PROSITE logo
Black ribbon
We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51723
Peptidase family M60 domain profile


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51723

Description

The peptidase family M60 domain belongs to the zincin superfamily of zinc-requiring metalloproteases (clan MA, subclan MA(E)) [E1]. The peptidase family M60 domain contains the metal-binding consensus motif HExxH. The two histidine residues are ligands of the catalytic Zn(2+) and the glutamic acid residue is involved in nucleophilic attack. An additional conserved glutamic acid is found approximately 20 residues from the first histidine within the metal-binding motif. The second conserved glutamic acid potentially acts as a third proteous Zn(2+) ligand. The peptidase family M60 domain targets complex host glycoproteins, such as mucins [1,2,3,4,5].

Some proteins known to contain a peptidase family M60 domain are listed below:

  • Baculovirus viral enhancing factor (VEF), also known as Enhancin, a metalloprotease that enhances viral infection by degrading the peritrophic membrane (PM) of the insect midgut.
  • Bacteria enhancin-like metalloproteases.
  • Mammalian FAM115 family proteins.

The profile we developed covers the entire peptidase family M60 domain.

Last update:

June 2014 / First entry.

-------------------------------------------------------------------------------


Technical section

PROSITE method (with tools and information) covered by this documentation:

PEPTIDASE_M60, PS51723; Peptidase family M60 domain profile  (MATRIX)


References

1AuthorsBischoff D.S. Slavicek J.M.
TitleMolecular analysis of an enhancin gene in the Lymantria dispar nuclear polyhedrosis virus.
SourceJ. Virol. 71:8133-8140(1997).
PubMed ID9343163

2AuthorsGalloway C.S. Wang P. Winstanley D. Jones I.M.
TitleComparison of the bacterial Enhancin-like proteins from Yersinia and Bacillus spp. with a baculovirus Enhancin.
SourceJ. Invertebr. Pathol. 90:134-137(2005).
PubMed ID16081094
DOI10.1016/j.jip.2005.06.008

3AuthorsHajaij-Ellouze M. Fedhila S. Lereclus D. Nielsen-LeRoux C.
TitleThe enhancin-like metalloprotease from the Bacillus cereus group is regulated by the pleiotropic transcriptional activator PlcR but is not essential for larvicidal activity.
SourceFEMS Microbiol. Lett. 260:9-16(2006).
PubMed ID16790012
DOI10.1111/j.1574-6968.2006.00289.x

4AuthorsToprak U. Harris S. Baldwin D. Theilmann D. Gillott C. Hegedus D.D. Erlandson M.A.
TitleRole of enhancin in Mamestra configurata nucleopolyhedrovirus virulence: selective degradation of host peritrophic matrix proteins.
SourceJ. Gen. Virol. 93:744-753(2012).
PubMed ID22238230
DOI10.1099/vir.0.038117-0

5AuthorsNakjang S. Ndeh D.A. Wipat A. Bolam D.N. Hirt R.P.
TitleA novel extracellular metallopeptidase domain shared by animal host-associated mutualistic and pathogenic microbes.
SourcePLoS ONE 7:E30287-E30287(2012).
PubMed ID22299034
DOI10.1371/journal.pone.0030287

E1Titlehttps://www.ebi.ac.uk/merops/cgi-bin/famsum?family=M60



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.