NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1271360255|ref|NP_001344412|]
View 

DCN1-like protein 5 isoform 1 [Mus musculus]

Protein Classification

DCN1-like protein( domain architecture ID 10507856)

defective in cullin neddylation 1 (DCN1)-like protein binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Cullin_binding super family cl04154
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ...
120-185 9.67e-18

Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices.


The actual alignment was detected with superfamily member pfam03556:

Pssm-ID: 460971  Cd Length: 117  Bit Score: 76.47  E-value: 9.67e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271360255 120 KLQSRFDFLRSQLND-ISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTW---PLFSVFYQYLE 185
Cdd:pfam03556   1 KLKAKLPELRKELTDpSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRFrifPLLDLWIEFLE 70
 
Name Accession Description Interval E-value
Cullin_binding pfam03556
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ...
120-185 9.67e-18

Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices.


Pssm-ID: 460971  Cd Length: 117  Bit Score: 76.47  E-value: 9.67e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271360255 120 KLQSRFDFLRSQLND-ISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTW---PLFSVFYQYLE 185
Cdd:pfam03556   1 KLKAKLPELRKELTDpSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRFrifPLLDLWIEFLE 70
 
Name Accession Description Interval E-value
Cullin_binding pfam03556
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ...
120-185 9.67e-18

Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices.


Pssm-ID: 460971  Cd Length: 117  Bit Score: 76.47  E-value: 9.67e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271360255 120 KLQSRFDFLRSQLND-ISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTW---PLFSVFYQYLE 185
Cdd:pfam03556   1 KLKAKLPELRKELTDpSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRFrifPLLDLWIEFLE 70
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH