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PDOC00670
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1995-07-26
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49 lines
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* Guanylate kinase signature *
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Guanylate kinase (EC 2.7.4.8) (GK) [1] catalyzes the ATP-dependent
phosphorylation of GMP into GDP. It is essential for recycling GMP and
indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes
(such as yeast) and in vertebrates, GK is a highly conserved monomeric
protein of about 200 amino acids. GK has been shown [2,3,4] to be structurally
similar to the following proteins:
- Protein A57R (or SalG2R) from various strains of Vaccinia virus. This
protein is highly similar to GK, but contains a frameshift mutation in the
N-terminal section and could therefore be inactive in that virus.
The following proteins are characterized by the presence in their sequence of
a SH3 domain as well as a C-terminal GK-like domain:
- Drosophila lethal(1)discs large-1 tumor suppressor protein (gene dlg1).
This protein is associated with septate junctions in developing flies and
defects in the dlg1 gene cause neoplastic overgrowth of the imaginal disks.
Dlg1 is a protein of 960 amino acids.
- Rat postsynaptic density protein 95 (PSD-95). PSD-95 is a protein of 724
amino acids which is enriched in the postsynaptic density fraction.
- Human 55 Kd erythrocyte membrane protein (p55). p55 is a palmitoylated,
membrane-associated protein of unknown function. p55 is a protein of 460
amino acids.
There is an ATP-binding site (P-loop) in the N-terminal section of GK. This
region is not conserved in the GK-like domain of the above proteins which are
therefore unlikely to be kinases. However these proteins retain the residues
known, in GK, to be involved in the binding of GMP. As a signature pattern we
selected a highly conserved region that contains two arginine and a tyrosine
which are involved in GMP-binding.
-Consensus pattern: T-T-R-x(2)-R-x(2)-E-x(2)-G-x(2)-Y-x-[FY]-[LIVM]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Last update: October 1993 / First entry.
[ 1] Stehle T., Schulz G.E.
J. Mol. Biol. 224:1127-1141(1992).
[ 2] Bryant P.J., Woods D.F.
Cell 68:621-622(1992).
[ 3] Goebl M.G.
Trends Biochem. Sci. 17:99-99(1992).
[ 4] Zschocke P.D., Schiltz E., Schulz G.E.
Eur. J. Biochem. 213:263-269(1993).