Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

• HOME
• SETUP
• FAQ
• ABOUT
• GLOSSARY
• WHAT'S NEW
• FEEDBACK

BING4CT BING4CT (NUC141) domain

SMART accession number:	SM01033
Description:	This C terminal domain is found in the BING4 family of nucleolar WD40 repeat proteins.
Interpro abstract (IPR012952):	This C-terminal domain is found in the BING4 family of nucleolar WD40 repeat proteins [(PUBMED:15112237)].
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 172 BING4CT domains in 172 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a BING4CT domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with BING4CT domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Staub E, Fiziev P, Rosenthal A, Hinzmann B
  • Insights into the evolution of the nucleolus by an analysis of its proteindomain repertoire.
  • Bioessays. 2004; 26: 567-81
  • Display abstract

  • Recently, the first investigation of nucleoli using mass spectrometry ledto the identification of 271 proteins. This represents a rich resource fora comprehensive investigation of nucleolus evolution. We applied aprotocol for the identification of known and novel conserved proteindomains of the nucleolus, resulting in the identification of 115 known and91 novel domain profiles. The phyletic distribution of nucleolar proteindomains in a collection of complete proteomes of selected organisms fromall domains of life confirms the archaebacterial origin of the coremachinery for ribosome maturation and assembly, but also revealssubstantial eubacterial and eukaryotic contributions to nucleolusevolution. We predict that, in different phases of nucleolus evolution,protein domains with different biochemical functions were recruited to thenucleolus. We suggest a model for the late and continuous evolution of thenucleolus in early eukaryotes and argue against an endosymbiotic origin ofthe nucleolus and the nucleus. Supplementary material for this article canbe found on the BioEssays website athttp://www.interscience.wiley.com/jpages/0265-9247/suppmat/index.html.

• Links (links to other resources describing this domain)

• PFAM	BING4CT
  INTERPRO	IPR012952

Send comments to Ivica Letunic