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Conserved domains on  [gi|578826356|ref|XP_006720407|]
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apoptosis-resistant E3 ubiquitin protein ligase 1 isoform X2 [Homo sapiens]

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 ...
476-810 2.01e-140

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: 417.79  E-value: 2.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   476 DWSKN-FEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFtRFSDNNQALVHPNPNRPAH-LRLKMYEFAGRLVGKCL 553
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLF-RYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   554 YEsslggayKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSE-MELVFAEeKYNKSGQLDKVVEL 632
Cdd:smart00119  80 YD-------NRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEeLDLTFSI-VLTSEFGQVKVVEL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   633 MTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVV 712
Cdd:smart00119 152 KPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   713 GGSWHFREKVmRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPT-HSTLPTAHTCFNQLCLPTYDS 791
Cdd:smart00119 232 GGYSANSQTI-KWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSdDERLPTAHTCFNRLKLPPYSS 310
                          330
                   ....*....|....*....
gi 578826356   792 YEEVHRMLQLAISEGcEGF 810
Cdd:smart00119 311 KEILREKLLLAINEG-KGF 328
Filamin super family cl44411
Filamin/ABP280 repeat;
56-144 2.05e-04

Filamin/ABP280 repeat;


The actual alignment was detected with superfamily member pfam00630:

Pssm-ID: 395505  Cd Length: 89  Bit Score: 40.74  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   56 DPRSCKVSWDWKdpyelfykngQPFPAHRPVGLRVHISHV--ELAVEI------PVTQEVLQEPNsNVVKVAFTVRKAGR 127
Cdd:pfam00630   3 DASKVKASGPGL----------EPGVVGKPAEFTVDTRDAggEGEVEVtgpdgsPVPVEVTDNGD-GTYTVSYTPTEPGD 71
                          90
                  ....*....|....*..
gi 578826356  128 YEITVKLGGLNVAYSPY 144
Cdd:pfam00630  72 YTVSVKFNGQHIPGSPF 88
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
476-810 2.01e-140

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: 417.79  E-value: 2.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   476 DWSKN-FEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFtRFSDNNQALVHPNPNRPAH-LRLKMYEFAGRLVGKCL 553
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLF-RYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   554 YEsslggayKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSE-MELVFAEeKYNKSGQLDKVVEL 632
Cdd:smart00119  80 YD-------NRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEeLDLTFSI-VLTSEFGQVKVVEL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   633 MTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVV 712
Cdd:smart00119 152 KPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   713 GGSWHFREKVmRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPT-HSTLPTAHTCFNQLCLPTYDS 791
Cdd:smart00119 232 GGYSANSQTI-KWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSdDERLPTAHTCFNRLKLPPYSS 310
                          330
                   ....*....|....*....
gi 578826356   792 YEEVHRMLQLAISEGcEGF 810
Cdd:smart00119 311 KEILREKLLLAINEG-KGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
454-811 7.21e-140

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: 417.35  E-value: 7.21e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 454 LKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFTRFSDNNQaLVHPNPNR 533
Cdd:cd00078    3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSG-LLYPNPSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 534 PAH-LRLKMYEFAGRLVGKCLYESslggaykQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNN-DMSEM 611
Cdd:cd00078   82 FADeDHLKLFRFLGRLLGKALYEG-------RLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDgDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 612 ELVFAEEKYNKSGQLdKVVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELE 691
Cdd:cd00078  155 ELTFTIELDSSFGGA-VTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 692 LLMCGTGDISVSDFKAHAVVVGGSWHFReKVMRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTH 771
Cdd:cd00078  234 LLICGSEDIDLEDLKKNTEYKGGYSSDS-PTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 578826356 772 ST-LPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGcEGFG 811
Cdd:cd00078  313 DDrLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
503-812 1.46e-97

