|PROSITE documentation PDOC00779
Glycoprotease family signature
Glycoprotease (GCP) (EC 220.127.116.11) , or o-syaloglycoprotein endopeptidase,
is a metalloprotease secreted by Pasteurella haemolytica which specifically
cleaves O-sialoglycoproteins such as glycophorin A. The sequence of GCP is
highly similar to uncharacterized orthologs in most complete genomes of
bacteria and archaebacteria as well as in yeast (QRI7 and YKR038c).
One of the conserved regions contains two conserved histidines. It is possible
that this region is involved in coordinating a metal ion such as zinc.
These proteins belong to family M22 in the classification of peptidases
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|GLYCOPROTEASE, PS01016; Glycoprotease family signature (PATTERN)
The 2 H's may be zinc ligands
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
2IVN 2IVO 2IVP 2VWB ... [ALL]
||Abdullah K.M., Lo R.Y.C., Mellors A.
||Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene.
||J. Bacteriol. 173:5597-5603(1991).
||Rawlings N.D., Barrett A.J.
||Evolutionary families of metallopeptidases.
||Methods Enzymol. 248:183-228(1995).
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