PHD finger found in Schizosaccharomyces pombe Set1 complex component ash2 (spAsh2p) and similar proteins
spAsh2p, also termed Set1C component ash2, or COMPASS component ash2, or complex proteins associated with set1 protein ash2, or Lid2 complex component ash2, or Lid2C component ash2, is orthologous to Drosophila melanogaster Ash2 protein. Both spAsh2p and D. melanogaster Ash2 contain a plant homeodomain (PHD) finger and a SPRY domain. In contrast, its counterpart in Saccharomyces cerevisiae, Bre2p, has no PHD finger and is not included in this family. spAsh2p shows histone H3 Lys4 (H3K4) methyltransferase activity through its PHD finger. It also interacts with Lid2p in S. pombe. Human Ash2L contains an atypical PHD finger that lacks part of the Cys4HisCys3 signature characteristic of PHD fingers, it binds to only one zinc ion through the second half of the motif and does not have histone tail binding activity.
Conserved feature residue pattern:C C C [CH] H [CH] C [CH]
Evidence:
Comment:Based on the structures of human Ash2L PHD1 bound with a zinc ion and with other PHD fingers having two zinc ions bound. Note that the human Ash2L PHD finger lacks part of the conserved Cys4HisCys3 signature that mediates the coordination of the two zinc ions.
Structure:3RSN: Human Ash2l PHD finger binds a zinc ion; contacts at 4A