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Conserved domains on  [gi|68533242|ref|NP_473434|]
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ubiquitin-protein ligase E3B isoform 1 [Mus musculus]

Protein Classification

HECT domain-containing protein( domain architecture ID 10050984)

HECT domain-containing protein may function as an E3 ubiquitin-protein ligase that catalyzes the attachment of ubiquitin chains to target proteins

CATH:  3.30.2410.10
EC:  2.3.2.26
Gene Ontology:  GO:0004842
PubMed:  22389392|29016349
SCOP:  4002196

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 ...
684-1068 1.60e-151

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: 454.72  E-value: 1.60e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  684 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 762
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  763 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 842
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  843 ADLGLTLSYDEDV-MGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 921
Cdd:cd00078  152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  922 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 1001
Cdd:cd00078  232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68533242 1002 EVSDDqdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFE 1068
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 ...
684-1068 1.60e-151

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: 454.72  E-value: 1.60e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  684 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 762
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  763 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 842
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  843 ADLGLTLSYDEDV-MGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 921
Cdd:cd00078  152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  922 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 1001
Cdd:cd00078  232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68533242 1002 EVSDDqdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFE 1068
Cdd:cd00078  310 GSPDD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
739-1070 2.38e-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: 353.07  E-value: 2.38e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    739 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGHHhsvfy 815
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    816 SSVDELPSLDSEFYKNLTSIKRYDGDI-ADLGLTLSYDedVMGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQI 894
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDdEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    895 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPEERAMF 974
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    975 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLR 1054
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILK 288
                          330
                   ....*....|....*.
gi 68533242   1055 EKLRYAISMNTGFELS 1070
Cdd:pfam00632  289 EKLLIAIEEGEGFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
709-1067 1.31e-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: 330.74  E-value: 1.31e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     709 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 787
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     788 VYEGIVVDVPFASFFLSQMLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDIADLGLTLSYDED-VMGQLVCHELVP 866
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     867 GGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 946
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     947 GFHGSHRVIIWLWDILASdFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcvevsddqdtgdtlgsvlrgfftiRKR 1026
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAG 287
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 68533242    1027 EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGF 1067
Cdd:smart00119  288 SDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
684-1070 1.70e-91

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 312.47  E-value: 1.70e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  684 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 762
Cdd:COG5021  516 HIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLP 590
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  763 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGHHhsvfySSVDELPSLDSEFYKNLTSIKRYDGDI 842
Cdd:COG5021  591 INPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYRSLVWLLNNDIDE 665
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  843 ADLGLTLSYDEDVMGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPEL 922
Cdd:COG5021  666 TILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESEL 745
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  923 QRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcve 1002
Cdd:COG5021  746 ELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVR--- 820
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68533242 1003 vsddqdtgdtlgsvlrgFFTIRKR-EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFELS 1070
Cdd:COG5021  821 -----------------KFTIEKGgTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
684-1068 1.60e-151

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: 454.72  E-value: 1.60e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  684 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 762
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVG-----EEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGlLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  763 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGhhhsvFYSSVDELPSLDSEFYKNLTSIKRYDGDI 842
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG-----KPLSLEDLEELDPELYKSLKELLDNDGDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  843 ADLGLTLSYDEDV-MGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPE 921
Cdd:cd00078  152 DDLELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  922 LQRLISGdNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCV 1001
Cdd:cd00078  232 LELLICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVL-ESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68533242 1002 EVSDDqdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFE 1068
Cdd:cd00078  310 GSPDD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
739-1070 2.38e-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: 353.07  E-value: 2.38e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    739 EIIKRVFDPALNLFKTTSGDERLY-PSPTSYI--HENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGHHhsvfy 815
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYwFNPSSSEspDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEP----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    816 SSVDELPSLDSEFYKNLTSIKRYDGDI-ADLGLTLSYDedVMGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQI 894
Cdd:pfam00632   77 LTLEDLESIDPELYKSLKSLLNMDNDDdEDLGLTFTIP--VFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    895 KNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNaEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILaSDFTPEERAMF 974
Cdd:pfam00632  155 EPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP-EIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242    975 LKFVTSCSRPPLLGFAYLkPPFSIRCVEVSDDQdtgdtlgsvlrgfftirkrepggRLPTSSTCFNLLKLPNYSKKSVLR 1054
Cdd:pfam00632  233 LKFVTGSSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILK 288
                          330
                   ....*....|....*.
gi 68533242   1055 EKLRYAISMNTGFELS 1070
Cdd:pfam00632  289 EKLLIAIEEGEGFGLS 304
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
709-1067 1.31e-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: 330.74  E-value: 1.31e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     709 KGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYI-HENYLQLFEFVGKMLGKA 787
Cdd:smart00119    4 KRVLEIEFEG-----EEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     788 VYEGIVVDVPFASFFLSQMLGHhhSVfysSVDELPSLDSEFYKNLTSIKRYDGDIADLGLTLSYDED-VMGQLVCHELVP 866
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLGK--PV---TLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTsEFGQVKVVELKP 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     867 GGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDnAEIDLEDLKKHTVYYG 946
Cdd:smart00119  154 GGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGS-PEIDVDDLKSNTEYKG 232
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242     947 GFHGSHRVIIWLWDILASdFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcvevsddqdtgdtlgsvlrgfftiRKR 1026
Cdd:smart00119  233 GYSANSQTIKWFWEVVES-FTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAG 287
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|.
gi 68533242    1027 EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGF 1067
Cdd:smart00119  288 SDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
684-1070 1.70e-91

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 312.47  E-value: 1.70e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  684 HITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNdlgvdEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDER-LY 762
Cdd:COG5021  516 HIKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVG-----EEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYtLP 590
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  763 PSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQMLGHHhsvfySSVDELPSLDSEFYKNLTSIKRYDGDI 842
Cdd:COG5021  591 INPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP-----VSLVDLESLDPELYRSLVWLLNNDIDE 665
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  843 ADLGLTLSYDEDVMGQLVCHELVPGGKTIPVTDENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPEL 922
Cdd:COG5021  666 TILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESEL 745
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68533242  923 QRLISGDNAEIDLEDLKKHTVYYgGFHGSHRVIIWLWDILASdFTPEERAMFLKFVTSCSRPPLLGFAYLKPPFSIRcve 1002
Cdd:COG5021  746 ELLIGGIPEDIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISE-FDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVR--- 820
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68533242 1003 vsddqdtgdtlgsvlrgFFTIRKR-EPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFELS 1070
Cdd:COG5021  821 -----------------KFTIEKGgTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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