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Conserved domains on  [gi|1844083981|ref|NP_877497|]
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probable E3 ubiquitin-protein ligase HECTD2 isoform a [Homo sapiens]

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 ...
417-774 1.97e-122

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: 371.13  E-value: 1.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 417 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 494
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 495 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 571
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 572 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 650
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 651 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 727
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083981 728 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 774
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 ...
417-774 1.97e-122

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: 371.13  E-value: 1.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 417 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 494
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 495 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 571
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 572 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 650
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 651 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 727
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083981 728 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 774
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
466-775 2.79e-111

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: 2.79e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 466 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 539
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 540 dqnipvgicnvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRKEYVQL 619
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 620 YTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGF 698
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083981 699 PLDLQKKLLHFTTGSDRVPVGGMADL-NFKISKNE-TSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 775
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGgDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
440-773 4.41e-107

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: 4.41e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  440 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 514
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  515 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 593
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  594 IKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQ 673
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  674 RSTQY-DGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNCLPVAHTCFNQLCL 750
Cdd:smart00119 226 SNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLKL 305
                          330       340
                   ....*....|....*....|...
gi 1844083981  751 PPYKSKKDLKQKLIIGISNSEGF 773
Cdd:smart00119 306 PPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
354-776 8.79e-106

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 344.06  E-value: 8.79e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 354 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 433
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 434 LTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGIL 508
Cdd:COG5021   532 IMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 509 MGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQ 588
Cdd:COG5021   612 IGKAIYDSRILDVQFSKAFYKKLLGKP--------------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVED 676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 589 EEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPD-L 667
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 668 DMHALQRSTQYDGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNCLPV 740
Cdd:COG5021   757 DIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLPS 836
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1844083981 741 AHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 776
Cdd:COG5021   837 AHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
417-774 1.97e-122

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: 371.13  E-value: 1.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 417 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 494
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 495 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLS 571
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 572 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALM 650
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 651 LLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-- 727
Cdd:cd00078   226 LFTPEELELLICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKft 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083981 728 ISKNETSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFG 774
Cdd:cd00078   306 IRRVGSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
466-775 2.79e-111

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: 2.79e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 466 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 539
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 540 dqnipvgicnvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRKEYVQL 619
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKEEYIRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 620 YTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQRSTQYD-GYAKTDLTIKYFWDVVLGF 698
Cdd:pfam00632 145 YVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEF 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083981 699 PLDLQKKLLHFTTGSDRVPVGGMADL-NFKISKNE-TSTNCLPVAHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGL 775
Cdd:pfam00632 225 SPEQRRLFLKFVTGSSRLPVGGFKSLpKFTIVRKGgDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
440-773 4.41e-107

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: 4.41e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  440 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWFS--SFKCDN--YSEFRLVGILMGLAVY 514
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNprSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  515 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 593
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  594 IKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPDLDMHALQ 673
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981  674 RSTQY-DGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK--ISKNETSTNCLPVAHTCFNQLCL 750
Cdd:smart00119 226 SNTEYkGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKftIRKAGSDDERLPTAHTCFNRLKL 305
                          330       340
                   ....*....|....*....|...
gi 1844083981  751 PPYKSKKDLKQKLIIGISNSEGF 773
Cdd:smart00119 306 PPYSSKEILREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
354-776 8.79e-106

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 344.06  E-value: 8.79e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 354 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 433
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 434 LTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGIL 508
Cdd:COG5021   532 IMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 509 MGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicnVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQ 588
Cdd:COG5021   612 IGKAIYDSRILDVQFSKAFYKKLLGKP--------------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVED 676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 589 EEFGIIKSYNLKPGGDKISVTNQNRKEYVQLYTDFLLNKSIYKQFAAFYYGFHSVCASNALMLLRPEEVEILVCGSPD-L 667
Cdd:COG5021   677 DSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdI 756
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083981 668 DMHALQRSTQYDGYAKTDLTIKYFWDVVLGFPLDLQKKLLHFTTGSDRVPVGGMADLNFK-------ISKNETSTNCLPV 740
Cdd:COG5021   757 DIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSdgvrkftIEKGGTDDDRLPS 836
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1844083981 741 AHTCFNQLCLPPYKSKKDLKQKLIIGISNSEGFGLE 776
Cdd:COG5021   837 AHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 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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