Family M11

Family

Summary Holotypes Alignment Tree Genomes Literature Architecture

Summary for family M11

NamePeptidase family M11 (gametolysin family)
Family type peptidaseM11.001 - gametolysin (Chlamydomonas reinhardtii), MEROPS Accession MER0001103 (peptidase unit: 184-638)
Content of familyPeptidase family M11 contains a metallo-endopeptidase, gametolysin.
History Identifier created: Biochem.J. 290:205-218 (1993)
Catalytic typeMetallo
Active site residuesH,Q396 E397 H400 H406 
Active siteGametolysin (M11.001) has a metal-binding motif HEXXHXXXXXH. In homologues from Volvox sp., the first His of the active site motif is replaced by Gln, and it has been suggested that this substitution shifts the selectivity of metal-binding from zinc to copper (Heitzer & Hallmann, 2002).
Activities and specificitiesGametolysin is synthesized with an N-terminal propeptide that appears to contain a "cysteine switch" analogous to those in other families in clan MA; activation is by cleavage at the Lys3Glu4 bond (Kinoshita et al., 1992). Gametolysin degrades the proline- and hydroxyproline-rich proteins of the algal cell wall.
Molecular structure
ClanMA
SubclanMA(M)
Basis of clan assignmentPredicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH
Distribution of family Bacteria details  
Archaea -  
Protozoa details  
Fungi -  
Plants details  
Animals -  
Viruses -  
Biological functionsGametolysin is a secreted enzyme that degrades the algal cell wall, allowing the release of gametes.
Statistics for family M11Sequences:229
Identifiers:3
Identifiers with PDB entries:0
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Other databases INTERPRO IPR008752
PFAM PF05548
Peptidases and Homologues MEROPS ID Structure
gametolysinM11.001-
VMP peptidaseM11.002-
mmp2 g.p. (Chlamydomonas reinhardtii)M11.003-
Family M11 non-peptidase homologuesnon-peptidase homologue-
Family M11 unassigned peptidasesunassigned-