ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ASCH resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.

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                  ....*....|....*....|....*....|....*....|.
gi 505238918    4 VHKKKLDFQFHKPVETGEKPFEVRINDCDYQVGDIIELKSY 44
Cdd:pfam12961   1 THELKILPQFFEAVITGRKNFEIRKNDRDYQVGDILLLLEY 41

Domain of unknown function (DUF3850); The search results from NCBI sequence alignment indicates a conserved domain belonging to ASCH superfamily. Dali searching results show that the protein is a structurally similar to the PUA domain, suggesting it may be involved in RNA recognition. It has been reported that the deletion of PUA genes results in impaired growth (RluD) and competitive disadvantage (TruB) in Escherichia coli. Suggestions have been put forward that, apart from their usual catalytic role, certain PUS enzymes (e.g. TruB) may also act as chaperones for RNA folding. The interface interaction indicates that the biomolecule of protein NP_809782.1 should be a dimer.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 505238918    4 VHKKKLDFQFHKPVETGEKPFEVRINDCDYQVGDIIELKSY 44
Cdd:pfam12961   1 THELKILPQFFEAVITGRKNFEIRKNDRDYQVGDILLLLEY 41

Domain of unknown function (DUF3850); The search results from NCBI sequence alignment indicates a conserved domain belonging to ASCH superfamily. Dali searching results show that the protein is a structurally similar to the PUA domain, suggesting it may be involved in RNA recognition. It has been reported that the deletion of PUA genes results in impaired growth (RluD) and competitive disadvantage (TruB) in Escherichia coli. Suggestions have been put forward that, apart from their usual catalytic role, certain PUS enzymes (e.g. TruB) may also act as chaperones for RNA folding. The interface interaction indicates that the biomolecule of protein NP_809782.1 should be a dimer.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 505238918    4 VHKKKLDFQFHKPVETGEKPFEVRINDCDYQVGDIIELKSY 44
Cdd:pfam12961   1 THELKILPQFFEAVITGRKNFEIRKNDRDYQVGDILLLLEY 41