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M12 family metallo-peptidase
reprolysin-like metallopeptidase
This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. (from Pfam)
M10 family metallopeptidase C-terminal domain-containing protein
Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain Pfam:PF00353. (from Pfam)
RTX calcium-binding repeat protein
matrixin family metalloprotease
The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. [1]. 7674922. Evolutionary families of metallopeptidases.. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228.. [2]. 7656014. The NMR structure of the inhibited catalytic domain of human. stromelysin-1.. Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL,. Hermes JD, Esser CK, Hagmann WK, Springer JP, et al;. Nat Struct Biol 1994;1:111-118. (from Pfam)
M10 family metallopeptidase
M10 family metallopeptidase similar to serralysin and Pseudomonas aeruginosa alkaline protease, which include an N-terminal peptidase domain and a C-terminal calcium-binding domain
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