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molybdopterin-binding protein
This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation [1]. [1]. 11325967. X-ray crystal structure of the trimeric N-terminal domain of gephyrin. Sola M, Kneussel M, Heck IS, Betz H, Weissenhorn W;. J Biol Chem 2001;276:25294-25301. (from Pfam)
competence/damage-inducible protein A
competence/damage-inducible protein A (CinA) may play a role in transformation
nicotinamide mononucleotide deamidase-related protein YfaY
YfaY from E. coli, previously known as CinA, is a protein of unknown function, similar to the nicotinamide mononucleotide deamidase PncC. Proteins described as CinA have been associated with the induction by DNA damage and with competence in species capable of natural transformation.
molybdenum cofactor synthesis domain-containing protein
The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this HMM. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
CinA family nicotinamide mononucleotide deamidase-related protein
CinA has been described a DNA damage-inducible protein associated with competence for natural transformation. Members of this family include the nicotinamide-nucleotide amidase PncC (EC 3.5.1.42), such as YfaY from E. coli, rather than PncC itself.
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