Protein Domain : IPR008330

Type:  Family Name:  Peptidase M17, peptidase B
Description:  Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].This family represents the peptidase B group of leucyl aminopeptidases, which are restricted to the gammaproteobacteria. They contain a C-terminal aminopeptidase catalytic domain and an N-terminal domain of unknown function. They are zinc-dependent exopeptidases () and belong to MEROPS peptidase family M17 (leucyl aminopeptidase family, clan MF).They selectively release N-terminal amino acid residues from polypeptides and proteins and are involved in the processing, catabolism and degradation of intracellular proteins [, , ]. Leucyl aminopeptidase forms a homohexamer containing two trimers stacked on top of one another []. Each monomer binds two zinc ions. The zinc-binding and catalytic sites are located within the C-terminal catalytic domain [].The same catalytic aminopeptidase domain is found in the other M17 peptidases . These two groups of aminopeptidases differ by their N-terminal domains. The N-terminal domain in members of has been implicated in DNA binding [, ] and it is not associated with members of this family which have a different N-terminal domain and therefore are not expected to bind DNA or be involved in transcriptional regulation. In addition, there are related proteins with the same catalytic domain and unique N-terminal sequences unrelated to any of the two N-terminal domains discussed above.For additional information please see [, , , ]. Short Name:  Pept_M17_PepB
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0 Child Features

1 Contains

DB identifier Type Name
IPR000819 Domain Peptidase M17, leucyl aminopeptidase, C-terminal

3 Cross Referencess

Identifier
PF12404
PIRSF036388
MF_00504

0 Found In

5 GO Annotations

GO Term Gene Name
GO:0004177 IPR008330
GO:0008235 IPR008330
GO:0030145 IPR008330
GO:0006508 IPR008330
GO:0005737 IPR008330

5 Ontology Annotations

GO Term Gene Name
GO:0004177 IPR008330
GO:0008235 IPR008330
GO:0030145 IPR008330
GO:0006508 IPR008330
GO:0005737 IPR008330

1 Parent Features

DB identifier Type Name
IPR011356 Family Leucine aminopeptidase/peptidase B

2 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Brdisv1pangenome1010331m.p PAC:33657846 Brachypodium distachyon Pangenome 638  
Brdisv1BdTR11A1040840m.p PAC:35688702 Brachypodium distachyon BdTR11a 372  

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            7674922
            8439290
            1555602
            2395881
            8703509
            10449417
            10970742
            10852868
            8506345