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Conserved domains on  [gi|1207160875|ref|XP_021324688|]
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E3 ubiquitin-protein ligase NEDD4-like isoform X2 [Danio rerio]

Protein Classification

WW domain-containing protein( domain architecture ID 11675134)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
945-1274 1.67e-177

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


:

Pssm-ID: 214523  Cd Length: 328  Bit Score: 526.80  E-value: 1.67e-177
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875   945 DSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1024
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1025 YHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLRFCIDEDN-FGQTYQVDLKPSGSDMV 1101
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1102 VTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHP 1181
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1182 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGTPD-KLPRAHTCFNRLDLPMYETFEDL 1260
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDeRLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1207160875  1261 REKLLMAVENAQGF 1274
Cdd:smart00119  315 REKLLLAINEGKGF 328
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
374-430 4.20e-25

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


The actual alignment was detected with superfamily member cd04033:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 133  Bit Score: 102.05  E-value: 4.20e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160875  374 NGQTRDDFLGQVDVPLTHLPTEDPAMERPYTFKDFLLRPRSHKSRVKGYLRLKMAYL 430
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
668-697 4.88e-13

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


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 64.06  E-value: 4.88e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  668 LPPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
855-884 4.79e-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: 4.79e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  855 PGWEERVHADGRTFYIDHNNKKTQWEDPRL 884
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
797-828 5.61e-11

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


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 58.38  E-value: 5.61e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1207160875   797 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 828
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
473-499 3.20e-09

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


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 53.28  E-value: 3.20e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160875  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
945-1274 1.67e-177

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


Pssm-ID: 214523  Cd Length: 328  Bit Score: 526.80  E-value: 1.67e-177
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875   945 DSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1024
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1025 YHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLRFCIDEDN-FGQTYQVDLKPSGSDMV 1101
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1102 VTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHP 1181
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1182 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGTPD-KLPRAHTCFNRLDLPMYETFEDL 1260
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDeRLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1207160875  1261 REKLLMAVENAQGF 1274
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
668-1274 7.65e-171

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 529.72  E-value: 7.65e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  668 LPPGWEERKDPKGRTYYVNHNNRSTTWTRPILQQhtEDGASTSVAAVGGataatppastpSTSSGHLSEP-QVRRPRSLS 746
Cdd:COG5021    299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEE--TLGESTSFLVVNN-----------DDSSSIKDLPhQVGSNPFLE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  747 SptvtlssplegannVPIRRAVKDTFSNpqspqpspysspktQHKANQSFLPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 826
Cdd:COG5021    366 A--------------HPEFSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  827 -RLKYPVHMR---TKASLD----PGDLGPLPNlpeepGWEERVHADGRTFYIDHNNKKTQWEDPRLQSPA--ITGPAVPY 896
Cdd:COG5021    418 rREQLGRESDesfYVASNVqqqrASREGPLLS-----GWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRI 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  897 SREFKQKYDYFRKKLKKPADIPnrFEMKLHRNNIFEESYRRIMSlKRPDSLKARLWIEFESEKGLDYGGVAREWFFLLSK 976
Cdd:COG5021    493 KEDKRRKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSK 569
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  977 EMFNPYYGLFEYSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVD 1056
Cdd:COG5021    570 EMFNPDYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLD 648
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1057 SEYYNSLKWILEN--DPTELDLRFCIDEDNFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGF 1134
Cdd:COG5021    649 PELYRSLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGF 728
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1135 TELIPIDLIKIFDENELELLMCGLGD-VDVNDWRQHTVYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPM 1213
Cdd:COG5021    729 SEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPI 807
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207160875 1214 NGFAELYGSNGPQLFTIEQWGTPDK-LPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGF 1274
Cdd:COG5021    808 NGFKDLQGSDGVRKFTIEKGGTDDDrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
921-1275 5.29e-169

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


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 505.56  E-value: 5.29e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  921 FEMKLHRNNIFEESYRRIMSLKRPDsLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 1000
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1001 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLRF 1078
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1079 CIDEDN-FGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCG 1157
Cdd:cd00078    159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1158 LGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGTPD 1237
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPD 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1207160875 1238 -KLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1275
Cdd:cd00078    314 dRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
972-1275 4.76e-133

