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PRC-barrel domain-containing protein
The PRC-barrel is an all beta barrel domain found in photosystem reaction centre subunit H of the purple bacteria and RNA metabolism proteins of the RimM group. PRC-barrels are approximately 80 residues long, and found widely represented in bacteria, archaea and plants. This domain is also present at the carboxyl terminus of the pan-bacterial protein RimM, which is involved in ribosomal maturation and processing of 16S rRNA. A family of small proteins conserved in all known euryarchaea are composed entirely of a single stand-alone copy of the domain [1]. [1]. 12429060. The PRC-barrel: a widespread, conserved domain shared by. photosynthetic reaction center subunits and proteins of RNA. metabolism.. Anantharaman V, Aravind L;. Genome Biol 2002;3:RESEARCH0061.. [2]. 10024457. Refined crystal structures of reaction centres from. Rhodopseudomonas viridis in complexes with the herbicide. atrazine and two chiral atrazine derivatives also lead to a new. model of the bound carotenoid.. Lancaster CR, Michel H;. J Mol Biol 1999;286:883-898. (from Pfam)
YlmC/YmxH family sporulation protein
Members of this family belong to the broader family of PRC-barrel domain proteins (see Pfam model PF05239), but are found only in endospore-forming bacteria of the Firmicutes lineage. Most such species have exactly two members of this family and all have at least one; the function is unknown. One of two members from Bacillus subtilis, YmxH, is strongly induced by the mother cell-specific sigma-E factor.
YlmC/YmxH family sporulation protein is a PRC-barrel domain-containing protein, similar to Bacillus subtilis YmxH that is strongly induced by the mother cell-specific sigma-E factor
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