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Conserved domains on  [gi|1907132296|ref|XP_036017460|]
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probable E3 ubiquitin-protein ligase HECTD2 isoform X6 [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 ...
67-424 1.16e-129

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: 377.68  E-value: 1.16e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  67 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 144
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 145 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLS 221
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPL--------------SLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 222 YEGNvEEDFYSTFQV-FQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALM 300
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 301 LLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-- 377
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132296 378 ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 424
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 ...
67-424 1.16e-129

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: 377.68  E-value: 1.16e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  67 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 144
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 145 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLS 221
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPL--------------SLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 222 YEGNvEEDFYSTFQV-FQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALM 300
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 301 LLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-- 377
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132296 378 ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 424
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
116-425 2.08e-116

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 342.28  E-value: 2.08e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 116 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvps 189
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 190 dqstpvgicsvTIDDLCQVMPELAHGLKELLSYEGNVEEDFYSTFQVfqEEFGVIKSYNLKPGGDKIPVTNQNRREYVQL 269
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 270 YTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGF 348
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132296 349 PLELQKKLLHFTTGSDRVPVGGMADL-NFKISKNETSTNW-LPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 425
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGGDDDDrLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
90-423 1.45e-114

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: 338.44  E-value: 1.45e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296   90 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 164
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  165 NSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKEL-LSYEGNVEEDfySTFQ-VFQEEFG 242
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPV--------------TLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSiVLTSEFG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  243 VIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHAL 322
Cdd:smart00119 145 QVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  323 QRSTQY-DGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNWLPVAHTCFNQLC 399
Cdd:smart00119 225 KSNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLK 304
                          330       340
                   ....*....|....*....|....
gi 1907132296  400 LPPYKSKKDLKQKLIIGISNSEGF 423
Cdd:smart00119 305 LPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
6-426 1.31e-110

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 345.21  E-value: 1.31e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296   6 TWQSFGNSHR---FSFCQYPFVISIAAKKiiiqrDSEQQMISIARQSLVDKVSRRQRPdmNMLFLNMKVRRTHLVSDSLD 82
Cdd:COG5021   458 LYRFYFVEHRkktLTKNDSRLGSFISLNK-----LDIRRIKEDKRRKLFYSLKQKAKI--FDPYLHIKVRRDRVFEDSYR 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  83 ELTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGI 157
Cdd:COG5021   531 EIMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGR 610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 158 LMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLSYEGNvEEDFYSTFQVF 237
Cdd:COG5021   611 VIGKAIYDSRILDVQFSKAFYKKLLGKPV--------------SLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVE 675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 238 QEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPE- 316
Cdd:COG5021   676 DDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEd 755
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 317 LDMHALQRSTQYDGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNWLP 389
Cdd:COG5021   756 IDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLP 835
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1907132296 390 VAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 426
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
67-424 1.16e-129

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: 377.68  E-value: 1.16e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  67 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 144
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 145 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLS 221
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPL--------------SLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 222 YEGNvEEDFYSTFQV-FQEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALM 300
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 301 LLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-- 377
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132296 378 ISKNETSTNWLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 424
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
116-425 2.08e-116

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 342.28  E-value: 2.08e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 116 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPVvps 189
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 190 dqstpvgicsvTIDDLCQVMPELAHGLKELLSYEGNVEEDFYSTFQVfqEEFGVIKSYNLKPGGDKIPVTNQNRREYVQL 269
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 270 YTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHALQRSTQYD-GYAKTDLTIRYFWDVVLGF 348
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132296 349 PLELQKKLLHFTTGSDRVPVGGMADL-NFKISKNETSTNW-LPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 425
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGGDDDDrLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
90-423 1.45e-114

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: 338.44  E-value: 1.45e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296   90 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 164
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  165 NSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKEL-LSYEGNVEEDfySTFQ-VFQEEFG 242
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKPV--------------TLHDLESLDPELYKSLKWLlLNNDTSEELD--LTFSiVLTSEFG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  243 VIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPELDMHAL 322
Cdd:smart00119 145 QVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  323 QRSTQY-DGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNWLPVAHTCFNQLC 399
Cdd:smart00119 225 KSNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLK 304
                          330       340
                   ....*....|....*....|....
gi 1907132296  400 LPPYKSKKDLKQKLIIGISNSEGF 423
Cdd:smart00119 305 LPPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
6-426 1.31e-110

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 345.21  E-value: 1.31e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296   6 TWQSFGNSHR---FSFCQYPFVISIAAKKiiiqrDSEQQMISIARQSLVDKVSRRQRPdmNMLFLNMKVRRTHLVSDSLD 82
Cdd:COG5021   458 LYRFYFVEHRkktLTKNDSRLGSFISLNK-----LDIRRIKEDKRRKLFYSLKQKAKI--FDPYLHIKVRRDRVFEDSYR 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296  83 ELTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGI 157
Cdd:COG5021   531 EIMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGR 610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 158 LMGLAVYNSITLDIRFPPCCYKKLLSPPVvpsdqstpvgicsvTIDDLCQVMPELAHGLKELLSYEGNvEEDFYSTFQVF 237
Cdd:COG5021   611 VIGKAIYDSRILDVQFSKAFYKKLLGKPV--------------SLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVE 675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 238 QEEFGVIKSYNLKPGGDKIPVTNQNRREYVQLYTDFLLNKSIYKQFAAFYCGFHSVCASNALMLLRPEEVEILVCGSPE- 316
Cdd:COG5021   676 DDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEd 755
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132296 317 LDMHALQRSTQYDGYAKTDLTIRYFWDVVLGFPLELQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNWLP 389
Cdd:COG5021   756 IDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLP 835
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1907132296 390 VAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 426
Cdd:COG5021   836 SAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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