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524  structures 9069  species 0  interactions 114899  sequences 531  architectures

Clan: Peptidase_ME (CL0094)


LuxS/MPP-like metallohydrolase Add an annotation

All members of this clan are characterised by a HXXEH motif, which is is involved in zinc binding. Furthermore all members adopt an alpha and beta fold. More specifically, there us a four to six stranded antiparallel beta sheet surrounded by five helices. However, LuxS (PFAM:PF02664) is not a peptidase, although its hydrolytic mechanism of catalysis appears to be conserved [1].

This clan contains 8 families and the total number of domains in the clan is 114899. The clan was built by RD Finn.

Literature references

  1. Hilgers MT, Ludwig ML; , Proc Natl Acad Sci U S A 2001;98:11169-11174.: Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site. PUBMED:11553770 EPMC:11553770


This clan contains the following 8 member families:

LuxS M16C_assoc Peptidase_M16 Peptidase_M16_C Peptidase_M16_M Peptidase_M44 tRNA_bind_4 tRNA_SAD

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
Peptidase_M16_C (PF05193) 44133 (38.4%) View
Peptidase_M16 (PF00675) 34678 (30.2%) View
tRNA_SAD (PF07973) 25601 (22.3%) View
Peptidase_M16_M (PF16187) 5343 (4.7%) View
M16C_assoc (PF08367) 3045 (2.7%) View
LuxS (PF02664) 2019 (1.8%) View
tRNA_bind_4 (PF18490) 41 (0.0%) View
Peptidase_M44 (PF03410) 39 (0.0%) View
Total: 8 Total: 114899 Clan alignment

Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.

Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

Tree controls


This tree shows the occurrence of the domains in this clan across different species. More...



For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

Loading structure mapping...