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Conserved domains on  [gi|1622966480|ref|XP_028682483|]
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probable E3 ubiquitin-protein ligase HECTD2 isoform X9 [Macaca mulatta]

Protein Classification

HECT domain-containing protein( domain architecture ID 706099)

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:  29016349|22389392
SCOP:  4002196

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc super family cl27008
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
439-636 1.72e-47

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.


The actual alignment was detected with superfamily member cd00078:

Pssm-ID: 474882 [Multi-domain]  Cd Length: 352  Bit Score: 170.44  E-value: 1.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 439 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 516
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 517 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicsVTVDDLCQIMPELAHGLSELLS 593
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622966480 594 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKE 189
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
439-636 1.72e-47

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: 170.44  E-value: 1.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 439 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 516
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 517 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicsVTVDDLCQIMPELAHGLSELLS 593
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622966480 594 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKE 189
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
344-636 2.04e-41

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 161.47  E-value: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 344 FSDTANNLVHLPLIP--YTDFYNSTLDHIDLMEE---------------YHTWQNFGNSHRFSFCQYPFVISIAAKKIII 406
Cdd:COG5021   410 SSSTYEDLRREQLGResDESFYVASNVQQQRASRegpllsgwktrlnnlYRFYFVEHRKKTLTKNDSRLGSFISLNKLDI 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 407 QRDSEqqminIARQSLVDKVSRRQRPdmNMLFLNMKVRRTHLVSDSLDELTRKRA-DLKKKLKVTFVGEAGLDMGGLTKE 485
Cdd:COG5021   490 RRIKE-----DKRRKLFYSLKQKAKI--FDPYLHIKVRRDRVFEDSYREIMDESGdDLKKTLEIEFVGEEGIDAGGLTRE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 486 WFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiips 561
Cdd:COG5021   563 WLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP---- 638
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966480 562 dqnipvgicsVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:COG5021   639 ----------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKK 702
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
462-636 4.14e-37

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: 141.22  E-value: 4.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480  462 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWF--SSFKCDN--YSEFRLVGILMGLAVY 536
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPnpRSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480  537 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicsVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 615
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180
                   ....*....|....*....|.
gi 1622966480  616 IKSYNLKPGGDKISVTNQNRK 636
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKK 166
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
488-636 4.34e-33

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 129.27  E-value: 4.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 488 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 561
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966480 562 dqnipvgicsvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKE 139
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
439-636 1.72e-47

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: 170.44  E-value: 1.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 439 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 516
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 517 KCDNYSE---FRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiipsdqnipvgicsVTVDDLCQIMPELAHGLSELLS 593
Cdd:cd00078    81 SFADEDHlklFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP--------------LSLEDLEELDPELYKSLKELLD 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622966480 594 HEGNvEEDFYSTFQV-FQEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:cd00078   147 NDGD-EDDLELTFTIeLDSSFGGAVTVELKPGGRDIPVTNENKE 189
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
344-636 2.04e-41

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 161.47  E-value: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 344 FSDTANNLVHLPLIP--YTDFYNSTLDHIDLMEE---------------YHTWQNFGNSHRFSFCQYPFVISIAAKKIII 406
Cdd:COG5021   410 SSSTYEDLRREQLGResDESFYVASNVQQQRASRegpllsgwktrlnnlYRFYFVEHRKKTLTKNDSRLGSFISLNKLDI 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 407 QRDSEqqminIARQSLVDKVSRRQRPdmNMLFLNMKVRRTHLVSDSLDELTRKRA-DLKKKLKVTFVGEAGLDMGGLTKE 485
Cdd:COG5021   490 RRIKE-----DKRRKLFYSLKQKAKI--FDPYLHIKVRRDRVFEDSYREIMDESGdDLKKTLEIEFVGEEGIDAGGLTRE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 486 WFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPiips 561
Cdd:COG5021   563 WLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKP---- 638
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966480 562 dqnipvgicsVTVDDLCQIMPELAHGLSELLSHEGNvEEDFYSTFQVFQEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:COG5021   639 ----------VSLVDLESLDPELYRSLVWLLNNDID-ETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKK 702
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
462-636 4.14e-37

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: 141.22  E-value: 4.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480  462 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWF--SSFKCDN--YSEFRLVGILMGLAVY 536
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPnpRSGFANEehLSYFRFIGRVLGKALY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480  537 NSITLDIRFPPCCYKKLLSPPiipsdqnipvgicsVTVDDLCQIMPELAHGLSELLsHEGNVEEDFYSTFQ-VFQEEFGI 615
Cdd:smart00119  81 DNRLLDLFFARPFYKKLLGKP--------------VTLHDLESLDPELYKSLKWLL-LNNDTSEELDLTFSiVLTSEFGQ 145
                          170       180
                   ....*....|....*....|.
gi 1622966480  616 IKSYNLKPGGDKISVTNQNRK 636
Cdd:smart00119 146 VKVVELKPGGSNIPVTEENKK 166
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
488-636 4.34e-33

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 129.27  E-value: 4.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966480 488 LLLIRQIFHPDYGMFTYHK-DSHCHWFS-----SFKCDNYSEFRLVGILMGLAVYNSITLDIRFPPCCYKKLLSPPIips 561
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETeDDRTYWFNpssseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPL--- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966480 562 dqnipvgicsvTVDDLCQIMPELAHGLSELLSHEGNVEEDFYSTFQVfqEEFGIIKSYNLKPGGDKISVTNQNRK 636
Cdd:pfam00632  78 -----------TLEDLESIDPELYKSLKSLLNMDNDDDEDLGLTFTI--PVFGESKTIELIPNGRNIPVTNENKE 139
 
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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