|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
914-1243 |
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: 555.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 914 DFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 993
Cdd:smart00119 1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 994 YHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWI-LENDPTE-LDLRF-IIDEELFGQTHQHELKNGGSEIV 1070
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1071 VTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQ 1150
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1151 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGsngpqSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEEL 1229
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 114520607 1230 WDKLQMAIENTQGF 1243
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
821-853 |
2.06e-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: 62.23 E-value: 2.06e-12
10 20 30
....*....|....*....|....*....|...
gi 114520607 821 PLPPGWEERTHTDGRIFYINHNIKRTQWEDPRL 853
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
697-726 |
1.33e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
:
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 59.83 E-value: 1.33e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 697 LPPGWEEKQDERGRSYYVDHNSRTTTWTKP 726
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
539-571 |
1.71e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
:
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 59.54 E-value: 1.71e-11
10 20 30
....*....|....*....|....*....|...
gi 114520607 539 PLPPGWEERQDILGRTYYVNHESRRTQWKRPTP 571
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
770-799 |
4.24e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
:
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 58.67 E-value: 4.24e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 770 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 799
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
914-1243 |
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: 555.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 914 DFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 993
Cdd:smart00119 1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 994 YHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWI-LENDPTE-LDLRF-IIDEELFGQTHQHELKNGGSEIV 1070
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1071 VTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQ 1150
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1151 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGsngpqSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEEL 1229
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 114520607 1230 WDKLQMAIENTQGF 1243
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
890-1244 |
3.82e-173 |
|
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: 515.58 E-value: 3.82e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 890 FEMKLRRATVLEDSYRRIMGVKRADfLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINP 969
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 970 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWILENDPT--ELDLRF 1047
Cdd:cd00078 80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1048 IID-EELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCG 1126
Cdd:cd00078 159 TIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1127 LGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELygsngPQSFTVEQWGTP- 1205
Cdd:cd00078 239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 114520607 1206 EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1244
Cdd:cd00078 314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
665-1244 |
4.47e-166 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 516.63 E-value: 4.47e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 665 SSSNHSSRRGSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNSRTTTWTKPTVQatvETSQLTSSQSSA 744
Cdd:COG5021 267 ISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLE---ETLGESTSFLVV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 745 GPQSQASTSDSGQQVTQPSEIE-----------QGFL--------PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPA 805
Cdd:COG5021 344 NNDDSSSIKDLPHQVGSNPFLEahpefsellknQSRGttrdfrnkPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 806 HLRGKTSLDTSN-------DLGPLPPGWEERTHTDGRIFYINHNIKRTQWEDPRLENVA--ITGPAVPYSRDYKRKYeFF 876
Cdd:COG5021 424 RESDESFYVASNvqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKL-FY 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 877 RRKLKKQNdIPNKFEMKLRRATVLEDSYRRIMGvKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFE 956
Cdd:COG5021 503 SLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 957 YSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWIL 1036
Cdd:COG5021 581 YITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1037 EN--DPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKI 1114
Cdd:COG5021 660 NNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1115 FDENELELLMCGLGD-VDVNDWREHTKYKnGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNG 1193
Cdd:COG5021 740 FDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDG 818
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 114520607 1194 PQSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1244
Cdd:COG5021 819 VRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFG 870
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
941-1244 |
6.28e-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: 408.54 E-value: 6.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 941 FLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLH 1019
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1020 DMESVDSEYYNSLRWIL---ENDPTELDLRFIIDEelFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQM 1096
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1097 AAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTG 1176
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1177 TSRVPMNGFAELygsngpQSFTVEQWGT--PEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1244
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
821-853 |
2.06e-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: 62.23 E-value: 2.06e-12
10 20 30
....*....|....*....|....*....|...
gi 114520607 821 PLPPGWEERTHTDGRIFYINHNIKRTQWEDPRL 853
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
823-853 |
9.06e-12 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 60.62 E-value: 9.06e-12
10 20 30
....*....|....*....|....*....|.
