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Conserved domains on  [gi|13278798|gb|AAH04169|]
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DCN1, defective in cullin neddylation 1, domain containing 5 (S. cerevisiae) [Homo sapiens]

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

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List of domain hits

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 ...
120-230 7.18e-48

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: 397562  Cd Length: 116  Bit Score: 153.49  E-value: 7.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278798   120 KLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTW---PLFSVFYQYLEQSKYRVMNKDQ 196
Cdd:pfam03556   1 KLKAKLPELRKELTDPEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGPGFrwfPLLDLWIEFLEEEKKKSISKDT 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 13278798   197 WYNVLEFSRTVHA--DLSNYDEDGAWPVLLDEFVEW 230
Cdd:pfam03556  81 WNMFLEFARKVDEdeDLSNYDEDGAWPSLIDEFVEW 116
 
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 ...
120-230 7.18e-48

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: 397562  Cd Length: 116  Bit Score: 153.49  E-value: 7.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278798   120 KLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTW---PLFSVFYQYLEQSKYRVMNKDQ 196
Cdd:pfam03556   1 KLKAKLPELRKELTDPEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGPGFrwfPLLDLWIEFLEEEKKKSISKDT 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 13278798   197 WYNVLEFSRTVHA--DLSNYDEDGAWPVLLDEFVEW 230
Cdd:pfam03556  81 WNMFLEFARKVDEdeDLSNYDEDGAWPSLIDEFVEW 116
 
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 ...
120-230 7.18e-48

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: 397562  Cd Length: 116  Bit Score: 153.49  E-value: 7.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278798   120 KLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTW---PLFSVFYQYLEQSKYRVMNKDQ 196
Cdd:pfam03556   1 KLKAKLPELRKELTDPEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGPGFrwfPLLDLWIEFLEEEKKKSISKDT 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 13278798   197 WYNVLEFSRTVHA--DLSNYDEDGAWPVLLDEFVEW 230
Cdd:pfam03556  81 WNMFLEFARKVDEdeDLSNYDEDGAWPSLIDEFVEW 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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