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Conserved domains on  [gi|2462517242|ref|XP_054220888|]
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probable E3 ubiquitin-protein ligase HECTD2 isoform X4 [Homo sapiens]

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 ...
 422-512 1.32e-21

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: 96.09  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517242 422 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 499
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80

                          90
                  ....*....|....*.
gi 2462517242 500 KCDNYSE---FRLVGI 512
Cdd:cd00078    81 SFADEDHlklFRFLGR 96
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 422-512 1.32e-21

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: 96.09  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517242 422 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 499
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80

                          90
                  ....*....|....*.
gi 2462517242 500 KCDNYSE---FRLVGI 512
Cdd:cd00078    81 SFADEDHlklFRFLGR 96
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
359-512 1.35e-19

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 92.52  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517242 359 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 438
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462517242 439 LTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGI 512
Cdd:COG5021   532 IMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGR 610
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 445-512 2.56e-14

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: 73.81  E-value: 2.56e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462517242  445 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWF--SSFKCDN--YSEFRLVGI 512
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPnpRSGFANEehLSYFRFIGR 73
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 422-512 1.32e-21

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: 96.09  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517242 422 LNMKVRRTHLVSDSLDEL-TRKRADLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTY-HKDSHCHWFSSF 499
Cdd:cd00078     1 LKITVRRDRILEDALRQLsKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYtPDDSGLLYPNPS 80

                          90
                  ....*....|....*.
gi 2462517242 500 KCDNYSE---FRLVGI 512
Cdd:cd00078    81 SFADEDHlklFRFLGR 96
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
359-512 1.35e-19

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 92.52  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517242 359 YHTWQNFGNSHRFSFCQYPFVIsvaakKIIIQRDSEQQMINIARQSLVDKVSRRQRPDMNilFLNMKVRRTHLVSDSLDE 438
Cdd:COG5021   459 YRFYFVEHRKKTLTKNDSRLGS-----FISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDP--YLHIKVRRDRVFEDSYRE 531

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462517242 439 LTRKRA-DLKKKLKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDS----HCHWFSSFKCDNYSEFRLVGI 512
Cdd:COG5021   532 IMDESGdDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDlytlPINPLSSINPEHLSYFKFLGR 610
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 445-512 2.56e-14

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: 73.81  E-value: 2.56e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462517242  445 DLKKK-LKVTFVGEAGLDMGGLTKEWFLLLIRQIFHPDYGMFTYHKDSHCHWF--SSFKCDN--YSEFRLVGI 512
Cdd:smart00119   1 DLKKRvLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPnpRSGFANEehLSYFRFIGR 73
 
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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