GGDEF domain is homologous to adenylyl cyclase.

@article{Pei2001GGDEFDI,
  title={GGDEF domain is homologous to adenylyl cyclase.},
  author={Jimin Pei and Nick V. Grishin},
  journal={Proteins},
  year={2001},
  volume={42 2},
  pages={210-6}
}
The GGDEF domain is detected in many prokaryotic proteins, most of which are of unknown function. Several bacteria carry 12-22 different GGDEF homologues in their genomes. Conducting extensive profile-based searches, we detect statistically supported sequence similarity between GGDEF domain and adenylyl cyclase catalytic domain. From this homology, we deduce that the prokaryotic GGDEF domain is a regulatory enzyme involved in nucleotide cyclization, with the fold similar to that of the… CONTINUE READING

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The structure, catalytic mechanism and regulation of adenylyl cyclase.

Current opinion in structural biology • 1998
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Highly Influenced

Hybrid fold recognition: combining sequence derived properties with evolutionary information.

Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing • 2000

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