Protein Family Models

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)

Date:

2024-10-16

molybdenum cofactor biosynthesis protein B (MoaB) similar to Escherichia coli K-12 MoaB, which may be involved in the biosynthesis of molybdopterin and can bind metal-binding pterin (MPT) but has no MPT adenylyl transferase activity

Date:

2023-03-08

This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA.

Gene:

moaB

Date:

2021-04-27

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.

Date:

2023-10-19