Protein Family Models for Protein (Select 498913422) - Protein Family Models

Select item 4262981.

This is a family of uncharacterised proteins that carry the highly characteristic met-zincin motif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases. [1]. 24095060. EcxAB is a founding member of a new family of metalloprotease AB5 toxins with a hybrid cholera-like B subunit. Ng NM, Littler DR, Paton AW, Le Nours J, Rossjohn J, Paton JC, Beddoe T;. Structure. 2013;21:2003-2013. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF027637.5
Method:: HMM

Select item 4220772.

reprolysin-like metallopeptidase

This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. (from Pfam)

GO Terms:

Molecular Function:: metallopeptidase activity (GO:0008237)

Molecular Function:: zinc ion binding (GO:0008270)

Date:: 2024-08-14

Family Accession:: NF024972.5
Method:: HMM

Select item 4181843.

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)

GO Terms:

Molecular Function:: calcium ion binding (GO:0005509)

Cellular Component:: extracellular space (GO:0005615)

Date:: 2024-08-14

Family Accession:: NF020137.5
Method:: HMM

Select item 4117664.

RTX calcium-binding repeat protein

GO Terms:

Molecular Function:: calcium ion binding (GO:0005509)

Date:: 2024-08-14

Family Accession:: NF012573.5
Method:: HMM

Select item 4109355.

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)

GO Terms:

Molecular Function:: metalloendopeptidase activity (GO:0004222)

Biological Process:: proteolysis (GO:0006508)

Molecular Function:: zinc ion binding (GO:0008270)

Cellular Component:: extracellular matrix (GO:0031012)

Date:: 2024-10-16

Family Accession:: NF012630.5
Method:: HMM

Select item 4086906.