Protein Domain : Protein farnesyltransferase subunit beta IPR026872

Type	Family
Description	Protein farnesyltransferase (FTase) is an enzyme responsible for the posttranslational modification (farnesylation) of proteins carrying a carboxy-terminal CaaX motif, including Ras, Ras homologues, and other small G proteins. FTase catalyses the transfer of a farnesyl moiety from farnesyl pyrophosphate to the cysteine at the CaaX motif, where a is a small aliphatic amino acid and X is the carboxy-terminal residue [ , ]. Prenyltransferase employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C terminus of protein acceptors and the C1 atom of isoprenoid lipids. FTase attaches a 15-carbon farnesyl group to the cysteine within the C-terminal CaaX motif of substrate proteins when X is Ala, Met, Ser, Cys or Gln [, , ]. FTase is a heterodimeric complex comprised of a regulatory alpha subunit shared with geranylgeranyltransferase I (also a CaaX prenyltransferase) and a unique catalytic beta subunit [ ]. FTase plays important roles in the growth and differentiation of eukaryotic cells. It is essential for embryonic proliferation, but dispensable for adult homeostasis []. In plants, is involved in abscisic acid signal transduction, which modulates a variety of developmental processes and responses to environmental stress []. In yeast, protein farnesylation is important for maintaining normal cell morphology [] and for cell cycle progression [].
Short Name	FTB