Raptor_N

Raptor N-terminal CASPase like domain
Raptor_N
SMART accession number:SM01302
Description: This domain is found at the N-terminus of the Raptor protein. It has been identified to have a CASPase like structure PMID:15450605. It conserves the characteristic cys/his dyad of the caspases suggesting it may have a peptidase activity.
Interpro abstract (IPR029347):

Human Raptor is involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals. It functions as a scaffold for recruiting mTORC1 substrates [(PUBMED:12150925)].

All Raptor orthologs contain a unique conserved region in their N-terminal half (raptor N-terminal conserved, also called the RNC domain) followed by three HEAT (huntingtin, elongation factor 3, A subunit of protein phosphatase 2A and TOR1) repeats and seven WD-40 repeats near the C terminus [(PUBMED:12150925), (PUBMED:12150926)].

This entry reprsents the RNC domain, which consists of 3 blocks with at least 67 to 79% sequence similarity and is predicted to have a high propensity to form alpha helices. The RNC domain is characterised by the presence of invariant catalytic Cys-His dyad, which is structurally and evolutionarily related to known caspases, suggesting that the raptor proteins may have protease activity [(PUBMED:15450605)].

Family alignment:
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There are 1906 Raptor_N domains in 1904 proteins in SMART's nrdb database.

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