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Conserved domains on  [gi|532281240|gb|JAB17578|]
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ubiquitin-protein ligase E3B isoform 1 [Callithrix jacchus]

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 8.55e-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: 455.49  E-value: 8.55e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078    77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  841 ADLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078   152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078   232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532281240 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 8.55e-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: 455.49  E-value: 8.55e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078    77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  841 ADLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078   152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078   232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532281240 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 4.89e-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: 4.89e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   737 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfy 813
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   814 SSVDELPSLDSEFYKNLTSIKRYDGDI-ADLGLTLSYDedVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQI 892
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDdEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   893 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMF 972
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   973 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLR 1052
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILK 288
                          330
                   ....*....|....*.
gi 532281240  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 1.88e-104

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: 330.35  E-value: 1.88e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    707 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 785
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    786 VYEGIVVDVPFASFFLSQLLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDIADLGLTLSYDED-VMGQLVCHELIP 864
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    865 GGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 944
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    945 GFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcvevsddqdtgdtlgsvlrgfftiRKR 1024
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAG 287
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 532281240   1025 EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGF 1065
Cdd:smart00119  288 SDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
670-1068 3.56e-90

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 308.62  E-value: 3.56e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  670 LVETSSASPHVTHITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNL 749
Cdd:COG5021   504 LKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGL 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  750 FKTTSGDER-LYPSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfySSVDELPSLDSEFYK 828
Cdd:COG5021   579 FEYITEDLYtLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYR 653
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  829 NLTSIKRYDGDIADLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIK 908
Cdd:COG5021   654 SLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIP 733
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  909 PEWIRMFSTPELQRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFA 988
Cdd:COG5021   734 PDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFK 811
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  989 YLKPPFSIRcvevsddqdtgdtlgsvlrgFFTIRKR-EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFEL 1067
Cdd:COG5021   812 DLQGSDGVR--------------------KFTIEKGgTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                  .
gi 532281240 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 8.55e-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: 455.49  E-value: 8.55e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  682 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 760
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  761 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 840
Cdd:cd00078    77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  841 ADLGLTLSYDEDV-MGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 919
Cdd:cd00078   152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  920 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 999
Cdd:cd00078   232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532281240 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 4.89e-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: 4.89e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   737 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfy 813
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   814 SSVDELPSLDSEFYKNLTSIKRYDGDI-ADLGLTLSYDedVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQI 892
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDdEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   893 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPDERAMF 972
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240   973 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLR 1052
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILK 288
                          330
                   ....*....|....*.
gi 532281240  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 1.88e-104

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: 330.35  E-value: 1.88e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    707 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 785
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    786 VYEGIVVDVPFASFFLSQLLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDIADLGLTLSYDED-VMGQLVCHELIP 864
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    865 GGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 944
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240    945 GFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcvevsddqdtgdtlgsvlrgfftiRKR 1024
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAG 287
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 532281240   1025 EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGF 1065
Cdd:smart00119  288 SDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
670-1068 3.56e-90

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 308.62  E-value: 3.56e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  670 LVETSSASPHVTHITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNL 749
Cdd:COG5021   504 LKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGL 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  750 FKTTSGDER-LYPSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHhsvfySSVDELPSLDSEFYK 828
Cdd:COG5021   579 FEYITEDLYtLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYR 653
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  829 NLTSIKRYDGDIADLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIK 908
Cdd:COG5021   654 SLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIP 733
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  909 PEWIRMFSTPELQRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPDERAMFLKFVTSCSRPPLLGFA 988
Cdd:COG5021   734 PDLLQIFDESELELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFK 811
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532281240  989 YLKPPFSIRcvevsddqdtgdtlgsvlrgFFTIRKR-EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFEL 1067
Cdd:COG5021   812 DLQGSDGVR--------------------KFTIEKGgTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGL 871

                  .
gi 532281240 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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