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Conserved domains on  [gi|386771532|ref|NP_001246859|]
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uncharacterized protein Dmel_CG10508, isoform K [Drosophila melanogaster]

Protein Classification

CUE domain-containing protein( domain architecture ID 10198281)

CUE domain-containing protein binds ubiquitin and may promote monoubiquitination

CATH:  1.10.8.10
Gene Ontology:  GO:0043130
PubMed:  12628920|12787494
SCOP:  4003786

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
291-327 4.11e-05

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


:

Pssm-ID: 270465  Cd Length: 38  Bit Score: 40.91  E-value: 4.11e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 386771532 291 KMKLRYMKNIFPKADEELLLDILANADNNVQFASEKL 327
Cdd:cd14279    1 DEKLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
 
Name Accession Description Interval E-value
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
291-327 4.11e-05

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 40.91  E-value: 4.11e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 386771532 291 KMKLRYMKNIFPKADEELLLDILANADNNVQFASEKL 327
Cdd:cd14279    1 DEKLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
 
Name Accession Description Interval E-value
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
291-327 4.11e-05

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 40.91  E-value: 4.11e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 386771532 291 KMKLRYMKNIFPKADEELLLDILANADNNVQFASEKL 327
Cdd:cd14279    1 DEKLEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
 
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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