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 305.69  E-value: 1.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356  503 LICKALFDTTNQLFTRfSDNNQALVHPNPNRPAHL---RLKMYEFAGRLVGKCLYESslggaykQLVRARFTRSFLAQII 579
Cdd:pfam00632   2 LLSKELFDPNYGLFEY-ETEDDRTYWFNPSSSESPdleLLDYFKFLGKLLGKAIYNG-------ILLDLPFPPFFYKKLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356  580 GLRMHYKYFETDDPEFYKSkVCFILNNDMS---EMELVFAEEKYNKSgqldKVVELMTGGAQTPVTNANKIFYLNLLAQY 656
Cdd:pfam00632  74 GEPLTLEDLESIDPELYKS-LKSLLNMDNDddeDLGLTFTIPVFGES----KTIELIPNGRNIPVTNENKEEYIRLYVDY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356  657 RLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVVGGsWHFREKVMRWFWTVVSSLTQE 736
Cdd:pfam00632 149 RLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGG-YTKNSPTIQWFWEILEEFSPE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578826356  737 ELARLLQFTTGSSQLPPGGFAALcPSFQI--IAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEgCEGFGM 812
Cdd:pfam00632 228 QRRLFLKFVTGSSRLPVGGFKSL-PKFTIvrKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE-GEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
426-813 1.30e-76

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 266.25  E-value: 1.30e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 426 SETFQDKVNFFQRELRQVHMkrphSKVTLKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELIC 505
Cdd:COG5021  493 KEDKRRKLFYSLKQKAKIFD----PYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLS 568
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 506 KALFDTTNQLFTrFSDNNQALVHPNPN---RPAHLRLkmYEFAGRLVGKCLYESslggaykQLVRARFTRSFLAQIIGLR 582
Cdd:COG5021  569 KEMFNPDYGLFE-YITEDLYTLPINPLssiNPEHLSY--FKFLGRVIGKAIYDS-------RILDVQFSKAFYKKLLGKP 638
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 583 MHYKYFETDDPEFYKSKVcFILNNDMSE--MELVFAEEkyNKSGQLDKVVELMTGGAQTPVTNANKIFYLNLLAQYRLAS 660
Cdd:COG5021  639 VSLVDLESLDPELYRSLV-WLLNNDIDEtiLDLTFTVE--DDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNK 715
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 661 QVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGD-ISVSDFKAHAVVVGgswhFRE--KVMRWFWTVVSSLTQEE 737
Cdd:COG5021  716 RVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHG----YTEdsPIIVWFWEIISEFDFEE 791
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 738 LARLLQFTTGSSQLPPGGFAALCPS-----FQIIAAPTHST-LPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGcEGFG 811
Cdd:COG5021  792 RAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG-AGFG 870

                 ..
gi 578826356 812 ML 813
Cdd:COG5021  871 LL 872
Filamin pfam00630
Filamin/ABP280 repeat;
56-144 2.05e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 40.74  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   56 DPRSCKVSWDWKdpyelfykngQPFPAHRPVGLRVHISHV--ELAVEI------PVTQEVLQEPNsNVVKVAFTVRKAGR 127
Cdd:pfam00630   3 DASKVKASGPGL----------EPGVVGKPAEFTVDTRDAggEGEVEVtgpdgsPVPVEVTDNGD-GTYTVSYTPTEPGD 71
                          90
                  ....*....|....*..
gi 578826356  128 YEITVKLGGLNVAYSPY 144
Cdd:pfam00630  72 YTVSVKFNGQHIPGSPF 88
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
476-810 2.01e-140

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: 417.79  E-value: 2.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   476 DWSKN-FEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFtRFSDNNQALVHPNPNRPAH-LRLKMYEFAGRLVGKCL 553
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLF-RYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   554 YEsslggayKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSE-MELVFAEeKYNKSGQLDKVVEL 632
Cdd:smart00119  80 YD-------NRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEeLDLTFSI-VLTSEFGQVKVVEL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   633 MTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVV 712
Cdd:smart00119 152 KPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   713 GGSWHFREKVmRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPT-HSTLPTAHTCFNQLCLPTYDS 791
Cdd:smart00119 232 GGYSANSQTI-KWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSdDERLPTAHTCFNRLKLPPYSS 310
                          330
                   ....*....|....*....
gi 578826356   792 YEEVHRMLQLAISEGcEGF 810
Cdd:smart00119 311 KEILREKLLLAINEG-KGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
454-811 7.21e-140

