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Conserved domains on  [gi|2217316465|ref|XP_006722488|]
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E3 ubiquitin-protein ligase NEDD4-like isoform X8 [Homo sapiens]

Protein Classification

WW and HECTc domain-containing protein( domain architecture ID 11675138)

protein containing domains C2, WW, and HECTc

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 ...
 751-1080 9.13e-179

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: 524.49  E-value: 9.13e-179
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   751 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 830
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   831 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 907
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   908 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 987
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   988 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 1066
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314

                           330
                    ....*....|....
gi 2217316465  1067 REKLLMAVENAQGF 1080
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 ...
 379-432 2.96e-25

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


The actual alignment was detected with superfamily member cd04033:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 133  Bit Score: 102.05  E-value: 2.96e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217316465  379 TRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 432
Cdd:cd04033     80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 658-690 1.33e-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: 59.92  E-value: 1.33e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217316465   658 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 690
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 477-503 4.59e-10

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


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 55.59  E-value: 4.59e-10
                           10        20
                   ....*....|....*....|....*..
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 79-404 7.56e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 7.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   79 TSIDARPTCSSSvqiSLQRKATDGATDGCGP-PEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPR 157
Cdd:PHA03247  2667 ARRLGRAAQASS---PPQRPRRRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  158 AARDPGLQVN-GTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRL----LPLGPDGQGGPAAAEPRRWSLQHVPD 232
Cdd:PHA03247  2744 VPAGPATPGGpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsresLPSPWDPADPPAAVLAPAAALPPAAS 2823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  233 ASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRLVRYPRIRLERSTSYPTQPRSERGSptedRGALEASPRAGR 312
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA----RPAVSRSTESFA 2899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  313 MAP---EIRRTNSAERTPQGQGCTFKIRQDQNAGQqhfrilvTRGPEEAPQNPEEKSAKSPVSTGADTTTRDDFL--GQV 387
Cdd:PHA03247  2900 LPPdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPP-------PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALvpGRV 2972

                          330
                   ....*....|....*..
gi 2217316465  388 DVPLSHLPTEDPTMERP 404
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAP 2989
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 751-1080 9.13e-179

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: 524.49  E-value: 9.13e-179
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   751 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 830
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   831 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 907
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   908 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 987
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   988 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 1066
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314

                           330
                    ....*....|....
gi 2217316465  1067 REKLLMAVENAQGF 1080
Cdd:smart00119  315 REKLLLAINEGKGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 727-1081 2.91e-169

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


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 500.94  E-value: 2.91e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  727 FEMKLHRNNIFEESYRRIMSVKRPDvLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 806
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  807 NSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLMF 884
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  885 CIDEEN-FGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 963
Cdd:cd00078    159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  964 LGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGSP- 1042
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2217316465 1043 EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1081
Cdd:cd00078    314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
477-1080 1.16e-160

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 497.75  E-value: 1.16e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQeaahrRFRSRRHisedlepepseggdvpepwetis 556
Cdd:COG5021    302 LFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNND-----DSSSIKD----------------------- 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  557 EEVNIAGDSLglalppppaspgsrTSPQELSEELSRRL--QITPDSN--GEQFSSLIqrEPSSRLRScsvTDAVAEQGHL 632
Cdd:COG5021    354 LPHQVGSNPF--------------LEAHPEFSELLKNQsrGTTRDFRnkPTGWSSSI--EDLGQFLF---SDFLTSSSTY 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  633 ppEDP-RLKFPVHMRSKTSLNPN-------DLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPA--ITGPAVPY 702
Cdd:COG5021    415 --EDLrREQLGRESDESFYVASNvqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRI 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  703 SREFKQKYDYFRKKLKKPADIPnrFEMKLHRNNIFEESYRRIMSvKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSK 782
Cdd:COG5021    493 KEDKRRKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSK 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  783 EMFNPYYGLFEYSATDNYTLQINPNSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVD 862
Cdd:COG5021    570 EMFNPDYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLD 648

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  863 SEYYNSLKWILEN--DPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGF 940
Cdd:COG5021    649 PELYRSLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGF 728

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  941 TELLPIDLIKIFDENELELLMCGLGD-VDVNDWRQHSIYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPM 1019
Cdd:COG5021    729 SEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPI 807

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316465 1020 NGFAELYGSNGPQLFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGF 1080
Cdd:COG5021    808 NGFKDLQGSDGVRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 778-1081 6.61e-134

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 407.38  E-value: 6.61e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  778 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLN 856
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  857 DMESVDSEYYNSLKWIL---ENDPTELDLMFCIDEenFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQM 933
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  934 NAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1013
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465 1014 TSRVPMNGFAELygsngpQLFTIEQWGS--PEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1081
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 379-432 2.96e-25

