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Conserved domains on  [gi|2024450188|ref|XP_040535900|]
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E3 ubiquitin-protein ligase NEDD4 isoform X1 [Gallus gallus]

Protein Classification

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 ...
975-1304 0e+00

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


:

Pssm-ID: 214523  Cd Length: 328  Bit Score: 542.98  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188   975 DFLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1054
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1055 YHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWI-LENDPAE-LDLRF-IVDEELFGQTHQHELKSGGSEIV 1131
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1132 VTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVADWKLHTKYKNGYSVNHQ 1211
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1212 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTVEQWGTP-EKLPRAHTCFNRLDLPPYDSFEDL 1290
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 2024450188  1291 WDKLLLAIENTQGF 1304
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 ...
504-557 2.13e-24

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


The actual alignment was detected with superfamily member cd04033:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 133  Bit Score: 99.73  E-value: 2.13e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024450188  504 TRDDFLGQVDIPLYQLPTEHPSMERPYTFRDFVLHPRSHKSRVKGHLRLKMTYL 557
Cdd:cd04033     80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
882-914 6.56e-14

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: 66.47  E-value: 6.56e-14
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2024450188   882 PLPPGWEERTHTDGRIFFINHNTKKTQWEDPRL 914
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
756-787 7.53e-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: 60.69  E-value: 7.53e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2024450188   756 GLPPGWEERQDEKGRSYYIDHNSRTTTWIKPV 787
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
833-863 2.57e-11

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


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.08  E-value: 2.57e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024450188  833 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 863
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
602-629 4.92e-08

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: 49.81  E-value: 4.92e-08
                           10        20
                   ....*....|....*....|....*...
gi 2024450188  602 SGWEERQDILGRTYYVNHEFRRTQWKRP 629
Cdd:pfam00397    3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
975-1304 0e+00

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


Pssm-ID: 214523  Cd Length: 328  Bit Score: 542.98  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188   975 DFLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1054
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1055 YHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWI-LENDPAE-LDLRF-IVDEELFGQTHQHELKSGGSEIV 1131
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1132 VTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVADWKLHTKYKNGYSVNHQ 1211
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1212 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTVEQWGTP-EKLPRAHTCFNRLDLPPYDSFEDL 1290
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 2024450188  1291 WDKLLLAIENTQGF 1304
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
683-1305 1.40e-172

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 535.12  E-value: 1.40e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  683 LYSNENPQIPLPQNSSDI-QTHLAEE----LNTRLTTSGSSATGQSAAYTNHSSRRGSLQTYRVEEQPAHPVLLPTSSGL 757
Cdd:COG5021    220 LTMRTNFLKLDTGNLSGEvQALLARYisikLVIKKLYLGPGPDASSRISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRL 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  758 PPGWEERQDEKGRSYYIDHNSRTTTWIKPVVQI-AMEAGQLPAAQNTSIARQPQATSGDSSQQSSNQQPEMEQGF----- 831
Cdd:COG5021    300 NSLFSTRADSFGRTYYLDHDRILTQYSRPLLEEtLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPEFSELLknqsr 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  832 --------LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP-RLKIPAHLRRKTSLD-------PVDLGPLPPGWEERTHTDG 895
Cdd:COG5021    380 gttrdfrnKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLrREQLGRESDESFYVAsnvqqqrASREGPLLSGWKTRLNNLY 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  896 RIFFINHNTKKTQWEDPRLQNVA--ITGPAVPYSRDYKRKYEFFRKKLKKQSDIPnrFEMKIHRTTILEDSYRrIIAVKR 973
Cdd:COG5021    460 RFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYR-EIMDES 536
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  974 ADFLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMA 1053
Cdd:COG5021    537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKA 615
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1054 VYHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWILEN--DPAELDLRFIVDEELFGQTHQHELKSGGSEIV 1131
Cdd:COG5021    616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1132 VTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGD-VDVADWKLHTKYKnGYSVNH 1210
Cdd:COG5021    696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDS 774
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1211 QVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTVEQWGTP-EKLPRAHTCFNRLDLPPYDSFED 1289
Cdd:COG5021    775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEK 854
                          650
                   ....*....|....*.
gi 2024450188 1290 LWDKLLLAIENTQGFD 1305
Cdd:COG5021    855 LRSKLLTAINEGAGFG 870
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
951-1305 4.02e-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: 506.72  E-value: 4.02e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  951 FEMKIHRTTILEDSYRRIIAVKRADfLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 1030
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1031 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWILENDP--AELDLRF 1108
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdeDDLELTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1109 -IVDEELFGQTHQHELKSGGSEIVVTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCG 1187
Cdd:cd00078    159 tIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1188 LGDVDVADWKLHTKYKNGYSVNHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTVEQWGTP- 1266
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2024450188 1267 EKLPRAHTCFNRLDLPPYDSFEDLWDKLLLAIENTQGFD 1305
Cdd:cd00078    314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1002-1305 1.94e-131