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: 417.35  E-value: 7.21e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 454 LKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFTRFSDNNQaLVHPNPNR 533
Cdd:cd00078    3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSG-LLYPNPSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 534 PAH-LRLKMYEFAGRLVGKCLYESslggaykQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNN-DMSEM 611
Cdd:cd00078   82 FADeDHLKLFRFLGRLLGKALYEG-------RLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDgDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 612 ELVFAEEKYNKSGQLdKVVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELE 691
Cdd:cd00078  155 ELTFTIELDSSFGGA-VTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 692 LLMCGTGDISVSDFKAHAVVVGGSWHFReKVMRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTH 771
Cdd:cd00078  234 LLICGSEDIDLEDLKKNTEYKGGYSSDS-PTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 578826356 772 ST-LPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGcEGFG 811
Cdd:cd00078  313 DDrLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
503-812 1.46e-97

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 305.69  E-value: 1.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356  503 LICKALFDTTNQLFTRfSDNNQALVHPNPNRPAHL---RLKMYEFAGRLVGKCLYESslggaykQLVRARFTRSFLAQII 579
Cdd:pfam00632   2 LLSKELFDPNYGLFEY-ETEDDRTYWFNPSSSESPdleLLDYFKFLGKLLGKAIYNG-------ILLDLPFPPFFYKKLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356  580 GLRMHYKYFETDDPEFYKSkVCFILNNDMS---EMELVFAEEKYNKSgqldKVVELMTGGAQTPVTNANKIFYLNLLAQY 656
Cdd:pfam00632  74 GEPLTLEDLESIDPELYKS-LKSLLNMDNDddeDLGLTFTIPVFGES----KTIELIPNGRNIPVTNENKEEYIRLYVDY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356  657 RLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVVGGsWHFREKVMRWFWTVVSSLTQE 736
Cdd:pfam00632 149 RLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGG-YTKNSPTIQWFWEILEEFSPE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578826356  737 ELARLLQFTTGSSQLPPGGFAALcPSFQI--IAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEgCEGFGM 812
Cdd:pfam00632 228 QRRLFLKFVTGSSRLPVGGFKSL-PKFTIvrKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE-GEGFGL 303
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
426-813 1.30e-76

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 266.25  E-value: 1.30e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 426 SETFQDKVNFFQRELRQVHMkrphSKVTLKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELIC 505
Cdd:COG5021  493 KEDKRRKLFYSLKQKAKIFD----PYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLS 568
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 506 KALFDTTNQLFTrFSDNNQALVHPNPN---RPAHLRLkmYEFAGRLVGKCLYESslggaykQLVRARFTRSFLAQIIGLR 582
Cdd:COG5021  569 KEMFNPDYGLFE-YITEDLYTLPINPLssiNPEHLSY--FKFLGRVIGKAIYDS-------RILDVQFSKAFYKKLLGKP 638
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 583 MHYKYFETDDPEFYKSKVcFILNNDMSE--MELVFAEEkyNKSGQLDKVVELMTGGAQTPVTNANKIFYLNLLAQYRLAS 660
Cdd:COG5021  639 VSLVDLESLDPELYRSLV-WLLNNDIDEtiLDLTFTVE--DDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNK 715
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 661 QVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGD-ISVSDFKAHAVVVGgswhFRE--KVMRWFWTVVSSLTQEE 737
Cdd:COG5021  716 RVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHG----YTEdsPIIVWFWEIISEFDFEE 791
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356 738 LARLLQFTTGSSQLPPGGFAALCPS-----FQIIAAPTHST-LPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGcEGFG 811
Cdd:COG5021  792 RAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDrLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEG-AGFG 870

                 ..
gi 578826356 812 ML 813
Cdd:COG5021  871 LL 872
Filamin pfam00630
Filamin/ABP280 repeat;
56-144 2.05e-04

Filamin/ABP280 repeat;


Pssm-ID: 395505  Cd Length: 89  Bit Score: 40.74  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826356   56 DPRSCKVSWDWKdpyelfykngQPFPAHRPVGLRVHISHV--ELAVEI------PVTQEVLQEPNsNVVKVAFTVRKAGR 127
Cdd:pfam00630   3 DASKVKASGPGL----------EPGVVGKPAEFTVDTRDAggEGEVEVtgpdgsPVPVEVTDNGD-GTYTVSYTPTEPGD 71
                          90
                  ....*....|....*..
gi 578826356  128 YEITVKLGGLNVAYSPY 144
Cdd:pfam00630  72 YTVSVKFNGQHIPGSPF 88
 
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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