Protein Family Models

This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3]. The structure of a representative of this family.. [1]. 8471602. Structure of the cobalt-dependent methionine aminopeptidase from. Escherichia coli: a new type of proteolytic enzyme.. Roderick SL, Matthews BW. Biochemistry 1993;32:3907-3912.. -!- Members of this family are metallopeptidases. They belong. to family M24 in the classification of Rawlings and Barrett.. [2]. 7674922. Evolutionary families of metallopeptidases.. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228.. [3]. 18579787. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding. module.. Stuwe T, Hothorn M, Lejeune E, Rybin V, Bortfeld M, Scheffzek K,. Ladurner AG;. Proc Natl Acad Sci U S A. 2008;105:8884-8889. (from Pfam)

Date:

2024-08-14

Methionine aminopeptidase (map) is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation.

Gene:

map

Date:

2024-06-04