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Conserved domains on  [gi|35493952|ref|NP_904324|]
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ubiquitin-protein ligase E3B isoform 1 [Homo sapiens]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 10050984)

HECT-type E3 ubiquitin-protein ligase catalyzes the attachment of ubiquitin chains to target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
682-1066 5.58e-152

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: 455.87  E-value: 5.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  841 TDLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078  152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078  232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35493952 1000 EVSDDqdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFE 1066
Cdd:cd00078  310 GSPDD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
682-1066 5.58e-152

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: 455.87  E-value: 5.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  841 TDLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078  152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078  232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35493952 1000 EVSDDqdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFE 1066
Cdd:cd00078  310 GSPDD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
737-1068 4.59e-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: 352.30  E-value: 4.59e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    737 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfy 813
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    814 SSVDELPSLDSEFYKNLTSIKRYDGDIT-DLGLTLSYDedVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQI 892
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDDeDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    893 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMF 972
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    973 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLR 1052
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILK 288
                          330
                   ....*....|....*.
gi 35493952   1053 EKLRYAISMNTGFELS 1068
Cdd:pfam00632  289 EKLLIAIEEGEGFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
707-1065 3.98e-105

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: 332.28  E-value: 3.98e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     707 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 785
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     786 VYEGIVVDVPFASFFLSQLLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDITDLGLTLSYDED-VMGQLVCHELIP 864
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     865 GGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 944
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     945 GFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcvevsddqdtgdtlgsvlrgfftiRKR 1024
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAG 287
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 35493952    1025 EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGF 1065
Cdd:smart00119  288 SDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
670-1068 1.52e-90

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 309.77  E-value: 1.52e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  670 LVETSSASPHVTHITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNL 749
Cdd:COG5021  504 LKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGL 578
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  750 FKTTSGDER-LYPSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfySSVDELPSLDSEFYK 828
Cdd:COG5021  579 FEYITEDLYtLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYR 653
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  829 NLTSIKRYDGDITDLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIK 908
Cdd:COG5021  654 SLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIP 733
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  909 PEWIRMFSTPELQRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFA 988
Cdd:COG5021  734 PDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFK 811
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  989 YLKPPFSIRcvevsddqdtgdtlgsvlrgFFTIRKR-EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFEL 1067
Cdd:COG5021  812 DLQGSDGVR--------------------KFTIEKGgTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                 .
gi 35493952 1068 S 1068
Cdd:COG5021  872 L 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
682-1066 5.58e-152

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: 455.87  E-value: 5.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  841 TDLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078  152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078  232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35493952 1000 EVSDDqdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFE 1066
Cdd:cd00078  310 GSPDD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
737-1068 4.59e-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: 352.30  E-value: 4.59e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    737 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfy 813
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    814 SSVDELPSLDSEFYKNLTSIKRYDGDIT-DLGLTLSYDedVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQI 892
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDDeDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    893 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMF 972
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952    973 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLR 1052
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILK 288
                          330
                   ....*....|....*.
gi 35493952   1053 EKLRYAISMNTGFELS 1068
Cdd:pfam00632  289 EKLLIAIEEGEGFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
707-1065 3.98e-105

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: 332.28  E-value: 3.98e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     707 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 785
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     786 VYEGIVVDVPFASFFLSQLLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDITDLGLTLSYDED-VMGQLVCHELIP 864
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     865 GGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 944
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952     945 GFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcvevsddqdtgdtlgsvlrgfftiRKR 1024
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAG 287
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 35493952    1025 EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGF 1065
Cdd:smart00119  288 SDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
670-1068 1.52e-90

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 309.77  E-value: 1.52e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  670 LVETSSASPHVTHITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNL 749
Cdd:COG5021  504 LKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGL 578
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  750 FKTTSGDER-LYPSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfySSVDELPSLDSEFYK 828
Cdd:COG5021  579 FEYITEDLYtLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYR 653
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  829 NLTSIKRYDGDITDLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIK 908
Cdd:COG5021  654 SLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIP 733
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  909 PEWIRMFSTPELQRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFA 988
Cdd:COG5021  734 PDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFK 811
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35493952  989 YLKPPFSIRcvevsddqdtgdtlgsvlrgFFTIRKR-EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFEL 1067
Cdd:COG5021  812 DLQGSDGVR--------------------KFTIEKGgTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                 .
gi 35493952 1068 S 1068
Cdd:COG5021  872 L 872
 
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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