forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins
EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain 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 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.",