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A 14 kDa protein homologous to the γ‐ d ‐glutamyl‐ l ‐diamino acid endopeptidase members of the NlpC/P60 Superfamily has been described in  Dermatophagoides pteronyssinus  and  Dermatophagoides farinae  but it is not clear whether other species produce homologues. Bioinformatics revealed homologous genes in other Sarcopteformes mite species ( Psoroptes ovis  and  Blomia tropicalis ) but not in  Tetranychus urticae  and  Metaseiulus occidentalis . The degrees of identity (similarity) between the  D. pteronyssinus  mature protein and those from  D. farinae ,  P. ovis  and  B. tropicalis  were 82% (96%), 77% (93%) and 61% (82%), respectively. Phylogenetic studies showed the mite proteins were monophyletic and shared a common ancestor with both actinomycetes and ascomycetes. The gene encoding the  D. pteronyssinus  protein was polymorphic and intronless in contrast to that reported for  D. farinae . Homology studies suggest that the mite, ascomycete and actinomycete proteins are involved in the catalysis of stem peptide attached to peptidoglycan. The finding of a gene encoding a P60 family member in the  D. pteronyssinus  genome together with the presence of a bacterial promotor suggests an evolutionary link to one or more prokaryotic endosymbionts.

House dust mites possess a polymorphic, single domain putative peptidoglycan d , l endopeptidase belonging to the NlpC/P60 Superfamily