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


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 102.05  E-value: 2.96e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217316465  379 TRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 432
Cdd:cd04033     80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 658-690 1.33e-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: 59.92  E-value: 1.33e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217316465   658 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 690
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 660-690 4.19e-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: 4.19e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217316465  660 PPGWEERIHLDGRTFYIDHNSKITQWEDPRL 690
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 659-688 8.99e-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: 57.51  E-value: 8.99e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217316465  659 LPPGWEERIHLDGRTFYIDHNSKITQWEDP 688
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 477-503 4.59e-10

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 55.59  E-value: 4.59e-10
                           10        20
                   ....*....|....*....|....*..
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 477-503 1.27e-09

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 54.07  E-value: 1.27e-09
                           10        20
                   ....*....|....*....|....*..
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 477-503 5.25e-09

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 52.60  E-value: 5.25e-09
                            10        20
                    ....*....|....*....|....*..
gi 2217316465   477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:smart00456    5 GWEERKDPDGRPYYYNHETKETQWEKP 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 79-404 7.56e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 7.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   79 TSIDARPTCSSSvqiSLQRKATDGATDGCGP-PEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPR 157
Cdd:PHA03247  2667 ARRLGRAAQASS---PPQRPRRRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  158 AARDPGLQVN-GTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRL----LPLGPDGQGGPAAAEPRRWSLQHVPD 232
Cdd:PHA03247  2744 VPAGPATPGGpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsresLPSPWDPADPPAAVLAPAAALPPAAS 2823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  233 ASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRLVRYPRIRLERSTSYPTQPRSERGSptedRGALEASPRAGR 312
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA----RPAVSRSTESFA 2899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  313 MAP---EIRRTNSAERTPQGQGCTFKIRQDQNAGQqhfrilvTRGPEEAPQNPEEKSAKSPVSTGADTTTRDDFL--GQV 387
Cdd:PHA03247  2900 LPPdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPP-------PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALvpGRV 2972

                          330
                   ....*....|....*..
gi 2217316465  388 DVPLSHLPTEDPTMERP 404
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAP 2989
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 751-1080 9.13e-179

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: 524.49  E-value: 9.13e-179
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   751 DVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFTFIGRVAGLAV 830
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   831 FHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLMFCIDEEN-FGQTYQVDLKPNGSEIM 907
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   908 VTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHP 987
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   988 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDL 1066
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314

                           330
                    ....*....|....
gi 2217316465  1067 REKLLMAVENAQGF 1080
Cdd:smart00119  315 REKLLLAINEGKGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 727-1081 2.91e-169

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


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 500.94  E-value: 2.91e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  727 FEMKLHRNNIFEESYRRIMSVKRPDvLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 806
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  807 NSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLMF 884
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  885 CIDEEN-FGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCG 963
Cdd:cd00078    159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  964 LGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGSP- 1042
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2217316465 1043 EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1081
Cdd:cd00078    314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
477-1080 1.16e-160

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 497.75  E-value: 1.16e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQeaahrRFRSRRHisedlepepseggdvpepwetis 556
Cdd:COG5021    302 LFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNND-----DSSSIKD----------------------- 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  557 EEVNIAGDSLglalppppaspgsrTSPQELSEELSRRL--QITPDSN--GEQFSSLIqrEPSSRLRScsvTDAVAEQGHL 632
Cdd:COG5021    354 LPHQVGSNPF--------------LEAHPEFSELLKNQsrGTTRDFRnkPTGWSSSI--EDLGQFLF---SDFLTSSSTY 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  633 ppEDP-RLKFPVHMRSKTSLNPN-------DLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPA--ITGPAVPY 702
Cdd:COG5021    415 --EDLrREQLGRESDESFYVASNvqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRI 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  703 SREFKQKYDYFRKKLKKPADIPnrFEMKLHRNNIFEESYRRIMSvKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSK 782
Cdd:COG5021    493 KEDKRRKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSK 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  783 EMFNPYYGLFEYSATDNYTLQINPNSGLcNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVD 862
Cdd:COG5021    570 EMFNPDYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLD 648

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  863 SEYYNSLKWILEN--DPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGF 940
Cdd:COG5021    649 PELYRSLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGF 728

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  941 TELLPIDLIKIFDENELELLMCGLGD-VDVNDWRQHSIYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPM 1019
Cdd:COG5021    729 SEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPI 807

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217316465 1020 NGFAELYGSNGPQLFTIEQWGSP-EKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGF 1080
Cdd:COG5021    808 NGFKDLQGSDGVRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 778-1081 6.61e-134

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 407.38  E-value: 6.61e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  778 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLN 856
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  857 DMESVDSEYYNSLKWIL---ENDPTELDLMFCIDEenFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQM 933
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  934 NAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1013
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465 1014 TSRVPMNGFAELygsngpQLFTIEQWGS--PEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFE 1081
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 379-432 2.96e-25

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


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 102.05  E-value: 2.96e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217316465  379 TRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYM 432
Cdd:cd04033     80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 658-690 1.33e-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: 59.92  E-value: 1.33e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2217316465   658 PLPPGWEERIHLDGRTFYIDHNSKITQWEDPRL 690
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 660-690 4.19e-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: 4.19e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217316465  660 PPGWEERIHLDGRTFYIDHNSKITQWEDPRL 690
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 659-688 8.99e-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: 57.51  E-value: 8.99e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217316465  659 LPPGWEERIHLDGRTFYIDHNSKITQWEDP 688
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 477-503 4.59e-10

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 55.59  E-value: 4.59e-10
                           10        20
                   ....*....|....*....|....*..
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 477-503 1.27e-09

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 54.07  E-value: 1.27e-09
                           10        20
                   ....*....|....*....|....*..
gi 2217316465  477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 477-503 5.25e-09

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 52.60  E-value: 5.25e-09
                            10        20
                    ....*....|....*....|....*..
gi 2217316465   477 GWEEKVDNLGRTYYVNHNNRTTQWHRP 503
Cdd:smart00456    5 GWEERKDPDGRPYYYNHETKETQWEKP 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 79-404 7.56e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 7.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   79 TSIDARPTCSSSvqiSLQRKATDGATDGCGP-PEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPR 157
Cdd:PHA03247  2667 ARRLGRAAQASS---PPQRPRRRAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  158 AARDPGLQVN-GTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRL----LPLGPDGQGGPAAAEPRRWSLQHVPD 232
Cdd:PHA03247  2744 VPAGPATPGGpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsresLPSPWDPADPPAAVLAPAAALPPAAS 2823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  233 ASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRLVRYPRIRLERSTSYPTQPRSERGSptedRGALEASPRAGR 312
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA----RPAVSRSTESFA 2899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  313 MAP---EIRRTNSAERTPQGQGCTFKIRQDQNAGQqhfrilvTRGPEEAPQNPEEKSAKSPVSTGADTTTRDDFL--GQV 387
Cdd:PHA03247  2900 LPPdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPP-------PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALvpGRV 2972

                          330
                   ....*....|....*..
gi 2217316465  388 DVPLSHLPTEDPTMERP 404
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAP 2989
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 99-327 3.04e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   99 ATDGATDGCGPPEGADDGPPCATPDPRDQASA-----TATTRASPQSGSREPSPRDtPGSSPPRAAR--------DPGLQ 165
Cdd:PHA03307    57 AGAAACDRFEPPTGPPPGPGTEAPANESRSTPtwslsTLAPASPAREGSPTPPGPS-SPDPPPPTPPpaspppspAPDLS 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  166 VNgtcGRRVRCSGPVDCAEEAAPGLriQHRASSADVRQVR----LLPLGPDGQGGPAAAEPRRWSLQHVPDASGSSGKRC 241
Cdd:PHA03307   136 EM---LRPVGSPGPPPAASPPAAGA--SPAAVASDAASSRqaalPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  242 FVFQLQQPQQGASGPGSD-----------LNFGFTGTKGDRLVRYPRIRLERSTSyPTQPRSERGSPTEDRGALEASPRA 310
Cdd:PHA03307   211 SPISASASSPAPAPGRSAaddagasssdsSSSESSGCGWGPENECPLPRPAPITL-PTRIWEASGWNGPSSRPGPASSSS 289

                          250
                   ....*....|....*..
gi 2217316465  311 GRMAPEIRRTNSAERTP 327
Cdd:PHA03307   290 SPRERSPSPSPSSPGSG 306
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 102-328 3.80e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  102 GATDGCGPPEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPRAARDPGLQVNGTCGRRVRCSGPVD 181
Cdd:PRK07764   593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  182 cAEEAAPglriqhraSSADVRQVRLLPLGPDGQGGPAAAEPRRWSLQHVPDASGSSgkrcfvfQLQQPQQGASGPGSDln 261
Cdd:PRK07764   673 -AGGAAP--------AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAA-------QPPQAAQGASAPSPA-- 734

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316465  262 fgftgtkGDRLVRYPRIRLERSTSYPTQPRSERGSPTEDRGALEASPRAGRMAPEIRRTNSAERTPQ 328
Cdd:PRK07764   735 -------ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 65-222 6.07e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   65 ALKRSSSMFIPQLLTSIDARPTCSSSVQISLQRKATDGATDGCGPP-----EGADDGPPCATPDPRDQASATATTRASPQ 139
Cdd:PHA03307   744 ARARASAWDITDALFSNPSLVPAKLAEALALLEPAEPQRGAGSSPPvraeaAFRRPGRLRRSGPAADAASRTASKRKSRS 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  140 SGSREPSPRDTPGSSPPRAARDPGLQVNGTCGRRVRCSGPVDCAEEAAPGLRIQHRASSADVRQVRLLPLGPDGQGGPAA 219
Cdd:PHA03307   824 HTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAP 903


                   ...
gi 2217316465  220 AEP 222
Cdd:PHA03307   904 RPR 906
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 83-331 1.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   83 ARPTCSSSVQISLQRKATDGATDGCGPPegaDDGPPcATPDPRDQASATATTRASPQSGSREPSPRD-----------TP 151
Cdd:PHA03307    86 STPTWSLSTLAPASPAREGSPTPPGPSS---PDPPP-PTPPPASPPPSPAPDLSEMLRPVGSPGPPPaasppaagaspAA 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  152 GSSPPRAARDPGLQVNGTcGRRVRCSG------PVDCAEEAAPGlRIQHRASSADVRQVRLLPLGPDGQGGPAAAEPrrw 225
Cdd:PHA03307   162 VASDAASSRQAALPLSSP-EETARAPSsppaepPPSTPPAAASP-RPPRRSSPISASASSPAPAPGRSAADDAGASS--- 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  226 slqhvPDASGSSGKRCFVFQLQQPQQGASGPGSDLNFGFTGTKGDRlvRYPRIRLERSTSYPTQPRSERGSPTEDRGALE 305
Cdd:PHA03307   237 -----SDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG--PSSRPGPASSSSSPRERSPSPSPSSPGSGPAP 309

                          250       260
                   ....*....|....*....|....*.
gi 2217316465  306 ASPRAGRMAPEIRRTNSAERTPQGQG 331
Cdd:PHA03307   310 SSPRASSSSSSSRESSSSSTSSSSES 335
PHA03378 PHA03378
EBNA-3B; Provisional
 109-319 1.07e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  109 PPEGADDGPPCATPDPRDQASATATTRASPQSGS------------REPSPRDTPGSS-PPRAARDPGLQVNGTCGRRVR 175
Cdd:PHA03378   697 PPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAApgrarppaaapgRARPPAAAPGRArPPAAAPGRARPPAAAPGAPTP 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  176 CSGPvdcaeEAAPGLRIQHRASSADVRQ-------VRLLPLGPDGQGGPAAAEPRRWSLQHVpdasgSSGKRCFVFQLQQ 248
Cdd:PHA03378   777 QPPP-----QAPPAPQQRPRGAPTPQPPpqagptsMQLMPRAAPGQQGPTKQILRQLLTGGV-----KRGRPSLKKPAAL 846

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217316465  249 PQQGASGPGSDLNFGftgtKGDRLVRYPRIRLERSTsyPTQPRSERGSPTEdrGALEASPRAGRMAPEIRR 319
Cdd:PHA03378   847 ERQAAAGPTPSPGSG----TSDKIVQAPVFYPPVLQ--PIQVMRQLGSVRA--AAASTVTQAPTEYTGERR 909
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 77-324 1.85e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   77 LLTSIDARPTCSSSVQISLQRKATDGATDGCGPPEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPP 156
Cdd:PHA03307   175 PLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  157 RAARDPGLQVNGTCGRRvrcsGPVDCAEEAAPGlriqhRASSADVRQVRLLPLGPDGQGGPAAAEPRRWSLQHVPDASGS 236
Cdd:PHA03307   255 CPLPRPAPITLPTRIWE----ASGWNGPSSRPG-----PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465  237 SGKRcfvfqlqqpqqGASGPGSDlnfgftgtkgDRLVRYPRiRLERSTSYPTQPRSERGSPTEDRGALEASPRAGRMA-- 314
Cdd:PHA03307   326 SSST-----------SSSSESSR----------GAAVSPGP-SPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASag 383

                          250
                   ....*....|.
gi 2217316465  315 -PEIRRTNSAE 324
Cdd:PHA03307   384 rPTRRRARAAV 394
PHA03247 PHA03247
large tegument protein UL36; Provisional
 95-236 4.77e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316465   95 LQRKATDgatDGCGPPEGADDGPPCATPDPRDQASATATTRASPQSGSREPSPRDTPGSSPPRAARDPGLQVNGTC---- 170
Cdd:PHA03247  2540 LEELASD---DAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAppsp 2616

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217316465  171 -------------GRRVRCSGPVDCAEEAAPGlRIQHRASSADVRQVRLLPLGPDGQGGPAAAEPRRWSLQHVPDASGS 236
Cdd:PHA03247  2617 lppdthapdppppSPSPAANEPDPHPPPTVPP-PERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS 2694
 
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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