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Conserved domains on  [gi|17554364|ref|NP_499392|]
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HECT domain-containing protein [Caenorhabditis elegans]

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 ...
684-1064 2.58e-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: 453.95  E-value: 2.58e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  684 WITVQRNRIIEDGFNHLSKLTIPALKSTIRVKFVNEQGldeagIDQDGVFKEFLELTLKKVFDPQLNLFSTT--STGVLY 761
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEG-----IDAGGVTREFFTLVSKELFNPSYGLFRYTpdDSGLLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  762 PSPTSSLHDDHLALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshRLCAFDELSQLDPELYRSLTFVKRYEGEMADL 841
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG--KPLSLEDLEELDPELYKSLKELLDNDGDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  842 SLTFSVDEDF-MGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRTQEQCKAFVTGMQSILQPTWLSLFAPNDLQC 920
Cdd:cd00078  155 ELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  921 LISGvNSDIDLADLKRNVQYFGGFHGNHRLIKWLWDILEnKFTSEERKLFLKFVTSCSRPPVLGFSYLEPPFSIRCVEVS 1000
Cdd:cd00078  235 LICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE-SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17554364 1001 DDqdqgdtlgsvvrgflalrkgtaatRLPTASTCFNLLKLPNYNKKSLLLEKLRYAIHAGTGFE 1064
Cdd:cd00078  313 DD------------------------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 ...
684-1064 2.58e-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: 453.95  E-value: 2.58e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  684 WITVQRNRIIEDGFNHLSKLTIPALKSTIRVKFVNEQGldeagIDQDGVFKEFLELTLKKVFDPQLNLFSTT--STGVLY 761
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEG-----IDAGGVTREFFTLVSKELFNPSYGLFRYTpdDSGLLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  762 PSPTSSLHDDHLALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshRLCAFDELSQLDPELYRSLTFVKRYEGEMADL 841
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG--KPLSLEDLEELDPELYKSLKELLDNDGDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  842 SLTFSVDEDF-MGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRTQEQCKAFVTGMQSILQPTWLSLFAPNDLQC 920
Cdd:cd00078  155 ELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  921 LISGvNSDIDLADLKRNVQYFGGFHGNHRLIKWLWDILEnKFTSEERKLFLKFVTSCSRPPVLGFSYLEPPFSIRCVEVS 1000
Cdd:cd00078  235 LICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE-SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17554364 1001 DDqdqgdtlgsvvrgflalrkgtaatRLPTASTCFNLLKLPNYNKKSLLLEKLRYAIHAGTGFE 1064
Cdd:cd00078  313 DD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
709-1063 1.02e-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: 333.82  E-value: 1.02e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     709 KSTIRVKFVNEQGLDEAGidqdgVFKEFLELTLKKVFDPQLNLFSTTSTG-VLYPSPTSSL-HDDHLALFTFVGRMLGKA 786
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGG-----VTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     787 VYEGIVVDVQLAPVLLAAVLGshRLCAFDELSQLDPELYRSLTFVKRYEGEMADLSLTFSVDEDF-MGKISTVDLVPSGR 865
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTSeFGQVKVVELKPGGS 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     866 TISVTNENKIDYVHRMAHHRVFRRTQEQCKAFVTGMQSILQPTWLSLFAPNDLQCLISGvNSDIDLADLKRNVQYFGGFH 945
Cdd:smart00119  157 NIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG-SPEIDVDDLKSNTEYKGGYS 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     946 GNHRLIKWLWDILEnKFTSEERKLFLKFVTSCSRPPVLGFSYLEPPFSIRcvevsddqdqgdtlgsvvrgflalRKGTAA 1025
Cdd:smart00119  236 ANSQTIKWFWEVVE-SFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAGSDD 290
                           330       340       350
                    ....*....|....*....|....*....|....*...
gi 17554364    1026 TRLPTASTCFNLLKLPNYNKKSLLLEKLRYAIHAGTGF 1063
Cdd:smart00119  291 ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
742-1066 1.48e-100