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 409.31  E-value: 4.76e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  972 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLN 1050
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1051 DMESVDSEYYNSLKWIL---ENDPTELDLRFCIDEdnFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQM 1127
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1128 NAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1207
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1208 TSRVPMNGFAELygsngpQLFTIEQWGT--PDKLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1275
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
374-430 4.20e-25

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


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 102.05  E-value: 4.20e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160875  374 NGQTRDDFLGQVDVPLTHLPTEDPAMERPYTFKDFLLRPRSHKSRVKGYLRLKMAYL 430
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
668-697 4.88e-13

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 64.06  E-value: 4.88e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  668 LPPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
667-697 4.06e-12

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 61.46  E-value: 4.06e-12
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1207160875   667 GLPPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
669-697 1.29e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.85  E-value: 1.29e-11
                           10        20
                   ....*....|....*....|....*....
gi 1207160875  669 PPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
855-884 4.79e-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: 4.79e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  855 PGWEERVHADGRTFYIDHNNKKTQWEDPRL 884
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
797-828 5.61e-11

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 58.38  E-value: 5.61e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1207160875   797 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 828
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
798-828 5.94e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 58.31  E-value: 5.94e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207160875  798 PPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 828
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
797-826 1.17e-10

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 1.17e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  797 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 826
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
852-884 1.23e-10

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 1.23e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1207160875   852 PEEPGWEERVHADGRTFYIDHNNKKTQWEDPRL 884
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
855-882 4.19e-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: 4.19e-10
                           10        20
                   ....*....|....*....|....*...
gi 1207160875  855 PGWEERVHADGRTFYIDHNNKKTQWEDP 882
Cdd:pfam00397    3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
473-499 3.20e-09

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 53.28  E-value: 3.20e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160875  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
473-499 6.73e-09

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 52.14  E-value: 6.73e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160875  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
473-501 6.23e-08

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 49.52  E-value: 6.23e-08
                            10        20
                    ....*....|....*....|....*....
gi 1207160875   473 GWEEKVDNLGRTYYVNHNNRTTQWKRPSS 501
Cdd:smart00456    5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
945-1274 1.67e-177

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


Pssm-ID: 214523  Cd Length: 328  Bit Score: 526.80  E-value: 1.67e-177
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875   945 DSLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1024
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1025 YHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWI-LENDPTE-LDLRFCIDEDN-FGQTYQVDLKPSGSDMV 1101
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFSIVLTSeFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1102 VTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHP 1181
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  1182 VIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTIEQWGTPD-KLPRAHTCFNRLDLPMYETFEDL 1260
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDDeRLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 1207160875  1261 REKLLMAVENAQGF 1274
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
668-1274 7.65e-171

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 529.72  E-value: 7.65e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  668 LPPGWEERKDPKGRTYYVNHNNRSTTWTRPILQQhtEDGASTSVAAVGGataatppastpSTSSGHLSEP-QVRRPRSLS 746
Cdd:COG5021    299 LNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEE--TLGESTSFLVVNN-----------DDSSSIKDLPhQVGSNPFLE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  747 SptvtlssplegannVPIRRAVKDTFSNpqspqpspysspktQHKANQSFLPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 826
Cdd:COG5021    366 A--------------HPEFSELLKNQSR--------------GTTRDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDL 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  827 -RLKYPVHMR---TKASLD----PGDLGPLPNlpeepGWEERVHADGRTFYIDHNNKKTQWEDPRLQSPA--ITGPAVPY 896
Cdd:COG5021    418 rREQLGRESDesfYVASNVqqqrASREGPLLS-----GWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRI 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  897 SREFKQKYDYFRKKLKKPADIPnrFEMKLHRNNIFEESYRRIMSlKRPDSLKARLWIEFESEKGLDYGGVAREWFFLLSK 976
Cdd:COG5021    493 KEDKRRKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSK 569
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  977 EMFNPYYGLFEYSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVD 1056
Cdd:COG5021    570 EMFNPDYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLD 648
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1057 SEYYNSLKWILEN--DPTELDLRFCIDEDNFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGF 1134
Cdd:COG5021    649 PELYRSLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGF 728
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1135 TELIPIDLIKIFDENELELLMCGLGD-VDVNDWRQHTVYKnGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPM 1213
Cdd:COG5021    729 SEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPI 807
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207160875 1214 NGFAELYGSNGPQLFTIEQWGTPDK-LPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGF 1274
Cdd:COG5021    808 NGFKDLQGSDGVRKFTIEKGGTDDDrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGF 869
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
921-1275 5.29e-169

