The domain within your query sequence starts at position 4096 and ends at position 4128; the E-value for the FATC domain shown below is 1.4e-6.
SGLSEETQVKCLVDQATDPNILGRTWEGWEPWM
FATC |
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PFAM accession number: | PF02260 |
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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) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry FATC