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Conserved domains on  [gi|19114290|ref|NP_593378|]
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ubiquitin-protein ligase E3 [Schizosaccharomyces pombe]

Protein Classification

HECT-type E3 ubiquitin transferase( domain architecture ID 11472073)

HECT-type E3 ubiquitin transferase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester, and then directly transfers the ubiquitin to targeted substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
155-1029 0e+00

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


:

Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 844.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  155 SNSNDSWLWQRFSSLLLNCLVSSINSHRIEGTDTSAETSLLHCLAYVAPYLKSSELSTYYDSVMTFYAQIYPKQNMTNLE 234
Cdd:COG5021    1 DLRVGGLLLEDLSCRLFSELFRSNSSVRAEFDLSKDESGVRNSLDYGAAGNKNMSLSDEKGLVRSSIAALDGLQNRDCLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  235 DIMSLSLLTPVSSKTDENANSSSAFLFHVLASDCFSsieNCIPPDLIIDKVFSSSLQLSEEACISSLLNLGMIKVFS-LA 313
Cdd:COG5021   81 SLDPLSVLSVDGLQTSETSFRSSALNPYVNEFLCEN---DVRLSSSITIQVSDESKQNVIEDVFSGLENLGSVDVLStEA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  314 GNCLHLLHTEYKNSSLWKFCSYILDALYVFSGESVNSRIQVVSDVDDDEDDENAFSQNYYSHLQMVAKHFSKNYANQSGI 393
Cdd:COG5021  158 TKGIDFLEILITRDFLFSSCSLNSDFLKIISGSSVKSRKLAVSNVEKSEPDNVLFGLPYRSALTMRTNFLKLDTGNLSGE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  394 VQRSFAECISSTFITKafKLVSSNTLQAMSHFYATMIKLFPSNRTSILMYISLVETNEGSLTRSFSRFSWDMFSESPVYQ 473
Cdd:COG5021  238 VQALLARYISIKLVIK--KLYLGPGPDASSRISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYY 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  474 LFHKKFDVQNVLKNDSGYWFQLQLLIDVYSrMLFTMIDDEFHNDKQNPLYPVMAEFCTVLKNLVLGLYWDVQAAKDVDCK 553
Cdd:COG5021  316 LDHDRILTQYSRPLLEETLGESTSFLVVNN-DDSSSIKDLPHQVGSNPFLEAHPEFSELLKNQSRGTTRDFRNKPTGWSS 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  554 SVVDISQLRVSSTSLLQQLYRINSRKQFLPEDFFLMSEYFNLNEFeaNALQESELASHAEAEINITYKFDNFSESRPRLN 633
Cdd:COG5021  395 SIEDLGQFLFSDFLTSSSTYEDLRREQLGRESDESFYVASNVQQQ--RASREGPLLSGWKTRLNNLYRFYFVEHRKKTLT 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  634 ILNN---CSFFLP--FHFRIHLLQQLLLLDKQANgYAQPFGHLKHAVIRRNRIFDDGFDAFYNFGKLLKGPiritFVDEH 708
Cdd:COG5021  473 KNDSrlgSFISLNklDIRRIKEDKRRKLFYSLKQ-KAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKK----TLEIE 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  709 GVVEEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAHLLYPNTHAYAQ-DVERLRCYEFLGMLIGKCIYEGIQIDAAFA 787
Cdd:COG5021  548 FVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSiNPEHLSYFKFLGRVIGKAIYDSRILDVQFS 627
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  788 SFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVENdMALNFTVVHEEFGVRNVIDLIPNGSNISVTNENRLQYIH 867
Cdd:COG5021  628 KAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVK 706
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  868 LVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVPIDIDDLRRHTVYaGGYEPNSPTIVLFWEVLR 947
Cdd:COG5021  707 KVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIIS 785
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  948 EFEEEDKRSFVKFVTSVARPPILGFKALMPS-----FCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRS 1022
Cdd:COG5021  786 EFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINE 865

                 ....*..
gi 19114290 1023 GVGFGFS 1029
Cdd:COG5021  866 GAGFGLL 872
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
155-1029 0e+00

