FATC domain (IPR003152)

Short name: FATC_dom

Overlapping homologous superfamilies


Domain relationships



Phosphatidylinositol kinase (PIK)-related kinases participate in meiotic and V(D)J recombination, chromosome maintenance and repair, cell cycle progression, and cell cycle checkpoints, and their dysfunction can result in a range of diseases, including immunodeficiency, neurological disorder and cancer. The catalytic kinase domain is highly homologuous to that of phosphatidylinositol 3- and 4-kinases. Nevertheless, members of 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 [PMID: 7569949] and the ~35 residue C-terminal FATC domain [PMID: 10782091].

It has been proposed that the FAT domain could be of importance as a structural scaffold or as a protein-binding domain, or both [PMID: 7569949].

The TOR1 FATC domain, in its oxidized form, consists of an alpha-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 of FATC to its partners [PMID: 15772072].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005515 protein binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles