SMART accession number:SM01343
Description: The FATC domain is named after FRAP, ATM, TRRAP C-terminal (PMID:10782091). The solution structure of the FATC domain suggests it plays a role in redox-dependent structural and cellular stability (PMID:15772072).
Interpro abstract (IPR003152):

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 [ (PUBMED:7569949) ] and the ~35 residue C-terminal FATC domain [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:15772072) ].

GO function:protein binding (GO:0005515)
Family alignment:
View or

There are 7901 FATC domains in 7895 proteins in SMART's nrdb database.

Click on the following links for more information.