gi 114520607 823 PPGWEERTHTDGRIFYINHNIKRTQWEDPRL 853
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
697-726 |
1.33e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 59.83 E-value: 1.33e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 697 LPPGWEEKQDERGRSYYVDHNSRTTTWTKP 726
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
539-571 |
1.71e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 59.54 E-value: 1.71e-11
10 20 30
....*....|....*....|....*....|...
gi 114520607 539 PLPPGWEERQDILGRTYYVNHESRRTQWKRPTP 571
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
822-851 |
2.79e-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: 2.79e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 822 LPPGWEERTHTDGRIFYINHNIKRTQWEDP 851
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
770-799 |
4.24e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 58.67 E-value: 4.24e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 770 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 799
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
771-801 |
4.37e-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: 4.37e-11
10 20 30
....*....|....*....|....*....|.
gi 114520607 771 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 801
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
696-727 |
6.16e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 58.00 E-value: 6.16e-11
10 20 30
....*....|....*....|....*....|..
gi 114520607 696 GLPPGWEEKQDERGRSYYVDHNSRTTTWTKPT 727
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
770-801 |
8.18e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 57.61 E-value: 8.18e-11
10 20 30
....*....|....*....|....*....|..
gi 114520607 770 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 801
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
540-569 |
9.83e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 57.51 E-value: 9.83e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 540 LPPGWEERQDILGRTYYVNHESRRTQWKRP 569
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
541-571 |
1.13e-10 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.15 E-value: 1.13e-10
10 20 30
....*....|....*....|....*....|.
gi 114520607 541 PPGWEERQDILGRTYYVNHESRRTQWKRPTP 571
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
698-727 |
1.57e-10 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 56.77 E-value: 1.57e-10
10 20 30
....*....|....*....|....*....|
gi 114520607 698 PPGWEEKQDERGRSYYVDHNSRTTTWTKPT 727
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
914-1243 |
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: 555.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 914 DFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDnYTLQINPNSGLCNEDHLSYFKFIGRVAGMAV 993
Cdd:smart00119 1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 994 YHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWI-LENDPTE-LDLRF-IIDEELFGQTHQHELKNGGSEIV 1070
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEeLDLTFsIVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1071 VTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQ 1150
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1151 VIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGsngpqSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEEL 1229
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 114520607 1230 WDKLQMAIENTQGF 1243
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
890-1244 |
3.82e-173 |
|
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: 515.58 E-value: 3.82e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 890 FEMKLRRATVLEDSYRRIMGVKRADfLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINP 969
Cdd:cd00078 1 LKITVRRDRILEDALRQLSKVSSSD-LKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 970 NSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWILENDPT--ELDLRF 1047
Cdd:cd00078 80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDedDLELTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1048 IID-EELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCG 1126
Cdd:cd00078 159 TIElDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1127 LGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELygsngPQSFTVEQWGTP- 1205
Cdd:cd00078 239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADL-----NPKFTIRRVGSPd 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 114520607 1206 EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1244
Cdd:cd00078 314 DRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
665-1244 |
4.47e-166 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 516.63 E-value: 4.47e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 665 SSSNHSSRRGSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNSRTTTWTKPTVQatvETSQLTSSQSSA 744
Cdd:COG5021 267 ISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLE---ETLGESTSFLVV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 745 GPQSQASTSDSGQQVTQPSEIE-----------QGFL--------PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPA 805
Cdd:COG5021 344 NNDDSSSIKDLPHQVGSNPFLEahpefsellknQSRGttrdfrnkPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 806 HLRGKTSLDTSN-------DLGPLPPGWEERTHTDGRIFYINHNIKRTQWEDPRLENVA--ITGPAVPYSRDYKRKYeFF 876
