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Conserved domains on  [gi|146099852|ref|XP_001468767|]
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conserved hypothetical protein [Leishmania infantum JPCM5]

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

CATH:  1.10.238.10
Gene Ontology:  GO:0031624|GO:0097602|GO:0000151|GO:0032182|GO:0045116

Graphical summary

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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 ...
 117-229 9.21e-21

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: 84.17  E-value: 9.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146099852  117 QMRQNVTEWVKDVRESGGSFLLMYNYLYDYIRGEEDRRMTLTTALSAWDVFFSKN----DLYAKWKAWAVANVKGGVSRD 192
Cdd:pfam03556   1 KLKAKLPELRKELTDPSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRfrifPLLDLWIEFLEEEKKVKISKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 146099852  193 LWRQLGIFFTMDTTAAQ-RFGDQISAlpWPSAIADFLD 229
Cdd:pfam03556  81 TWNMFLEFARKVDEDEDlSNYDEDGA--WPSLIDEFVE 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 ...
 117-229 9.21e-21

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: 84.17  E-value: 9.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146099852  117 QMRQNVTEWVKDVRESGGSFLLMYNYLYDYIRGEEDRRMTLTTALSAWDVFFSKN----DLYAKWKAWAVANVKGGVSRD 192
Cdd:pfam03556   1 KLKAKLPELRKELTDPSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRfrifPLLDLWIEFLEEEKKVKISKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 146099852  193 LWRQLGIFFTMDTTAAQ-RFGDQISAlpWPSAIADFLD 229
Cdd:pfam03556  81 TWNMFLEFARKVDEDEDlSNYDEDGA--WPSLIDEFVE 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 ...
 117-229 9.21e-21

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: 84.17  E-value: 9.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146099852  117 QMRQNVTEWVKDVRESGGSFLLMYNYLYDYIRGEEDRRMTLTTALSAWDVFFSKN----DLYAKWKAWAVANVKGGVSRD 192
Cdd:pfam03556   1 KLKAKLPELRKELTDPSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRfrifPLLDLWIEFLEEEKKVKISKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 146099852  193 LWRQLGIFFTMDTTAAQ-RFGDQISAlpWPSAIADFLD 229
Cdd:pfam03556  81 TWNMFLEFARKVDEDEDlSNYDEDGA--WPSLIDEFVE 116
 
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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