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Conserved domains on  [gi|1907132292|ref|XP_036017458|]
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probable E3 ubiquitin-protein ligase HECTD2 isoform X4 [Mus musculus]

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 ...
154-511 6.02e-128

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: 376.52  E-value: 6.02e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 154 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 231
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 232 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLS 308
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPL--------------SLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 309 YEGNvEEDFYSTFQV-FQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALM 387
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 388 LLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-- 464
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132292 465 ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 511
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
154-511 6.02e-128

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: 376.52  E-value: 6.02e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 154 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 231
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 232 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLS 308
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPL--------------SLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 309 YEGNvEEDFYSTFQV-FQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALM 387
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 388 LLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-- 464
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132292 465 ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 511
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
203-512 1.76e-114

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 340.36  E-value: 1.76e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 203 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvps 276
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 277 dqstpvgicsvTIDDLCQVMPELAHGLKELLSYEGNVEEDFYSTFQVfqEEFGVIKSYNLKPGGDKIPVTNQNRREYVQL 356
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 357 YTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGF 435
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132292 436 PLELQKKLLHFTTGSDRVPVGGMADL-NFKISKNETSTNW-LPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 512
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGGDDDDrLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
177-510 6.75e-113

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: 337.28  E-value: 6.75e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  177 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 251
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  252 NSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKEL-LSYEGNVEEDfySTFQ-VFQEEFG 329
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPV--------------TLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSiVLTSEFG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  330 VIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHAL 409
Cdd:smart00119 145 QVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  410 QRSTQY-DGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNWLPVAHTCFNQLC 486
Cdd:smart00119 225 KSNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLK 304
                          330       340
                   ....*....|....*....|....
gi 1907132292  487 LPPYKSKKDLKQKLIIGISNSEGF 510
Cdd:smart00119 305 LPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
74-513 1.36e-109

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 345.60  E-value: 1.36e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  74 YTDFYNSTLDHIDLMEEYH------------TWQSFGNSHR---FSFCQYPFVISIAAKKiiiqrDSEQQMISIARQSLV 138
Cdd:COG5021   427 DESFYVASNVQQQRASREGpllsgwktrlnnLYRFYFVEHRkktLTKNDSRLGSFISLNK-----LDIRRIKEDKRRKLF 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 139 DKVSRRQRPdmNMLFLNMKVRRTHLVSDSLDELTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMF 217
Cdd:COG5021   502 YSLKQKAKI--FDPYLHIKVRRDRVFEDSYREIMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLF 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 218 TYHKDS----HCHWFSSFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLC 293
Cdd:COG5021   580 EYITEDlytlPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV--------------SLVDLE 645
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 294 QVMPELAHGLKELLSYEGNvEEDFYSTFQVFQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAF 373
Cdd:COG5021   646 SLDPELYRSLVWLLNNDID-ETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAF 724
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 374 YCGFHSVCASNALMLLRPEEVEILVCGSPE-LDMHALQRSTQYDGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDR 452
Cdd:COG5021   725 KSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSR 804
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132292 453 VPVGGMADLNFK-------ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 513
Cdd:COG5021   805 IPINGFKDLQGSdgvrkftIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
154-511 6.02e-128

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: 376.52  E-value: 6.02e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 154 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 231
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 232 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLS 308
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPL--------------SLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 309 YEGNvEEDFYSTFQV-FQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALM 387
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 388 LLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-- 464
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132292 465 ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 511
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
203-512 1.76e-114

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 340.36  E-value: 1.76e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 203 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvps 276
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 277 dqstpvgicsvTIDDLCQVMPELAHGLKELLSYEGNVEEDFYSTFQVfqEEFGVIKSYNLKPGGDKIPVTNQNRREYVQL 356
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 357 YTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGF 435
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132292 436 PLELQKKLLHFTTGSDRVPVGGMADL-NFKISKNETSTNW-LPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 512
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGGDDDDrLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
177-510 6.75e-113

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: 337.28  E-value: 6.75e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  177 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 251
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  252 NSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKEL-LSYEGNVEEDfySTFQ-VFQEEFG 329
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPV--------------TLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSiVLTSEFG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  330 VIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHAL 409
Cdd:smart00119 145 QVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  410 QRSTQY-DGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNWLPVAHTCFNQLC 486
Cdd:smart00119 225 KSNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLK 304
                          330       340
                   ....*....|....*....|....
gi 1907132292  487 LPPYKSKKDLKQKLIIGISNSEGF 510
Cdd:smart00119 305 LPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
74-513 1.36e-109

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 345.60  E-value: 1.36e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292  74 YTDFYNSTLDHIDLMEEYH------------TWQSFGNSHR---FSFCQYPFVISIAAKKiiiqrDSEQQMISIARQSLV 138
Cdd:COG5021   427 DESFYVASNVQQQRASREGpllsgwktrlnnLYRFYFVEHRkktLTKNDSRLGSFISLNK-----LDIRRIKEDKRRKLF 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 139 DKVSRRQRPdmNMLFLNMKVRRTHLVSDSLDELTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMF 217
Cdd:COG5021   502 YSLKQKAKI--FDPYLHIKVRRDRVFEDSYREIMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLF 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 218 TYHKDS----HCHWFSSFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLC 293
Cdd:COG5021   580 EYITEDlytlPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPV--------------SLVDLE 645
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 294 QVMPELAHGLKELLSYEGNvEEDFYSTFQVFQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAF 373
Cdd:COG5021   646 SLDPELYRSLVWLLNNDID-ETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAF 724
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132292 374 YCGFHSVCASNALMLLRPEEVEILVCGSPE-LDMHALQRSTQYDGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDR 452
Cdd:COG5021   725 KSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSR 804
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132292 453 VPVGGMADLNFK-------ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 513
Cdd:COG5021   805 IPINGFKDLQGSdgvrkftIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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