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Conserved domains on  [gi|24645661|ref|NP_649996|]
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uncharacterized protein Dmel_CG12818 [Drosophila melanogaster]

Protein Classification

CIR N-terminal domain-containing protein( domain architecture ID 10660961)

CIR N-terminal domain-containing protein such as CWC25 which is involved in pre-mRNA splicing as a component of the spliceosome, and CIR1 (corepressor interacting with RBPJ) which is a component of the Notch corepressor complex and the histone deacetylase complex, and plays a role in splicing regulation and in RBPJ-mediated repression of transcription

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cir_N smart01083
N-terminal domain of CBF1 interacting co-repressor CIR; This is a 45 residue conserved region ...
8-44 5.16e-05

N-terminal domain of CBF1 interacting co-repressor CIR; This is a 45 residue conserved region at the N-terminal end of a family of proteins referred to as CIRs (CBF1-interacting co-repressors). CBF1 (centromere-binding factor 1) acts as a transcription factor that causes repression by binding specifically to GTGGGAA motifs in responsive promoters, and it requires CIR as a co-repressor. CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex.


:

Pssm-ID: 198151 [Multi-domain]  Cd Length: 37  Bit Score: 39.83  E-value: 5.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 24645661      8 RWHVRTKENIARVRRDQAAAAAEEKVRQEKLEFAESE 44
Cdd:smart01083   1 SWHPGNKKNQKRVWKAEQKAEEEKKKIEERRKEIEKE 37
 
Name Accession Description Interval E-value
Cir_N smart01083
N-terminal domain of CBF1 interacting co-repressor CIR; This is a 45 residue conserved region ...
8-44 5.16e-05

N-terminal domain of CBF1 interacting co-repressor CIR; This is a 45 residue conserved region at the N-terminal end of a family of proteins referred to as CIRs (CBF1-interacting co-repressors). CBF1 (centromere-binding factor 1) acts as a transcription factor that causes repression by binding specifically to GTGGGAA motifs in responsive promoters, and it requires CIR as a co-repressor. CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex.


Pssm-ID: 198151 [Multi-domain]  Cd Length: 37  Bit Score: 39.83  E-value: 5.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 24645661      8 RWHVRTKENIARVRRDQAAAAAEEKVRQEKLEFAESE 44
Cdd:smart01083   1 SWHPGNKKNQKRVWKAEQKAEEEKKKIEERRKEIEKE 37
 
Name Accession Description Interval E-value
Cir_N smart01083
N-terminal domain of CBF1 interacting co-repressor CIR; This is a 45 residue conserved region ...
8-44 5.16e-05

N-terminal domain of CBF1 interacting co-repressor CIR; This is a 45 residue conserved region at the N-terminal end of a family of proteins referred to as CIRs (CBF1-interacting co-repressors). CBF1 (centromere-binding factor 1) acts as a transcription factor that causes repression by binding specifically to GTGGGAA motifs in responsive promoters, and it requires CIR as a co-repressor. CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex.


Pssm-ID: 198151 [Multi-domain]  Cd Length: 37  Bit Score: 39.83  E-value: 5.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 24645661      8 RWHVRTKENIARVRRDQAAAAAEEKVRQEKLEFAESE 44
Cdd:smart01083   1 SWHPGNKKNQKRVWKAEQKAEEEKKKIEERRKEIEKE 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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