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 844.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  155 SNSNDSWLWQRFSSLLLNCLVSSINSHRIEGTDTSAETSLLHCLAYVAPYLKSSELSTYYDSVMTFYAQIYPKQNMTNLE 234
Cdd:COG5021    1 DLRVGGLLLEDLSCRLFSELFRSNSSVRAEFDLSKDESGVRNSLDYGAAGNKNMSLSDEKGLVRSSIAALDGLQNRDCLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  235 DIMSLSLLTPVSSKTDENANSSSAFLFHVLASDCFSsieNCIPPDLIIDKVFSSSLQLSEEACISSLLNLGMIKVFS-LA 313
Cdd:COG5021   81 SLDPLSVLSVDGLQTSETSFRSSALNPYVNEFLCEN---DVRLSSSITIQVSDESKQNVIEDVFSGLENLGSVDVLStEA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  314 GNCLHLLHTEYKNSSLWKFCSYILDALYVFSGESVNSRIQVVSDVDDDEDDENAFSQNYYSHLQMVAKHFSKNYANQSGI 393
Cdd:COG5021  158 TKGIDFLEILITRDFLFSSCSLNSDFLKIISGSSVKSRKLAVSNVEKSEPDNVLFGLPYRSALTMRTNFLKLDTGNLSGE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  394 VQRSFAECISSTFITKafKLVSSNTLQAMSHFYATMIKLFPSNRTSILMYISLVETNEGSLTRSFSRFSWDMFSESPVYQ 473
Cdd:COG5021  238 VQALLARYISIKLVIK--KLYLGPGPDASSRISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYY 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  474 LFHKKFDVQNVLKNDSGYWFQLQLLIDVYSrMLFTMIDDEFHNDKQNPLYPVMAEFCTVLKNLVLGLYWDVQAAKDVDCK 553
Cdd:COG5021  316 LDHDRILTQYSRPLLEETLGESTSFLVVNN-DDSSSIKDLPHQVGSNPFLEAHPEFSELLKNQSRGTTRDFRNKPTGWSS 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  554 SVVDISQLRVSSTSLLQQLYRINSRKQFLPEDFFLMSEYFNLNEFeaNALQESELASHAEAEINITYKFDNFSESRPRLN 633
Cdd:COG5021  395 SIEDLGQFLFSDFLTSSSTYEDLRREQLGRESDESFYVASNVQQQ--RASREGPLLSGWKTRLNNLYRFYFVEHRKKTLT 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  634 ILNN---CSFFLP--FHFRIHLLQQLLLLDKQANgYAQPFGHLKHAVIRRNRIFDDGFDAFYNFGKLLKGPiritFVDEH 708
Cdd:COG5021  473 KNDSrlgSFISLNklDIRRIKEDKRRKLFYSLKQ-KAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKK----TLEIE 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  709 GVVEEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAHLLYPNTHAYAQ-DVERLRCYEFLGMLIGKCIYEGIQIDAAFA 787
Cdd:COG5021  548 FVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSiNPEHLSYFKFLGRVIGKAIYDSRILDVQFS 627
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  788 SFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVENdMALNFTVVHEEFGVRNVIDLIPNGSNISVTNENRLQYIH 867
Cdd:COG5021  628 KAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVK 706
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  868 LVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVPIDIDDLRRHTVYaGGYEPNSPTIVLFWEVLR 947
Cdd:COG5021  707 KVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIIS 785
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  948 EFEEEDKRSFVKFVTSVARPPILGFKALMPS-----FCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRS 1022
Cdd:COG5021  786 EFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINE 865

                 ....*..
gi 19114290 1023 GVGFGFS 1029
Cdd:COG5021  866 GAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
676-1027 5.70e-148

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: 444.32  E-value: 5.70e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  676 IRRNRIFDDGFDAFYNFG-KLLKGPIRITFVDEhgvveEGIDGGGLTKEFLTSICKTVFDINYGLF--SETKAHLLYPNT 752
Cdd:cd00078    5 VRRDRILEDALRQLSKVSsSDLKKVLEVEFVGE-----EGIDAGGVTREFFTLVSKELFNPSYGLFryTPDDSGLLYPNP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  753 HAYAqDVERLRCYEFLGMLIGKCIYEGIQIDAAFASFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVEnDMALN 832
Cdd:cd00078   80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDED-DLELT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  833 FTVVHEE-FGVRNVIDLIPNGSNISVTNENRLQYIHLVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVG 911
Cdd:cd00078  158 FTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLIC 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  912 GDPvPIDIDDLRRHTVYAGGYEPNSPTIVLFWEVLREFEEEDKRSFVKFVTSVARPPILGFKALMPSFCIRVNGEDETRL 991
Cdd:cd00078  238 GSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRL 316
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 19114290  992 PTASTCVNLLKLPMYSTKQTLRDKLLTAVRSGVGFG 1027
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
695-1026 2.33e-143

