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Conserved domains on  [gi|1338847002|ref|XP_023666597|]
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uncharacterized protein LOC111843331 isoform X1 [Paramormyrops kingsleyae]

Protein Classification

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 ...
 611-665 1.40e-04

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: 44.48  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338847002 611 KFVQFWVGWNVLP-----------THLDVEVVESSFPRSSTCFYLLKLPgHYKEYSVFERDLLAAI 665
Cdd:cd00078   281 KFLQFVTGSSRLPvggfadlnpkfTIRRVGSPDDRLPTAHTCFNLLKLP-PYSSKEILREKLLYAI 345
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 611-665 1.40e-04

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: 44.48  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338847002 611 KFVQFWVGWNVLP-----------THLDVEVVESSFPRSSTCFYLLKLPgHYKEYSVFERDLLAAI 665
Cdd:cd00078   281 KFLQFVTGSSRLPvggfadlnpkfTIRRVGSPDDRLPTAHTCFNLLKLP-PYSSKEILREKLLYAI 345
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 632-675 1.68e-04

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 44.14  E-value: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1338847002 632 ESSFPRSSTCFYLLKLPgHYKEYSVFERDLLAAIwSVDTGFGMV 675
Cdd:pfam00632 263 DDRLPTAHTCFNRLKLP-DYSSKEILKEKLLIAI-EEGEGFGLS 304
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 611-665 1.40e-04

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: 44.48  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338847002 611 KFVQFWVGWNVLP-----------THLDVEVVESSFPRSSTCFYLLKLPgHYKEYSVFERDLLAAI 665
Cdd:cd00078   281 KFLQFVTGSSRLPvggfadlnpkfTIRRVGSPDDRLPTAHTCFNLLKLP-PYSSKEILREKLLYAI 345
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 632-675 1.68e-04

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 44.14  E-value: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1338847002 632 ESSFPRSSTCFYLLKLPgHYKEYSVFERDLLAAIwSVDTGFGMV 675
Cdd:pfam00632 263 DDRLPTAHTCFNRLKLP-DYSSKEILKEKLLIAI-EEGEGFGLS 304
 
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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