The domain within your query sequence starts at position 184 and ends at position 375; the E-value for the Peptidase_M20 domain shown below is 2.9e-8.



PFAM accession number:PF01546
Interpro abstract (IPR002933):

This group of proteins contains the metallopeptidases and non-peptidase homologues (amidohydrolases) that belong to the MEROPS peptidase family M20 (clan MH) [ (PUBMED:7674922) ]. The peptidases of this clan have two catalytic zinc ions at the active site, bound by His/Asp, Asp, Glu, Asp/Glu and His. The catalysed reaction involves the release of an N-terminal amino acid, usually neutral or hydrophobic, from a polypeptide [ (PUBMED:7674922) ]. The peptidase M20 family has four subfamilies:

  • M20A - type example, glutamate carboxypeptidase from Pseudomonas sp. RS16 ( P06621 )
  • M20B - type example, peptidase T from Escherichia coli ( P29745 )
  • M20C - type example, X-His dipeptidase from E. coli ( P15288 )
  • M20D - type example, carboxypeptidase Ss1 from Sulfolobus solfataricus ( P80092 )

Homologues from the family that are not peptidases include:

  • Acetylornithine deacetylase, which releases an acetyl group and L-ornithine from N(2)-acetyl-L-ornithine [ (PUBMED:10684608) ]
  • N-acetyldiaminopimelate deacetylase, which catalyses the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate [ (PUBMED:5411754) ]
  • N-carbamoyl-L-amino-acid hydrolase, which converts D,L-5-monosubstituted hydantoins into D- or L-amino acids [ (PUBMED:1732229) ]
  • Aminoacylase-1, which hydrolyses N-acylated or N-acetylated amino acids [ (PUBMED:12933810) ]
  • Succinyl-diaminopimelate desuccinylase (EC:, which catalyses the hydrolysis of N-succinyl-L,L-diaminopimelic acid, forming succinate and LL-2,6-diaminoheptanedioate (DAP, a component of bacterial cell walls) [ (PUBMED:3276674) ]
GO function:hydrolase activity (GO:0016787)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M20