N-terminal Putative NodB-like catalytic domain of hypothetical proteins containing C-terminal cadherin or MopE copper binding domains
The family includes several cadherin or MopE copper binding domain containing hypothetical proteins found in bacteria. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium. They play a role in cell fate, signalling, proliferation, differentiation, and migration. The copper binding domain involves a tryptophan metabolite, kynurenine, in the protein MopE. Members of this family contain an additional conserved domain, which is N-terminally fused to the cadherin domain or the MopE copper binding domain. Although its function remains unclear, the conserved domain exhibits a seven-stranded barrel with a detectable sequence similarity to the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily.