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353  structures 5373  species 39  interactions 52666  sequences 265  architectures

Clan: Peptidase_ME (CL0094)

Summary

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 7 families and the total number of domains in the clan is 52666. 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

Members

This clan contains the following 7 member families:

LuxS M16C_assoc Peptidase_M16 Peptidase_M16_C Peptidase_M16_M Peptidase_M44 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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Alignments

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) 19884 (37.8%) View
Peptidase_M16 (PF00675) 15545 (29.5%) View
tRNA_SAD (PF07973) 12565 (23.9%) View
Peptidase_M16_M (PF16187) 2076 (3.9%) View
M16C_assoc (PF08367) 1373 (2.6%) View
LuxS (PF02664) 1212 (2.3%) View
Peptidase_M44 (PF03410) 11 (0.0%) View
Total: 7 Total: 52666 Clan alignment
 

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Family relationships

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

Species distribution

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

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Interactions

Structures

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.

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