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 319.17  E-value: 1.48e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    742 KKVFDPQLNLFSTTST--GVLYPSPTSSLHDDH--LALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshRLCAFDEL 817
Cdd:pfam00632    5 KELFDPNYGLFEYETEddRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLG--EPLTLEDL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    818 SQLDPELYRSLTFVKRYEGEM-ADLSLTFSVDEdfMGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRTQEQCKA 896
Cdd:pfam00632   83 ESIDPELYKSLKSLLNMDNDDdEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    897 FVTGMQSILQPTWLSLFAPNDLQCLISGvNSDIDLADLKRNVQYFGGFHGNHRLIKWLWDILeNKFTSEERKLFLKFVTS 976
Cdd:pfam00632  161 FRKGFYSVIPKEALSLFTPEELELLICG-SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    977 CSRPPVLGFSYLePPFSIRCVEVSDDQdqgdtlgsvvrgflalrkgtaatRLPTASTCFNLLKLPNYNKKSLLLEKLRYA 1056
Cdd:pfam00632  239 SSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
                          330
                   ....*....|
gi 17554364   1057 IHAGTGFELS 1066
Cdd:pfam00632  295 IEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
653-1066 2.78e-92

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 314.40  E-value: 2.78e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  653 PIKDRMLLFRRQVQDdKNRVATSLNDPQMQtwITVQRNRIIEDGFNHLSKLTIPALKSTIRVKFVNEQGLDEAGIDqdgv 732
Cdd:COG5021  488 DIRRIKEDKRRKLFY-SLKQKAKIFDPYLH--IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLT---- 560
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  733 fKEFLELTLKKVFDPQLNLF--STTSTGVLYPSPTSSLHDDHLALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshR 810
Cdd:COG5021  561 -REWLFLLSKEMFNPDYGLFeyITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--K 637
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  811 LCAFDELSQLDPELYRSLTFVKRYEGEMADLSLTFSVDEDFMGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRT 890
Cdd:COG5021  638 PVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRV 717
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  891 QEQCKAFVTGMQSILQPTWLSLFAPNDLQCLISGVNSDIDLADLKRNVQYfGGFHGNHRLIKWLWDILEnKFTSEERKLF 970
Cdd:COG5021  718 EKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIIS-EFDFEERAKL 795
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  971 LKFVTSCSRPPVLGFSYLEPPFSircvevsddqdqgdtlgsvVRGFLALRKGTAATRLPTASTCFNLLKLPNYNKKSLLL 1050
Cdd:COG5021  796 LQFVTGTSRIPINGFKDLQGSDG-------------------VRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLR 856
                        410
                 ....*....|....*.
gi 17554364 1051 EKLRYAIHAGTGFELS 1066
Cdd:COG5021  857 SKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
684-1064 2.58e-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: 453.95  E-value: 2.58e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  684 WITVQRNRIIEDGFNHLSKLTIPALKSTIRVKFVNEQGldeagIDQDGVFKEFLELTLKKVFDPQLNLFSTT--STGVLY 761
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEG-----IDAGGVTREFFTLVSKELFNPSYGLFRYTpdDSGLLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  762 PSPTSSLHDDHLALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshRLCAFDELSQLDPELYRSLTFVKRYEGEMADL 841
Cdd:cd00078   77 PNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLG--KPLSLEDLEELDPELYKSLKELLDNDGDEDDL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  842 SLTFSVDEDF-MGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRTQEQCKAFVTGMQSILQPTWLSLFAPNDLQC 920
Cdd:cd00078  155 ELTFTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  921 LISGvNSDIDLADLKRNVQYFGGFHGNHRLIKWLWDILEnKFTSEERKLFLKFVTSCSRPPVLGFSYLEPPFSIRCVEVS 1000
Cdd:cd00078  235 LICG-SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLE-SFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGSP 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17554364 1001 DDqdqgdtlgsvvrgflalrkgtaatRLPTASTCFNLLKLPNYNKKSLLLEKLRYAIHAGTGFE 1064
Cdd:cd00078  313 DD------------------------RLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
709-1063 1.02e-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: 333.82  E-value: 1.02e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     709 KSTIRVKFVNEQGLDEAGidqdgVFKEFLELTLKKVFDPQLNLFSTTSTG-VLYPSPTSSL-HDDHLALFTFVGRMLGKA 786
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGG-----VTREFFFLLSKELFNPDYGLFRYSPNDyLLYPNPRSGFaNEEHLSYFRFIGRVLGKA 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     787 VYEGIVVDVQLAPVLLAAVLGshRLCAFDELSQLDPELYRSLTFVKRYEGEMADLSLTFSVDEDF-MGKISTVDLVPSGR 865
Cdd:smart00119   79 LYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLTSeFGQVKVVELKPGGS 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     866 TISVTNENKIDYVHRMAHHRVFRRTQEQCKAFVTGMQSILQPTWLSLFAPNDLQCLISGvNSDIDLADLKRNVQYFGGFH 945
Cdd:smart00119  157 NIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICG-SPEIDVDDLKSNTEYKGGYS 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364     946 GNHRLIKWLWDILEnKFTSEERKLFLKFVTSCSRPPVLGFSYLEPPFSIRcvevsddqdqgdtlgsvvrgflalRKGTAA 1025
Cdd:smart00119  236 ANSQTIKWFWEVVE-SFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIR------------------------KAGSDD 290
                           330       340       350
                    ....*....|....*....|....*....|....*...
gi 17554364    1026 TRLPTASTCFNLLKLPNYNKKSLLLEKLRYAIHAGTGF 1063
Cdd:smart00119  291 ERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
742-1066 1.48e-100

