forkhead associated (FHA) domain found in PHD finger protein 12 (PHF12) and similar proteins
PHF12, also called PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. It also contains an FHA domain, which is a small phosphopeptide recognition module.
Feature 1:putative phosphopeptide binding site [polypeptide binding site]
Evidence:
Comment:based on structures of other FHA domains with bound phosphopeptide
Comment:GR at the C terminus of strand beta3, SRxH just preceding beta5, and motif SxNG (SxHG in this model) in the beta6-beta7 turn indicate a canonical mode of pThr recognition.
Comment:Conserved residues are involved in binding directly to the ligand backbone and phosphate group. Non-conserved residues may determine binding specificity.
Jiyao W et al.(2023). "The conserved domain database in 2023.",