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


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 505.56  E-value: 5.29e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  921 FEMKLHRNNIFEESYRRIMSLKRPDsLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 1000
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1001 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPT--ELDLRF 1078
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1079 CIDEDN-FGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQMNAFLEGFTELIPIDLIKIFDENELELLMCG 1157
Cdd:cd00078    159 TIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1158 LGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTIEQWGTPD 1237
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPD 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1207160875 1238 -KLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1275
Cdd:cd00078    314 dRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
972-1275 4.76e-133

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 409.31  E-value: 4.76e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875  972 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLGKQITLN 1050
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1051 DMESVDSEYYNSLKWIL---ENDPTELDLRFCIDEdnFGQTYQVDLKPSGSDMVVTNDNKKEYIDLVIQWRFVNRVQKQM 1127
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1128 NAFLEGFTELIPIDLIKIFDENELELLMCGLGDVDVNDWRQHTVYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTG 1207
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207160875 1208 TSRVPMNGFAELygsngpQLFTIEQWGT--PDKLPRAHTCFNRLDLPMYETFEDLREKLLMAVENAQGFE 1275
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
374-430 4.20e-25

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


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 102.05  E-value: 4.20e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207160875  374 NGQTRDDFLGQVDVPLTHLPTEDPAMERPYTFKDFLLRPRSHKSRVKGYLRLKMAYL 430
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
668-697 4.88e-13

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 64.06  E-value: 4.88e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  668 LPPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
667-697 4.06e-12

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 61.46  E-value: 4.06e-12
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1207160875   667 GLPPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
669-697 1.29e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.85  E-value: 1.29e-11
                           10        20
                   ....*....|....*....|....*....
gi 1207160875  669 PPGWEERKDPKGRTYYVNHNNRSTTWTRP 697
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
855-884 4.79e-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: 4.79e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  855 PGWEERVHADGRTFYIDHNNKKTQWEDPRL 884
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
797-828 5.61e-11

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 58.38  E-value: 5.61e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1207160875   797 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 828
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
798-828 5.94e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 58.31  E-value: 5.94e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207160875  798 PPGWEMRIAPNGRPFFIDHNSRTTTWEDPRL 828
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
797-826 1.17e-10

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 57.13  E-value: 1.17e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207160875  797 LPPGWEMRIAPNGRPFFIDHNSRTTTWEDP 826
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
852-884 1.23e-10

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 1.23e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1207160875   852 PEEPGWEERVHADGRTFYIDHNNKKTQWEDPRL 884
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
855-882 4.19e-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: 4.19e-10
                           10        20
                   ....*....|....*....|....*...
gi 1207160875  855 PGWEERVHADGRTFYIDHNNKKTQWEDP 882
Cdd:pfam00397    3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
473-499 3.20e-09

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 53.28  E-value: 3.20e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160875  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
473-499 6.73e-09

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 52.14  E-value: 6.73e-09
                           10        20
                   ....*....|....*....|....*..
gi 1207160875  473 GWEEKVDNLGRTYYVNHNNRTTQWKRP 499
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
473-501 6.23e-08

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


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 49.52  E-value: 6.23e-08
                            10        20
                    ....*....|....*....|....*....
gi 1207160875   473 GWEEKVDNLGRTYYVNHNNRTTQWKRPSS 501
Cdd:smart00456    5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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