ASCH |
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| SMART accession number: | SM01022
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| Description: |
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation (PUBMED:16322048). |
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| Interpro abstract (IPR007374): |
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain (IPR002478). It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation [(PUBMED:16322048)].
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| Family alignment: |
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There are 902
ASCH domains in 902 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: translation
Binding / catalysis: RNA
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Iyer LM, Burroughs AM, Aravind L
- The ASCH superfamily: novel domains with a fold related to the PUA domainand a potential role in RNA metabolism.
- Bioinformatics. 2006; 22: 257-63
- Display abstract
Several studies show that transcription coactivators are oftenbi-functional ribonucleoprotein complexes that also regulate pre-mRNAprocessing and splicing decisions. Using sensitive sequence profilesearches and structural comparisons we show that the C-terminal domain ofthe human coactivator protein ASC-1 defines a novel superfamily, the ASC-1homology (ASCH) domain. The approximately 110 amino acid long ASCH domainsare widely represented in all the three superkingdoms of life and severalprokaryotic viruses. We show that the ASCH superfamily adopts abeta-barrel fold similar to the PUA domain superfamily. Using multiplelines of evidence, we suggest that members of the ASCH superfamily arelikely to function as RNA-binding domains in contexts related tocoactivation, RNA-processing and possibly prokaryotic translationregulation. Structural analysis of ASCH domains reveals the presence of apotential RNA-binding cleft associated with a conserved sequence motif,which is characteristic of this superfamily. Despite their similarstructure, the ASCH and PUA domains appear to occupy distinct functionalniches, with the former domains typically occurring in a standalone formin polypeptides, and the latter domains showing fusions to a variety ofRNA-modifying enzymes.
- Structure (3D structures containing this domain)
3D Structures of ASCH domains in PDB
| PDB code | Main view | Title | | 1s04 |  | Solution nmr structure of protein pf0455 from pyrococcus furiosus. northeast structural genomics consortium target pfr13 |
| 1t62 |  | Crystal structure of protein ef3133 from enterococcus faecalis v583, pfam duf984 |
| 1te7 |  | Solution nmr structure of protein yqfb from escherichia coli. northeast structural genomics consortium target et99 |
| 1wk2 |  | Crystal structure of a hypothetical protein from thermus thermophilus hb8 |
| 1xne |  | Solution structure of pyrococcus furiosus protein pf0470: the northeast structural genomics consortium target pfr14 |
| 2dp9 |  | Crystal structure of conserved hypothetical protein ttha0113 from thermus thermophilus hb8 |
| 2e5o |  | 'solution structure of the trip_4c domain of target of activating signal cointegrator 1 |
| 2z0t |  | Crystal structure of hypothetical protein ph0355 |
| 3iuw |  | Crystal structure of activating signal cointegrator (np_814290.1) from enterococcus faecalis v583 at 1.58 a resolution |
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a ASCH domain in a specific node, click on it.