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 319.17  E-value: 1.48e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    742 KKVFDPQLNLFSTTST--GVLYPSPTSSLHDDH--LALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshRLCAFDEL 817
Cdd:pfam00632    5 KELFDPNYGLFEYETEddRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLG--EPLTLEDL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    818 SQLDPELYRSLTFVKRYEGEM-ADLSLTFSVDEdfMGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRTQEQCKA 896
Cdd:pfam00632   83 ESIDPELYKSLKSLLNMDNDDdEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    897 FVTGMQSILQPTWLSLFAPNDLQCLISGvNSDIDLADLKRNVQYFGGFHGNHRLIKWLWDILeNKFTSEERKLFLKFVTS 976
Cdd:pfam00632  161 FRKGFYSVIPKEALSLFTPEELELLICG-SPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEIL-EEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364    977 CSRPPVLGFSYLePPFSIRCVEVSDDQdqgdtlgsvvrgflalrkgtaatRLPTASTCFNLLKLPNYNKKSLLLEKLRYA 1056
Cdd:pfam00632  239 SSRLPVGGFKSL-PKFTIVRKGGDDDD-----------------------RLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
                          330
                   ....*....|
gi 17554364   1057 IHAGTGFELS 1066
Cdd:pfam00632  295 IEEGEGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
653-1066 2.78e-92

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 314.40  E-value: 2.78e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  653 PIKDRMLLFRRQVQDdKNRVATSLNDPQMQtwITVQRNRIIEDGFNHLSKLTIPALKSTIRVKFVNEQGLDEAGIDqdgv 732
Cdd:COG5021  488 DIRRIKEDKRRKLFY-SLKQKAKIFDPYLH--IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLT---- 560
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  733 fKEFLELTLKKVFDPQLNLF--STTSTGVLYPSPTSSLHDDHLALFTFVGRMLGKAVYEGIVVDVQLAPVLLAAVLGshR 810
Cdd:COG5021  561 -REWLFLLSKEMFNPDYGLFeyITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG--K 637
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  811 LCAFDELSQLDPELYRSLTFVKRYEGEMADLSLTFSVDEDFMGKISTVDLVPSGRTISVTNENKIDYVHRMAHHRVFRRT 890
Cdd:COG5021  638 PVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRV 717
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  891 QEQCKAFVTGMQSILQPTWLSLFAPNDLQCLISGVNSDIDLADLKRNVQYfGGFHGNHRLIKWLWDILEnKFTSEERKLF 970
Cdd:COG5021  718 EKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEDIDIDDWKSNTAY-HGYTEDSPIIVWFWEIIS-EFDFEERAKL 795
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554364  971 LKFVTSCSRPPVLGFSYLEPPFSircvevsddqdqgdtlgsvVRGFLALRKGTAATRLPTASTCFNLLKLPNYNKKSLLL 1050
Cdd:COG5021  796 LQFVTGTSRIPINGFKDLQGSDG-------------------VRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLR 856
                        410
                 ....*....|....*.
gi 17554364 1051 EKLRYAIHAGTGFELS 1066
Cdd:COG5021  857 SKLLTAINEGAGFGLL 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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