Probable serine/threonine-protein kinase pknG (Mycobacterium) | Serine/threonine-protein kinase pknB (Mycobacterium) |
Motif | Protein | Start | End | Switch Type | Switch Subtype | Switch description | Information | Evidence |
Probable serine/threonine-protein kinase pknG - PKNG -  Mycobacterium tuberculosis | ||||||||
LIG_FHA_1 | Y1827_MYCTU | 19 | 25 | Binary | Physicochemical compatibility | Phosphorylation of T21 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Probable serine/threonine-protein kinase pknG (pknG) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details). | Curated | |
Serine/threonine-protein kinase pknB - PKNB -  Mycobacterium tuberculosis | ||||||||
LIG_FHA_1 | Y1827_MYCTU | 20 | 26 | Binary | Physicochemical compatibility | Phosphorylation of T22 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Serine/threonine-protein kinase pknB (pknB) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details). | Curated |