The domain within your query sequence starts at position 3815 and ends at position 3847; the E-value for the FATC domain shown below is 1.89e-3.

QFDGGESKVNTLVAAANSLDNLCRMDPAWHPWL

FATC

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

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