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 405.46  E-value: 1.94e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1002 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDAFFIRPFYKMMLQKPITLH 1080
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1081 DMESVDSEYYNSLRWIL---ENDPAELDLRFIVDEelFGQTHQHELKSGGSEIVVTNKNKRDYIHLVIQWRFVSRVQKQM 1157
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1158 AAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVADWKLHTKYKNGYSVNHQVIQWFWKAVLMMDSEKRIRLLQFVTG 1237
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1238 TSRVPMNGFAELygsngpQLFTVEQWGT--PEKLPRAHTCFNRLDLPPYDSFEDLWDKLLLAIENTQGFD 1305
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
504-557 2.13e-24

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


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 99.73  E-value: 2.13e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024450188  504 TRDDFLGQVDIPLYQLPTEHPSMERPYTFRDFVLHPRSHKSRVKGHLRLKMTYL 557
Cdd:cd04033     80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
882-914 6.56e-14

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: 66.47  E-value: 6.56e-14
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2024450188   882 PLPPGWEERTHTDGRIFFINHNTKKTQWEDPRL 914
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
884-914 4.30e-13

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: 64.09  E-value: 4.30e-13
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024450188  884 PPGWEERTHTDGRIFFINHNTKKTQWEDPRL 914
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
883-912 6.88e-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: 63.68  E-value: 6.88e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  883 LPPGWEERTHTDGRIFFINHNTKKTQWEDP 912
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
756-787 7.53e-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: 60.69  E-value: 7.53e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2024450188   756 GLPPGWEERQDEKGRSYYIDHNSRTTTWIKPV 787
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
757-786 7.75e-12

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 60.60  E-value: 7.75e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  757 LPPGWEERQDEKGRSYYIDHNSRTTTWIKP 786
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
833-863 2.57e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.08  E-value: 2.57e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024450188  833 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 863
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
832-861 2.57e-11

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 59.06  E-value: 2.57e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  832 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 861
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
758-787 3.84e-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: 58.69  E-value: 3.84e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  758 PPGWEERQDEKGRSYYIDHNSRTTTWIKPV 787
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
832-863 3.92e-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: 58.77  E-value: 3.92e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2024450188   832 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 863
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
602-629 4.92e-08

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: 49.81  E-value: 4.92e-08
                           10        20
                   ....*....|....*....|....*...
gi 2024450188  602 SGWEERQDILGRTYYVNHEFRRTQWKRP 629
Cdd:pfam00397    3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
602-630 6.17e-08

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 49.45  E-value: 6.17e-08
                           10        20
                   ....*....|....*....|....*....
gi 2024450188  602 SGWEERQDILGRTYYVNHEFRRTQWKRPT 630
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
602-630 1.54e-07

