|
Name |
Accession |
Description |
Interval |
E-value |
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
246-787 |
2.00e-178 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.35 E-value: 2.00e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 246 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 318
Cdd:COG5021 297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 319 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 372
Cdd:COG5021 377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 373 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 452
Cdd:COG5021 457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 453 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 532
Cdd:COG5021 536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 533 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 612
Cdd:COG5021 616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 613 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 691
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 692 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 770
Cdd:COG5021 776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
|
570
....*....|....*..
gi 443906717 771 KEKLLFAIEETEGFGQE 787
Cdd:COG5021 856 RSKLLTAINEGAGFGLL 872
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
433-785 |
9.18e-171 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 495.55 E-value: 9.18e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 433 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 512
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 513 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 592
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 593 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 671
Cdd:cd00078 162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 672 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 749
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 443906717 750 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 785
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
456-784 |
2.30e-160 |
|
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: 468.25 E-value: 2.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 456 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 533
Cdd:smart00119 1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 534 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 612
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 613 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 691
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 692 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 770
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 443906717 771 KEKLLFAIEETEGF 784
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
482-785 |
3.87e-121 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 366.16 E-value: 3.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 482 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 559
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 560 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 637
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 638 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 716
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 443906717 717 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 785
Cdd:pfam00632 238 GSSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
216-245 |
4.69e-13 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 63.68 E-value: 4.69e-13
10 20 30
....*....|....*....|....*....|
gi 443906717 216 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 245
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
216-247 |
2.21e-12 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 61.85 E-value: 2.21e-12
10 20 30
....*....|....*....|....*....|..
gi 443906717 216 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 247
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
217-247 |
2.54e-12 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 61.39 E-value: 2.54e-12
10 20 30
....*....|....*....|....*....|.
gi 443906717 217 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 247
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
3-250 |
1.29e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 51.88 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 3 RAADCKCDPTDHLGVP--SLESPHfKGRCSIRKSNSGLETSAVNTQQKMLPVEGTIgidnhVSTNTVVPNSCCSHVVNGE 80
Cdd:pfam17823 146 RAAACRANASAAPRAAiaAASAPH-AASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATAT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 81 NTPSSPSQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEH 160
Cdd:pfam17823 220 GHPAAGTALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKH 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 161 SECIPSAS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYV 233
Cdd:pfam17823 286 MPSDTMARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPV 365
|
250 260
....*....|....*....|...
gi 443906717 234 DHNTR------TTTWERPQPLPP 250
Cdd:pfam17823 366 LHTSMipeveaTSPTTQPSPLLP 388
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
246-787 |
2.00e-178 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 534.35 E-value: 2.00e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 246 QPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQF------NQRYLYSASMLAAEND- 318
Cdd:COG5021 297 LRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVVNNDDSSSIKDlphqvgSNPFLEAHPEFSELLKn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 319 -------PYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL-------------------PNEEPLPEGWEIRYT 372
Cdd:COG5021 377 qsrgttrDFRNKPTGWSSSIEDLGQFLFSDFLTSSSTYEDLRREQLgresdesfyvasnvqqqraSREGPLLSGWKTRLN 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 373 REGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNaLPSHVKINVSRQTLFEDSFQQIMAL 452
Cdd:COG5021 457 NLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYREIMDE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 453 KPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMA 532
Cdd:COG5021 536 SGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 533 LFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNIL 612
Cdd:COG5021 616 IYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNIS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 613 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE-VDLADWQRNTVYRHYTRNSK 691
Cdd:COG5021 696 VTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSP 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 692 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 770
Cdd:COG5021 776 IIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYSSKEKL 855
|
570
....*....|....*..
gi 443906717 771 KEKLLFAIEETEGFGQE 787
Cdd:COG5021 856 RSKLLTAINEGAGFGLL 872
|
|
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
433-785 |
9.18e-171 |
|
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.
Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 495.55 E-value: 9.18e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 433 KINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPAS 512
Cdd:cd00078 2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 513 TINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVD 592
Cdd:cd00078 82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 593 MEI-LGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQE 671
Cdd:cd00078 162 LDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 672 VDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMgsngpQKFCIEKVGK-DTWL 749
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 443906717 750 PRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 785
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
456-784 |
2.30e-160 |
|
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: 468.25 E-value: 2.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 456 DLR-RRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAgKNNYCLQINP-ASTINPDHLSYFCFIGRFIAMAL 533
Cdd:smart00119 1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPrSGFANEEHLSYFRFIGRVLGKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 534 FHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFS-VDMEILGKVTSHDLKLGGSNIL 612
Cdd:smart00119 80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSiVLTSEFGQVKVVELKPGGSNIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 613 VTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSK 691
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 692 QIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGsngpqKFCIEKVG-KDTWLPRSHTCFNRLDLPPYKSYEQL 770
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314
|
330
....*....|....
