PROSITE documentation PDOC00703

Protein prenyltransferases alpha subunit repeat profile




Description

Protein prenyltransferases catalyze the transfer of an isoprenyl moiety to a cysteine at or near the C-terminus of several eukaryotic proteins. They are heterodimeric enzymes consisting of α and β subunits. The α subunit is thought to participate in a stable complex with the isoprenyl substrate; the β subunit binds the peptide substrate. There are three types of protein prenyltransferases. The α subunits of two types, i.e. farnesyltransferase and geranylgeranyltransferase I are encoded by the same gene, FNTA. These proteins bind the same motif (the CaaX box) around the cysteine in their substrates. The third type, geranylgeranyl transferase type II (Rab GG transferase) recognizes a different, non-CaaX motif [1].

Both the α and β subunit show repetitive sequence motifs [2]. These repeats have distinct structural and functional implications and are unrelated to each other. The conserved domain of the α subunit consists of about 35 amino acids and is repeated five times. The domain folds into a pair of antiparallel α helices, which are packed in a parallel arrangement with adjacent domains in a superhelical pattern (see <PDB:1TN6>). A conserved tryptophan in the fourth position of the second helix interacts with both the first helix and the neighboring helix of the next repeat [3].

Two types of protein prenyltransferase α subunits are known:

  • Farnesyltransferase/geranylgeranyltransferase type-1 subunit α (EC 2.5.1.58) (EC 2.5.1.59).
  • Geranylgeranyl transferase type-2 subunit α (EC 2.5.1.60).

The profile we developed covers the entire protein prenyltransferases α subunit repeat.

Last update:

October 2005 / Pattern removed, profile added and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PFTA, PS51147; Protein prenyltransferases alpha subunit repeat profile  (MATRIX)


References

1AuthorsMaurer-Stroh S., Washietl S., Eisenhaber F.
TitleProtein prenyltransferases.
SourceGenome Biol. 4:212-212(2003).
PubMed ID12702202

2AuthorsBoguski M.S., Murray A.W., Powers S.
TitleNovel repetitive sequence motifs in the alpha and beta subunits of prenyl-protein transferases and homology of the alpha subunit to the MAD2 gene product of yeast.
SourceNew Biol. 4:408-411(1992).
PubMed ID1622936

3AuthorsZhang H., Grishin N.V.
TitleThe alpha-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family.
SourceProtein Sci. 8:1658-1667(1999).
PubMed ID10452610



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