| Primary Identifier | IPR043172 | Type | Homologous_superfamily |
| Short Name | Prp8_domainIV_palm |
| description | Prp8 is the largest and most highly conserved spliceosomal protein and is considered a master regulator of the spliceosome. It forms a salt-stable complex with the Brr2 helicase that is required for spliceosome catalytic activation and disassembly, and with the Snu114 GTPase that regulates Brr2 activity. Prp8 consists of a phylogenetically conserved Rnase H fold along with Prp8-specific elements. The function of this domain is to help assemble and stabilise the spliceosomal catalytic core and coordinate the activities of other splicing factors []. The overall structure of Rnase H is reminiscent of a left-hand mitten, in which a central six-stranded mixed β-sheet and the surrounding α-helices of the N-terminal domain correspond to the palm, an extended β-hairpin of the N-terminal domain comprises the thumb and the α-helical C-terminal domain represents the fingers []. This entry represents the palm region of the Rnase H domain which also includes the β-hairpin thumb. |
