| Type: | Conserved_site | Name: | Peptidase M22, conserved site |
| Description: | Glycoprotease (Gcp) () [], or o-syaloglycoprotein endopeptidase, is a metalloprotease secreted by Pasteurella haemolytica which specifically cleaves O-sialoglycoproteins such as glycophorin A. It belongs to the peptidase family M22. The sequence of Gcp is highly similar to uncharacterised orthologues in most complete genomes of bacteria and archaebacteria as well as in yeast (QRI7 and YKR038c).This entry represents a conserved site found in proteins classified as M22 peptidases, though there is a lack of experimental evidence to support peptidase activity as a general property of this family. This site contains two conserved histidines. It is possible that this region is involved in coordinating a metal ion such as zinc. | Short Name: | Peptidase_M22_CS |
| DB identifier | Type | Name |
|---|---|---|
| IPR017861 | Family | Kae1/TsaD family |
| IPR000905 | Domain | Gcp-like domain |
| IPR022450 | Family | tRNA N6-adenosine threonylcarbamoyltransferase, TsaD |
| IPR009220 | Family | Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein |
| IPR022449 | Family | tRNA N6-adenosine threonylcarbamoyltransferase, Kae1 |