gi 443906717 771 KEKLLFAIEETEGF 784
Cdd:smart00119 315 REKLLLAINEGKGF 328
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
482-785 |
3.87e-121 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 366.16 E-value: 3.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 482 FLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDH--LSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIK 559
Cdd:pfam00632 1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 560 DLESIDTEFYNSLIWIR--DNNIEECgLEMYFSVDmeILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQ 637
Cdd:pfam00632 81 DLESIDPELYKSLKSLLnmDNDDDED-LGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 638 TKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRH-YTRNSKQIIWFWQFVKETDNEVRMRLLQFVT 716
Cdd:pfam00632 158 LEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 443906717 717 GTCRLPLGGFAELmgsngpQKFCIEKVG--KDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFG 785
Cdd:pfam00632 238 GSSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFG 302
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
216-245 |
4.69e-13 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 63.68 E-value: 4.69e-13
10 20 30
....*....|....*....|....*....|
gi 443906717 216 LPSGWEQRKDPHGRTYYVDHNTRTTTWERP 245
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
248-277 |
1.62e-12 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.14 E-value: 1.62e-12
10 20 30
....*....|....*....|....*....|
gi 443906717 248 LPPGWERRVDDRGRVYYVDHNTRTTTWQRP 277
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
216-247 |
2.21e-12 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 61.85 E-value: 2.21e-12
10 20 30
....*....|....*....|....*....|..
gi 443906717 216 LPSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 247
Cdd:smart00456 2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
217-247 |
2.54e-12 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 61.39 E-value: 2.54e-12
10 20 30
....*....|....*....|....*....|.
gi 443906717 217 PSGWEQRKDPHGRTYYVDHNTRTTTWERPQP 247
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
323-352 |
3.44e-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: 60.98 E-value: 3.44e-12
10 20 30
....*....|....*....|....*....|
gi 443906717 323 LPPGWEKRVDSTDRVYFVNHNTKTTQWEDP 352
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
324-353 |
1.47e-11 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 59.46 E-value: 1.47e-11
10 20 30
....*....|....*....|....*....|
gi 443906717 324 PPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 353
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
322-353 |
1.61e-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: 59.15 E-value: 1.61e-11
10 20 30
....*....|....*....|....*....|..
gi 443906717 322 PLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPR 353
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
249-279 |
1.84e-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: 59.08 E-value: 1.84e-11
10 20 30
....*....|....*....|....*....|.
gi 443906717 249 PPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 279
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
247-279 |
3.28e-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: 3.28e-11
10 20 30
....*....|....*....|....*....|...
gi 443906717 247 PLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTM 279
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
215-297 |
1.20e-09 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 61.63 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 215 ALPSG-----WEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDD---------RGRVYYVDHNTRTTTWQRPTME 280
Cdd:COG5104 7 GMASGearseWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdpwkecrtaDGKVYYYNSITRESRWKIPPER 86
|
90
....*....|....*....
gi 443906717 281 SVRN--FEQWQSQRNQLQG 297
Cdd:COG5104 87 KKVEpiAEQKHDERSMIGG 105
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
364-393 |
2.01e-08 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 50.22 E-value: 2.01e-08
10 20 30
....*....|....*....|....*....|
gi 443906717 364 PEGWEIRYTREGVRYFVDHNTRTTTFKDPR 393
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
362-394 |
2.76e-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: 49.91 E-value: 2.76e-08
10 20 30
....*....|....*....|....*....|...
gi 443906717 362 PLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRN 394
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
363-392 |
1.51e-07 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 47.88 E-value: 1.51e-07
10 20 30
....*....|....*....|....*....|
gi 443906717 363 LPEGWEIRYTREGVRYFVDHNTRTTTFKDP 392
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
3-250 |
1.29e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 51.88 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 3 RAADCKCDPTDHLGVP--SLESPHfKGRCSIRKSNSGLETSAVNTQQKMLPVEGTIgidnhVSTNTVVPNSCCSHVVNGE 80
Cdd:pfam17823 146 RAAACRANASAAPRAAiaAASAPH-AASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATAT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 81 NTPSSPSQVAARPKNAPAPKPVTSAptsdtVNGESSSVLADNTSTMGTLLPSEDTTSTSNctstttqepPVQEPPASSEH 160
Cdd:pfam17823 220 GHPAAGTALAAVGNSSPAAGTVTAA-----VGTVTPAALATLAAAAGTVASAAGTINMGD---------PHARRLSPAKH 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443906717 161 SECIPSAS---AEVGPEAR---SLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQS-GNTNTEALPSGWEQRKDPHGRTYYV 233
Cdd:pfam17823 286 MPSDTMARnpaAPMGAQAQgpiIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSvASTNLAVVTTTKAQAKEPSASPVPV 365
|
250 260
....*....|....*....|...
gi 443906717 234 DHNTR------TTTWERPQPLPP 250
Cdd:pfam17823 366 LHTSMipeveaTSPTTQPSPLLP 388
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
327-392 |
4.18e-03 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 40.45 E-value: 4.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 443906717 327 WEKRVDSTDRVYFVNHNTKTTQWEDPRTQGLPNEEPLPE-GWEIRYTREGVRYFVDHNTRTTTFKDP 392
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVdPWKECRTADGKVYYYNSITRESRWKIP 83
|
|
| |
