291  structures 509  species 2  interactions 2664  sequences 220  architectures

Clan: Peptidase_CD (CL0093)

Summary

Peptidase clan CD Add an annotation

The members of this clan are all endopeptidase that have the catalytic dyad histidine followed by cysteine. The catalytic histidine is preceded by a block of hydrophobic residues and a glycine, where as the cysteine is preceded by a block of hydrophobic residues and a glutamine and an alanine. The members with a know structure adopt an alpha/beta fold [1].

This clan contains 6 families and the total number of domains in the clan is 2664.

Literature references

  1. Chen JM, Rawlings ND, Stevens RA, Barrett AJ; , FEBS Lett 1998;441:361-365.: Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. 9891971

Members

This clan contains the following 6 member families:

Peptidase_C11 Peptidase_C13 Peptidase_C14 Peptidase_C25 Peptidase_C50 Peptidase_C80

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_C14 (PF00656) 1689 (63.4%) View
Peptidase_C13 (PF01650) 445 (16.7%) View
Peptidase_C50 (PF03568) 174 (6.5%) View
Peptidase_C11 (PF03415) 145 (5.4%) View
Peptidase_C80 (PF11713) 141 (5.3%) View
Peptidase_C25 (PF01364) 70 (2.6%) View
Total: 6 Total: 2664 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

There are 2 interactions for this clan. More...

Interacting families
A B
Peptidase_C14 BIR
Peptidase_C14

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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