{PDOC00779}
{PS01016; GLYCOPROTEASE}
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* Glycoprotease family signature *
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Glycoprotease (GCP)  (EC 3.4.24.57) [1], 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.

-Consensus pattern: [KRC]-[GSAT]-x(4)-[FYWLMH]-[DQNGKRH]-x-P-x-[LIVMFY]-x(3)-
                    H-x(2)-[GSA]-H-[LIVMFA]
                    [The 2 H's may be zinc ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These proteins belong to family M22 in the classification of peptidases
 [2,E1].

-Expert(s) to contact by email:
           Lo R.Y.C.; rlo@uoguelph.ca

-Last update: April 2006 / Pattern revised.

[ 1] 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).
     PubMed=1885539
[ 2] Rawlings N.D., Barrett A.J.
     "Evolutionary families of metallopeptidases."
     Methods Enzymol. 248:183-228(1995).
     PubMed=7674922
[E1] https://www.uniprot.org/docs/peptidas

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