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: 431.66  E-value: 2.33e-143
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     695 LLKGPIRITFVDEhgvveEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAH-LLYPNTHAYAQDVERLRCYEFLGMLIG 773
Cdd:smart00119    2 LKKRVLEIEFEGE-----EGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFANEEHLSYFRFIGRVLG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     774 KCIYEGIQIDAAFASFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKnYDGDVENDMALNFT-VVHEEFGVRNVIDLIPNG 852
Cdd:smart00119   77 KALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQVKVVELKPGG 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     853 SNISVTNENRLQYIHLVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPvPIDIDDLRRHTVYAGGY 932
Cdd:smart00119  156 SNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYKGGY 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     933 EPNSPTIVLFWEVLREFEEEDKRSFVKFVTSVARPPILGFKALMPSFCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTL 1012
Cdd:smart00119  235 SANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 19114290    1013 RDKLLTAVRSGVGF 1026
Cdd:smart00119  315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
726-1029 1.64e-113

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 352.68  E-value: 1.64e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290    726 TSICKTVFDINYGLFSE--TKAHLLYPNTHAYAQ-DVERLRCYEFLGMLIGKCIYEGIQIDAAFASFFVAKWLGHPSYFD 802
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYetEDDRTYWFNPSSSESpDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290    803 DLTSLDPNLYEGLVFLKNYDGDVENDMALNFTVvhEEFGVRNVIDLIPNGSNISVTNENRLQYIHLVSNYYLNARLSRQC 882
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290    883 RAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVpIDIDDLRRHTVYAGGYEPNSPTIVLFWEVLREFEEEDKRSFVKFVT 962
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114290    963 SVARPPILGFKALmPSFCI-RVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRSGVGFGFS 1029
Cdd:pfam00632  238 GSSRLPVGGFKSL-PKFTIvRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
155-1029 0e+00

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 844.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  155 SNSNDSWLWQRFSSLLLNCLVSSINSHRIEGTDTSAETSLLHCLAYVAPYLKSSELSTYYDSVMTFYAQIYPKQNMTNLE 234
Cdd:COG5021    1 DLRVGGLLLEDLSCRLFSELFRSNSSVRAEFDLSKDESGVRNSLDYGAAGNKNMSLSDEKGLVRSSIAALDGLQNRDCLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  235 DIMSLSLLTPVSSKTDENANSSSAFLFHVLASDCFSsieNCIPPDLIIDKVFSSSLQLSEEACISSLLNLGMIKVFS-LA 313
Cdd:COG5021   81 SLDPLSVLSVDGLQTSETSFRSSALNPYVNEFLCEN---DVRLSSSITIQVSDESKQNVIEDVFSGLENLGSVDVLStEA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  314 GNCLHLLHTEYKNSSLWKFCSYILDALYVFSGESVNSRIQVVSDVDDDEDDENAFSQNYYSHLQMVAKHFSKNYANQSGI 393
Cdd:COG5021  158 TKGIDFLEILITRDFLFSSCSLNSDFLKIISGSSVKSRKLAVSNVEKSEPDNVLFGLPYRSALTMRTNFLKLDTGNLSGE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  394 VQRSFAECISSTFITKafKLVSSNTLQAMSHFYATMIKLFPSNRTSILMYISLVETNEGSLTRSFSRFSWDMFSESPVYQ 473
Cdd:COG5021  238 VQALLARYISIKLVIK--KLYLGPGPDASSRISTLIIRLSNTNLNRRLSYILSHSSFEDSLLRLNSLFSTRADSFGRTYY 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  474 LFHKKFDVQNVLKNDSGYWFQLQLLIDVYSrMLFTMIDDEFHNDKQNPLYPVMAEFCTVLKNLVLGLYWDVQAAKDVDCK 553
Cdd:COG5021  316 LDHDRILTQYSRPLLEETLGESTSFLVVNN-DDSSSIKDLPHQVGSNPFLEAHPEFSELLKNQSRGTTRDFRNKPTGWSS 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  554 SVVDISQLRVSSTSLLQQLYRINSRKQFLPEDFFLMSEYFNLNEFeaNALQESELASHAEAEINITYKFDNFSESRPRLN 633
Cdd:COG5021  395 SIEDLGQFLFSDFLTSSSTYEDLRREQLGRESDESFYVASNVQQQ--RASREGPLLSGWKTRLNNLYRFYFVEHRKKTLT 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  634 ILNN---CSFFLP--FHFRIHLLQQLLLLDKQANgYAQPFGHLKHAVIRRNRIFDDGFDAFYNFGKLLKGPiritFVDEH 708
Cdd:COG5021  473 KNDSrlgSFISLNklDIRRIKEDKRRKLFYSLKQ-KAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKK----TLEIE 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  709 GVVEEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAHLLYPNTHAYAQ-DVERLRCYEFLGMLIGKCIYEGIQIDAAFA 787
Cdd:COG5021  548 FVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSiNPEHLSYFKFLGRVIGKAIYDSRILDVQFS 627
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  788 SFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVENdMALNFTVVHEEFGVRNVIDLIPNGSNISVTNENRLQYIH 867
Cdd:COG5021  628 KAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETI-LDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVK 706
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  868 LVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVPIDIDDLRRHTVYaGGYEPNSPTIVLFWEVLR 947
Cdd:COG5021  707 KVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIIS 785
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  948 EFEEEDKRSFVKFVTSVARPPILGFKALMPS-----FCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRS 1022
Cdd:COG5021  786 EFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINE 865