Cdd:COG5021 424 RESDESFYVASNvqqqrasREGPLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSRLGSFIslNKLDIRRIKEDKRRKL-FY 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 877 RRKLKKQNdIPNKFEMKLRRATVLEDSYRRIMGvKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFE 956
Cdd:COG5021 503 SLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMD-ESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 957 YSATDNYTLQINPNSGLcNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWIL 1036
Cdd:COG5021 581 YITEDLYTLPINPLSSI-NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1037 EN--DPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKI 1114
Cdd:COG5021 660 NNdiDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQI 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1115 FDENELELLMCGLGD-VDVNDWREHTKYKnGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNG 1193
Cdd:COG5021 740 FDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDG 818
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 114520607 1194 PQSFTVEQWGTP-EKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1244
Cdd:COG5021 819 VRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFG 870
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
941-1244 |
6.28e-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: 408.54 E-value: 6.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 941 FLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCN-EDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLH 1019
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPdLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1020 DMESVDSEYYNSLRWIL---ENDPTELDLRFIIDEelFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQM 1096
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmdNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1097 AAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTG 1176
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114520607 1177 TSRVPMNGFAELygsngpQSFTVEQWGT--PEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFD 1244
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGGddDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
821-853 |
2.06e-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: 62.23 E-value: 2.06e-12
10 20 30
....*....|....*....|....*....|...
gi 114520607 821 PLPPGWEERTHTDGRIFYINHNIKRTQWEDPRL 853
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
823-853 |
9.06e-12 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 60.62 E-value: 9.06e-12
10 20 30
....*....|....*....|....*....|.
gi 114520607 823 PPGWEERTHTDGRIFYINHNIKRTQWEDPRL 853
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
697-726 |
1.33e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 59.83 E-value: 1.33e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 697 LPPGWEEKQDERGRSYYVDHNSRTTTWTKP 726
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
539-571 |
1.71e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 59.54 E-value: 1.71e-11
10 20 30
....*....|....*....|....*....|...
gi 114520607 539 PLPPGWEERQDILGRTYYVNHESRRTQWKRPTP 571
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
822-851 |
2.79e-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: 2.79e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 822 LPPGWEERTHTDGRIFYINHNIKRTQWEDP 851
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
770-799 |
4.24e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 58.67 E-value: 4.24e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 770 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDP 799
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
771-801 |
4.37e-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: 4.37e-11
10 20 30
....*....|....*....|....*....|.
gi 114520607 771 PKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 801
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
696-727 |
6.16e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 58.00 E-value: 6.16e-11
10 20 30
....*....|....*....|....*....|..
gi 114520607 696 GLPPGWEEKQDERGRSYYVDHNSRTTTWTKPT 727
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
770-801 |
8.18e-11 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 57.61 E-value: 8.18e-11
10 20 30
....*....|....*....|....*....|..
gi 114520607 770 LPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRL 801
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
540-569 |
9.83e-11 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 57.51 E-value: 9.83e-11
10 20 30
....*....|....*....|....*....|
gi 114520607 540 LPPGWEERQDILGRTYYVNHESRRTQWKRP 569
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
541-571 |
1.13e-10 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.15 E-value: 1.13e-10
10 20 30
....*....|....*....|....*....|.
gi 114520607 541 PPGWEERQDILGRTYYVNHESRRTQWKRPTP 571
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
698-727 |
1.57e-10 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 56.77 E-value: 1.57e-10
10 20 30
....*....|....*....|....*....|
gi 114520607 698 PPGWEEKQDERGRSYYVDHNSRTTTWTKPT 727
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
774-851 |
1.81e-04 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 45.84 E-value: 1.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114520607 774 WEVRHAPNGRPFFIDHNTKTTTWEDPRlkipaHLRGKTSLDTSNDlgplppGWEERTHTDGRIFYINHNIKRTQWEDP 851
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPK-----ELLKGSEEDLDVD------PWKECRTADGKVYYYNSITRESRWKIP 83
|
|
| |
