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Here we discovered a novel motif (FMDVF) required for this critical CnaA septal localization, including residues Phe368, Asp370 and Phe372 overlapping the cyclosporine A\u2010cyclophilin A\u2010binding domain, CnaB\u2010binding helix and the FK506\u2010FKBP12\u2010binding pocket. Mutations in adjacent residues Asn367, Trp374, and Ser375 confer FK506 resistance without impacting CnaA septal localization. Modeling <jats:italic>A.\u00a0fumigatus<\/jats:italic> CnaA confirmed that the FMDVF motif forms a bridge between the two known substrate\u2010binding motifs, PxIxIT and LxVP, and concurrent mutations (F368A D370A; F368A F372A) in the FMDVF motif disrupt CnaA\u2010substrate interaction at the septum.<\/jats:p>","DOI":"10.1002\/1873-3468.12075","type":"journal-article","created":{"date-parts":[[2016,2,1]],"date-time":"2016-02-01T07:55:05Z","timestamp":1454313305000},"page":"501-508","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Novel motif in calcineurin catalytic subunit is required for septal localization of calcineurin in <i>Aspergillus\u00a0fumigatus<\/i>"],"prefix":"10.1002","volume":"590","author":[{"given":"Praveen R.","family":"Juvvadi","sequence":"first","affiliation":[{"name":"Division of Pediatric Infectious Diseases Department of Pediatrics Duke University Medical Center Durham NC 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