWEERQDILGRTYYVNHESRRTQWKRPTP 643
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
894-923 3.19e-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: 59.06  E-value: 3.19e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   894 LPPGWEERTHTDGRIFYINHNIKRTQWEDP 923
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
842-871 4.85e-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: 58.29  E-value: 4.85e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   842 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 871
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
843-873 5.09e-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: 5.09e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547234945  843 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 873
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
768-799 7.32e-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: 58.00  E-value: 7.32e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 547234945    768 GLPPGWEEKQDERGRSYYVDHNSRTTTWTKPT 799
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
842-873 9.26e-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: 9.26e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 547234945    842 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 873
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
612-641 1.11e-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: 57.51  E-value: 1.11e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   612 LPPGWEERQDILGRTYYVNHESRRTQWKRP 641
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
613-643 1.30e-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: 57.15  E-value: 1.30e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547234945  613 PPGWEERQDILGRTYYVNHESRRTQWKRPTP 643
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
770-799 1.88e-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: 56.77  E-value: 1.88e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 547234945  770 PPGWEEKQDERGRSYYVDHNSRTTTWTKPT 799
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
986-1315 0e+00

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: 554.54  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945    986 DFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1065
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1066 YHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWI-LENDPTE-LDLRF-IIDEELFGQTHQHELKNGGSEIV 1142
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1143 VTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQ 1222
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945   1223 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGsngpqSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEEL 1301
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 547234945   1302 WDKLQMAIENTQGF 1315
Cdd:smart00119  315 REKLLLAINEGKGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
962-1316 6.13e-172

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: 514.42  E-value: 6.13e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  962 FEMKLRRATVLEDSYRRIMGVKRADfLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINP 1041
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1042 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWILENDPT--ELDLRF 1119
Cdd:cd00078    80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1120 IID-EELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCG 1198
Cdd:cd00078   159 TIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1199 LGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELygsngPQSFTVEQWGTP- 1277
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 547234945 1278 EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1316
Cdd:cd00078   314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
737-1316 4.06e-165

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 515.86  E-value: 4.06e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  737 SSSNHSSRRGSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNSRTTTWTKPTVQatvETSQLTSSQSSA 816
Cdd:COG5021   267 ISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLE---ETLGESTSFLVV 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  817 GPQSQASTSDSGQQVTQPSEIE-----------QGFL--------PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPA 877
Cdd:COG5021   344 NNDDSSSIKDLPHQVGSNPFLEahpefsellknQSRGttrdfrnkPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLG 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  878 HLRGKTSLDTSN-------DLGPLPPGWEERTHTDGRIFYINHNIKRTQWEDPRLENVA--ITGPAVPYSRDYKRKYeFF 948
Cdd:COG5021   424 RESDESFYVASNvqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKL-FY 502
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  949 RRKLKKQNdIPNKFEMKLRRATVLEDSYRRIMGvKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFE 1028
Cdd:COG5021   503 SLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1029 YSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWIL 1108
Cdd:COG5021   581 YITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL 659
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1109 EN--DPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKI 1186
Cdd:COG5021   660 NNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945 1187 FDENELELLMCGLGD-VDVNDWREHTKYKnGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNG 1265
Cdd:COG5021   740 FDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDG 818
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 547234945 1266 PQSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1316
Cdd:COG5021   819 VRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFG 870
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1013-1316 3.13e-132

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 407.77  E-value: 3.13e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1013 FLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLH 1091
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1092 DMESVDSEYYNSLRWIL---ENDPTELDLRFIIDEelFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQM 1168
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1169 AAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTG 1248
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547234945  1249 TSRVPMNGFAELygsngpQSFTVEQWGT--PEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1316
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
517-570 2.09e-24

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: 100.12  E-value: 2.09e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 547234945  517 TRDDFLGQVDVPLYPLPTENPRLERPYTFKDFVLHPRSHKSRVKGYLRLKMTYL 570
Cdd:cd04033    80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
893-925 2.47e-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: 62.23  E-value: 2.47e-12
                            10        20        30
                    ....*....|....*....|....*....|...
gi 547234945    893 PLPPGWEERTHTDGRIFYINHNIKRTQWEDPRL 925
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
895-925 1.05e-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: 1.05e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547234945  895 PPGWEERTHTDGRIFYINHNIKRTQWEDPRL 925
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
769-798 1.49e-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: 59.83  E-value: 1.49e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   769 LPPGWEEKQDERGRSYYVDHNSRTTTWTKP 798
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
611-643 2.08e-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: 2.08e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 547234945    611 PLPPGWEERQDILGRTYYVNHESRRTQWKRPTP 643
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
894-923 3.19e-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: 59.06  E-value: 3.19e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   894 LPPGWEERTHTDGRIFYINHNIKRTQWEDP 923
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
842-871 4.85e-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: 58.29  E-value: 4.85e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   842 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 871
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
843-873 5.09e-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: 5.09e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547234945  843 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 873
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
768-799 7.32e-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: 58.00  E-value: 7.32e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 547234945    768 GLPPGWEEKQDERGRSYYVDHNSRTTTWTKPT 799
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
842-873 9.26e-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: 9.26e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 547234945    842 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 873
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
612-641 1.11e-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: 57.51  E-value: 1.11e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 547234945   612 LPPGWEERQDILGRTYYVNHESRRTQWKRP 641
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
613-643 1.30e-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: 57.15  E-value: 1.30e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 547234945  613 PPGWEERQDILGRTYYVNHESRRTQWKRPTP 643
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
770-799 1.88e-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: 56.77  E-value: 1.88e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 547234945  770 PPGWEEKQDERGRSYYVDHNSRTTTWTKPT 799
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
PRP40 COG5104
Splicing factor [RNA processing and modification];
846-923 2.18e-04

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 45.46  E-value: 2.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547234945  846 WEVRHAPNGRPFFIDHNTKTTTWEDPRlkipaHLRGKTSLDTSNDlgplppGWEERTHTDGRIFYINHNIKRTQWEDP 923
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPK-----ELLKGSEEDLDVD------PWKECRTADGKVYYYNSITRESRWKIP 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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