The domain within your query sequence starts at position 367 and ends at position 563; the E-value for the GuKc domain shown below is 4.01e-65.

All catalytic sites are present in this domain. Check the literature (PubMed 92235848 ) for details.



Guanylate kinase homologues.
SMART accession number:SM00072
Description: Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.
Interpro abstract (IPR008145):

This entry represents a domain found in guanylate kinase ( EC ) and in L-type calcium channel.

Guanylate kinase ( EC ) (GK) [ (PUBMED:1314905) ] 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 [ (PUBMED:1310897) (PUBMED:8097461) (PUBMED:1329277) ] to be structurally similar to protein A57R (or SalG2R) from various strains of Vaccinia virus.

L-type calcium channnels are formed from different alpha-1 subunit isoforms that determine the pharmacological properties of the channel, since they form the drug binding domain. Other properties, such as gating voltage-dependence, G protein modulation and kinase susceptibility, are influenced by alpha-2, delta and beta subunits.

Family alignment:
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There are 42084 GuKc domains in 42042 proteins in SMART's nrdb database.

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