                 ....*..
gi 19114290 1023 GVGFGFS 1029
Cdd:COG5021  866 GAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
676-1027 5.70e-148

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: 444.32  E-value: 5.70e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  676 IRRNRIFDDGFDAFYNFG-KLLKGPIRITFVDEhgvveEGIDGGGLTKEFLTSICKTVFDINYGLF--SETKAHLLYPNT 752
Cdd:cd00078    5 VRRDRILEDALRQLSKVSsSDLKKVLEVEFVGE-----EGIDAGGVTREFFTLVSKELFNPSYGLFryTPDDSGLLYPNP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  753 HAYAqDVERLRCYEFLGMLIGKCIYEGIQIDAAFASFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKNYDGDVEnDMALN 832
Cdd:cd00078   80 SSFA-DEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDED-DLELT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  833 FTVVHEE-FGVRNVIDLIPNGSNISVTNENRLQYIHLVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVG 911
Cdd:cd00078  158 FTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLIC 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290  912 GDPvPIDIDDLRRHTVYAGGYEPNSPTIVLFWEVLREFEEEDKRSFVKFVTSVARPPILGFKALMPSFCIRVNGEDETRL 991
Cdd:cd00078  238 GSE-DIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSPDDRL 316
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 19114290  992 PTASTCVNLLKLPMYSTKQTLRDKLLTAVRSGVGFG 1027
Cdd:cd00078  317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
695-1026 2.33e-143

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: 431.66  E-value: 2.33e-143
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     695 LLKGPIRITFVDEhgvveEGIDGGGLTKEFLTSICKTVFDINYGLFSETKAH-LLYPNTHAYAQDVERLRCYEFLGMLIG 773
Cdd:smart00119    2 LKKRVLEIEFEGE-----EGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFANEEHLSYFRFIGRVLG 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     774 KCIYEGIQIDAAFASFFVAKWLGHPSYFDDLTSLDPNLYEGLVFLKnYDGDVENDMALNFT-VVHEEFGVRNVIDLIPNG 852
Cdd:smart00119   77 KALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQVKVVELKPGG 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     853 SNISVTNENRLQYIHLVSNYYLNARLSRQCRAFTNGFTQIIDPHWLAMFHESEIQILVGGDPvPIDIDDLRRHTVYAGGY 932
Cdd:smart00119  156 SNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSP-EIDVDDLKSNTEYKGGY 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290     933 EPNSPTIVLFWEVLREFEEEDKRSFVKFVTSVARPPILGFKALMPSFCIRVNGEDETRLPTASTCVNLLKLPMYSTKQTL 1012
Cdd:smart00119  235 SANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEIL 314
                           330
                    ....*....|....
gi 19114290    1013 RDKLLTAVRSGVGF 1026
Cdd:smart00119  315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
726-1029 1.64e-113

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 352.68  E-value: 1.64e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290    726 TSICKTVFDINYGLFSE--TKAHLLYPNTHAYAQ-DVERLRCYEFLGMLIGKCIYEGIQIDAAFASFFVAKWLGHPSYFD 802
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYetEDDRTYWFNPSSSESpDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290    803 DLTSLDPNLYEGLVFLKNYDGDVENDMALNFTVvhEEFGVRNVIDLIPNGSNISVTNENRLQYIHLVSNYYLNARLSRQC 882
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114290    883 RAFTNGFTQIIDPHWLAMFHESEIQILVGGDPVpIDIDDLRRHTVYAGGYEPNSPTIVLFWEVLREFEEEDKRSFVKFVT 962
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPE-IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVT 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114290    963 SVARPPILGFKALmPSFCI-RVNGEDETRLPTASTCVNLLKLPMYSTKQTLRDKLLTAVRSGVGFGFS 1029
Cdd:pfam00632  238 GSSRLPVGGFKSL-PKFTIvRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGLS 304
 
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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