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: 48.75  E-value: 1.54e-07
                            10        20
                    ....*....|....*....|....*....
gi 2024450188   602 SGWEERQDILGRTYYVNHEFRRTQWKRPT 630
Cdd:smart00456    4 PGWEERKDPDGRPYYYNHETKETQWEKPR 32
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
975-1304 0e+00

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


Pssm-ID: 214523  Cd Length: 328  Bit Score: 542.98  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188   975 DFLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 1054
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1055 YHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWI-LENDPAE-LDLRF-IVDEELFGQTHQHELKSGGSEIV 1131
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1132 VTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVADWKLHTKYKNGYSVNHQ 1211
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  1212 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSngpqlFTVEQWGTP-EKLPRAHTCFNRLDLPPYDSFEDL 1290
Cdd:smart00119  240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 2024450188  1291 WDKLLLAIENTQGF 1304
Cdd:smart00119  315 REKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
683-1305 1.40e-172

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 535.12  E-value: 1.40e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  683 LYSNENPQIPLPQNSSDI-QTHLAEE----LNTRLTTSGSSATGQSAAYTNHSSRRGSLQTYRVEEQPAHPVLLPTSSGL 757
Cdd:COG5021    220 LTMRTNFLKLDTGNLSGEvQALLARYisikLVIKKLYLGPGPDASSRISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRL 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  758 PPGWEERQDEKGRSYYIDHNSRTTTWIKPVVQI-AMEAGQLPAAQNTSIARQPQATSGDSSQQSSNQQPEMEQGF----- 831
Cdd:COG5021    300 NSLFSTRADSFGRTYYLDHDRILTQYSRPLLEEtLGESTSFLVVNNDDSSSIKDLPHQVGSNPFLEAHPEFSELLknqsr 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  832 --------LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP-RLKIPAHLRRKTSLD-------PVDLGPLPPGWEERTHTDG 895
Cdd:COG5021    380 gttrdfrnKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLrREQLGRESDESFYVAsnvqqqrASREGPLLSGWKTRLNNLY 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  896 RIFFINHNTKKTQWEDPRLQNVA--ITGPAVPYSRDYKRKYEFFRKKLKKQSDIPnrFEMKIHRTTILEDSYRrIIAVKR 973
Cdd:COG5021    460 RFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKLFYSLKQKAKIFDPY--LHIKVRRDRVFEDSYR-EIMDES 536
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  974 ADFLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMA 1053
Cdd:COG5021    537 GDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKA 615
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1054 VYHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWILEN--DPAELDLRFIVDEELFGQTHQHELKSGGSEIV 1131
Cdd:COG5021    616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNdiDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1132 VTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGD-VDVADWKLHTKYKnGYSVNH 1210
Cdd:COG5021    696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDS 774
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1211 QVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTVEQWGTP-EKLPRAHTCFNRLDLPPYDSFED 1289
Cdd:COG5021    775 PIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEK 854
                          650
                   ....*....|....*.
gi 2024450188 1290 LWDKLLLAIENTQGFD 1305
Cdd:COG5021    855 LRSKLLTAINEGAGFG 870
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
951-1305 4.02e-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: 506.72  E-value: 4.02e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188  951 FEMKIHRTTILEDSYRRIIAVKRADfLKARLWIEFDGEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINP 1030
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1031 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDAFFIRPFYKMMLQKPITLHDMESVDSEYYNSLRWILENDP--AELDLRF 1108
Cdd:cd00078     80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGdeDDLELTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1109 -IVDEELFGQTHQHELKSGGSEIVVTNKNKRDYIHLVIQWRFVSRVQKQMAAFKEGFFELIPQDLIKIFDENELELLMCG 1187
Cdd:cd00078    159 tIELDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1188 LGDVDVADWKLHTKYKNGYSVNHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELygsngPQLFTVEQWGTP- 1266
Cdd:cd00078    239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2024450188 1267 EKLPRAHTCFNRLDLPPYDSFEDLWDKLLLAIENTQGFD 1305
Cdd:cd00078    314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1002-1305 1.94e-131

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 405.46  E-value: 1.94e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1002 FLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDAFFIRPFYKMMLQKPITLH 1080
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1081 DMESVDSEYYNSLRWIL---ENDPAELDLRFIVDEelFGQTHQHELKSGGSEIVVTNKNKRDYIHLVIQWRFVSRVQKQM 1157
Cdd:pfam00632   81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1158 AAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVADWKLHTKYKNGYSVNHQVIQWFWKAVLMMDSEKRIRLLQFVTG 1237
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024450188 1238 TSRVPMNGFAELygsngpQLFTVEQWGT--PEKLPRAHTCFNRLDLPPYDSFEDLWDKLLLAIENTQGFD 1305
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
504-557 2.13e-24

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


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 99.73  E-value: 2.13e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024450188  504 TRDDFLGQVDIPLYQLPTEHPSMERPYTFRDFVLHPRSHKSRVKGHLRLKMTYL 557
Cdd:cd04033     80 TRDDFLGQVEVPLNNLPTETPGNERRYTFKDYLLRPRSSKSRVKGHLRLYMAYL 133
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
882-914 6.56e-14

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: 66.47  E-value: 6.56e-14
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2024450188   882 PLPPGWEERTHTDGRIFFINHNTKKTQWEDPRL 914
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
884-914 4.30e-13

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: 64.09  E-value: 4.30e-13
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024450188  884 PPGWEERTHTDGRIFFINHNTKKTQWEDPRL 914
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
883-912 6.88e-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: 63.68  E-value: 6.88e-13
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  883 LPPGWEERTHTDGRIFFINHNTKKTQWEDP 912
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
756-787 7.53e-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: 60.69  E-value: 7.53e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2024450188   756 GLPPGWEERQDEKGRSYYIDHNSRTTTWIKPV 787
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
757-786 7.75e-12

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 60.60  E-value: 7.75e-12
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  757 LPPGWEERQDEKGRSYYIDHNSRTTTWIKP 786
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
833-863 2.57e-11

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 59.08  E-value: 2.57e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024450188  833 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 863
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
832-861 2.57e-11

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 59.06  E-value: 2.57e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  832 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 861
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
758-787 3.84e-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: 58.69  E-value: 3.84e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024450188  758 PPGWEERQDEKGRSYYIDHNSRTTTWIKPV 787
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
832-863 3.92e-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: 58.77  E-value: 3.92e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2024450188   832 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 863
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
602-629 4.92e-08

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: 49.81  E-value: 4.92e-08
                           10        20
                   ....*....|....*....|....*...
gi 2024450188  602 SGWEERQDILGRTYYVNHEFRRTQWKRP 629
Cdd:pfam00397    3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
602-630 6.17e-08

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


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 49.45  E-value: 6.17e-08
                           10        20
                   ....*....|....*....|....*....
gi 2024450188  602 SGWEERQDILGRTYYVNHEFRRTQWKRPT 630
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
602-630 1.54e-07

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: 48.75  E-value: 1.54e-07
                            10        20
                    ....*....|....*....|....*....
gi 2024450188   602 SGWEERQDILGRTYYVNHEFRRTQWKRPT 630
Cdd:smart00456    4 PGWEERKDPDGRPYYYNHETKETQWEKPR 32
PRP40 COG5104
Splicing factor [RNA processing and modification];
836-912 2.96e-04

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 45.07  E-value: 2.96e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024450188  836 WEVRHAPNGRPFFIDHNTKTTTWEDPRlKIPAHLRRKTSLDPvdlgplppgWEERTHTDGRIFFINHNTKKTQWEDP 912
Cdd:COG5104     17 WEELKAPDGRIYYYNKRTGKSSWEKPK-ELLKGSEEDLDVDP---------WKECRTADGKVYYYNSITRESRWKIP 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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