The domain within your query sequence starts at position 1084 and ends at position 1189; the E-value for the RICTOR_phospho domain shown below is 4.06e-58.

SFPFFGSSKLVKNRILNSLTLPTKKHRSSSDPKGGKLSSENKTSNRRIRTLTEPSVDLNH
SEDFTSSSAQKSLQLEPSFVGNKHLEDAGSTPSIGENDLKFPKSFG

RICTOR_phospho

Rapamycin-insensitive companion of mTOR, phosphorylation-site
RICTOR_phospho
SMART accession number:SM01309
Description: Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient- and growth-factor signalling. This short region is the phoshorylation site. Rictor does interact with 14-3-3 in a Thr1135-dependent manner. Rictor can be inhibited by short-term rapamycin treatment showing that Thr1135 is an mTORC1-regulated site.
Interpro abstract (IPR029259):

The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTORC1 and mTORC2, important for nutrient- and growth-factor signalling [(PUBMED:20418915)]. Rictor (rapamycin-insensitive companion of mTOR) is an essential component of the complex mTORC2 [(PUBMED:15268862)]. It appears to serve as a scaffolding protein important for maintaining mTORC2 integrity. Rictor interacts with 14-3-3 in a Thr1135-dependent manner [(PUBMED:15268862)]. Rictor can be inhibited by short-term rapamycin treatment, showing that Thr1135 is an mTORC1-regulated site [(PUBMED:19995915)].

This short region is the phoshorylation site of Rictor.

Family alignment:
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There are 531 RICTOR_phospho domains in 477 proteins in SMART's nrdb database.

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