This domain can be found in the eukaryotic ribosome biogenesis protein Tsr3, which is involved in ribosomal RNA biogenesis []. This domain is also found in the C terminus of Tsr3 homologues from archaea. It is usually associated with a putative metal-binding region in RNase L inhibitor, RLI (). Tsr3 from fungi and animals are responsible for 18S rRNA hypermodification. The Crystal structure of archaeal Tsr3 homologues revealed the same fold as in SPOUT-class RNA-methyltransferases but a distinct SAM binding mode. This unique SAM binding mode explains why Tsr3 transfers the acp and not the methyl group of SAM to its substrate. Structurally, Tsr3 therefore represents a novel class of acp transferase enzymes [].
Characterization of mutant forms of recombinant human properdin lacking single thrombospondin type I repeats. Identification of modules important for function.
