LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | Phosphatidylinositol kinase (PIK)-related kinases participate in meiotic and V(D)J recombination, chromosome maintenance and repair, cell cycleprogression, and cell cycle checkpoints, and their dysfunction can result in a range of diseases, including immunodeficiency, neurological disorder andcancer. The catalytic kinase domain is highly homologuous to that of phosphatidylinositol 3- and 4-kinases. Nevertheless, membersof the PIK-related family appear functionally distinct, as none of them has been shown to phosphorylate lipids, such as phosphatidylinositol; instead,many have Ser/Thr protein kinase activity. The PI-kinase domain of members of the PIK-related family is wedged between the ~550-amino acid-long FAT (FRAP,ATM, TRRAP) domain [ ] and the ~35 residue C-terminal FATC domain [].It has been proposed that the FAT domain could be of importance as a structural scaffold or as a protein-binding domain, or both [].The TOR1 FATC domain, in its oxidized form, consists of an α-helix and a well structured COOH-terminal disulfide-bonded loop.Reduction of the disulfide bond dramatically increases the flexibility within the COOH-terminal loop region. The reduction may alter the binding behavior ofFATC to its partners [ ]. |
| Short Name | FATC_dom |
