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Conserved domains on  [gi|1243938454|ref|NP_001342151|]
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NEDD4-like E3 ubiquitin-protein ligase WWP1 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HUL4 super family cl34867
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
309-850 1.18e-177

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


The actual alignment was detected with superfamily member COG5021:

Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 534.35  E-value: 1.18e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 309 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 381
Cdd:COG5021   297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 382 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 435
Cdd:COG5021   377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 436 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 515
Cdd:COG5021   457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 516 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 595
Cdd:COG5021   536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 596 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 675
Cdd:COG5021   616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 754
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:COG5021   776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855

                         570
                  ....*....|....*..
gi 1243938454 834 KEKLLFAIEETEGFGQE 850
Cdd:COG5021   856 RSKLLTAINEGAGFGLL 872
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 8-72 3.81e-27

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 cd04021:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 125  Bit Score: 106.98  E-value: 3.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938454   8 TTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 72
Cdd:cd04021    61 STLEFKVWSHHTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 279-308 4.50e-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: 63.68  E-value: 4.50e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 308
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 80-313 8.85e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 49.19  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  80 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 149
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 150 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 229
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 230 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 301
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371

                         250
                  ....*....|....*..
gi 1243938454 302 -----TTTWERPQPLPP 313
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
309-850 1.18e-177

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 534.35  E-value: 1.18e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 309 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 381
Cdd:COG5021   297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 382 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 435
Cdd:COG5021   377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 436 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 515
Cdd:COG5021   457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 516 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 595
Cdd:COG5021   536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 596 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 675
Cdd:COG5021   616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 754
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:COG5021   776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855

                         570
                  ....*....|....*..
gi 1243938454 834 KEKLLFAIEETEGFGQE 850
Cdd:COG5021   856 RSKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 496-848 7.47e-170

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: 495.55  E-value: 7.47e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 496 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 575
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 576 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 655
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 656 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 734
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 735 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 812
Cdd:cd00078   242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1243938454 813 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 519-847 2.56e-159

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: 467.48  E-value: 2.56e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  519 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 596
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  597 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 675
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 754
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 1243938454  834 KEKLLFAIEETEGF 847
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 545-848 2.30e-120

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 366.16  E-value: 2.30e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 545 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 622
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 623 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 700
Cdd:pfam00632  81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 701 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 779
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243938454 780 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:pfam00632 238 GSSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 8-72 3.81e-27

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. 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: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 106.98  E-value: 3.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938454   8 TTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 72
Cdd:cd04021    61 STLEFKVWSHHTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 279-308 4.50e-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: 63.68  E-value: 4.50e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 308
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 279-310 2.04e-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: 61.85  E-value: 2.04e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1243938454  279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 280-310 2.14e-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: 61.77  E-value: 2.14e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1243938454 280 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 80-313 8.85e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 49.19  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  80 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 149
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 150 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 229
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 230 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 301
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371

                         250
                  ....*....|....*..
gi 1243938454 302 -----TTTWERPQPLPP 313
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
309-850 1.18e-177

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 534.35  E-value: 1.18e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 309 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 381
Cdd:COG5021   297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 382 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 435
Cdd:COG5021   377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 436 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 515
Cdd:COG5021   457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 516 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 595
Cdd:COG5021   536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 596 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 675
Cdd:COG5021   616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 754
Cdd:COG5021   696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:COG5021   776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855

                         570
                  ....*....|....*..
gi 1243938454 834 KEKLLFAIEETEGFGQE 850
Cdd:COG5021   856 RSKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 496-848 7.47e-170

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: 495.55  E-value: 7.47e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 496 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 575
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 576 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 655
Cdd:cd00078    82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 656 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 734
Cdd:cd00078   162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 735 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 812
Cdd:cd00078   242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1243938454 813 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:cd00078   317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 519-847 2.56e-159

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: 467.48  E-value: 2.56e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  519 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 596
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  597 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 675
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  676 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 754
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  755 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 833
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 1243938454  834 KEKLLFAIEETEGF 847
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 545-848 2.30e-120

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 366.16  E-value: 2.30e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 545 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 622
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 623 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 700
Cdd:pfam00632  81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 701 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 779
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243938454 780 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 848
Cdd:pfam00632 238 GSSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 8-72 3.81e-27

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. 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: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 106.98  E-value: 3.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938454   8 TTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLD 72
Cdd:cd04021    61 STLEFKVWSHHTLKADVLLGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 279-308 4.50e-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: 63.68  E-value: 4.50e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 308
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 311-340 1.55e-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: 62.14  E-value: 1.55e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 311 LPPGWERRVDDRGRVYYVDHNTRTTTWQRP 340
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 279-310 2.04e-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: 61.85  E-value: 2.04e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1243938454  279 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 280-310 2.14e-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: 61.77  E-value: 2.14e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1243938454 280 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 310
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 386-415 3.23e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 61.37  E-value: 3.23e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 386 LPPGWEKRVDSTDRVYFVNHNTKTTQWEDP 415
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 387-416 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: 59.46  E-value: 1.25e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 387 PPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 416
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 385-416 1.48e-11

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 59.54  E-value: 1.48e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1243938454  385 PLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 416
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 312-342 1.57e-11

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.46  E-value: 1.57e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1243938454 312 PPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 342
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 310-342 2.97e-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: 2.97e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1243938454  310 PLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 342
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
PRP40 COG5104
Splicing factor [RNA processing and modification];
278-340 1.64e-09

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 61.25  E-value: 1.64e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938454 278 ALPSG-----WEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDD---------RGRVYYVDHNTRTTTWQRP 340
Cdd:COG5104     7 GMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdpwkecrtaDGKVYYYNSITRESRWKIP 83
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 427-456 1.79e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 50.60  E-value: 1.79e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 427 PEGWEIRYTREGVRYFVDHNTRTTTFKDPR 456
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 425-457 2.62e-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: 50.29  E-value: 2.62e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1243938454  425 PLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRN 457
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 426-455 1.49e-07

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: 47.88  E-value: 1.49e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1243938454 426 LPEGWEIRYTREGVRYFVDHNTRTTTFKDP 455
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 80-313 8.85e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 49.19  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454  80 PVTNRSSSPPIEIQqNGDALHeNGDPATRT----------TPRLPVEGTIGIDNHVSTntVVPNSCCSHVVNGENTPSSP 149
Cdd:pfam17823 150 CRANASAAPRAAIA-AASAPH-AASPAPRTaassttaassTTAASSAPTTAASSAPAT--LTPARGISTAATATGHPAAG 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 150 SQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEHSECIPS 229
Cdd:pfam17823 226 TALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKHMPSDTM 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938454 230 AS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYVDHNTR- 301
Cdd:pfam17823 292 ARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPVLHTSMi 371

                         250
                  ....*....|....*..
gi 1243938454 302 -----TTTWERPQPLPP 313
Cdd:pfam17823 372 peveaTSPTTQPSPLLP 388
PRP40 COG5104
Splicing factor [RNA processing and modification];
390-455 5.05e-03

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 40.45  E-value: 5.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938454 390 WEKRVDSTDRVYFVNHNTKTTQWEDPRTQGLPNEEPLPE-GWEIRYTREGVRYFVDHNTRTTTFKDP 455
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdPWKECRTADGKVYYYNSITRESRWKIP 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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