Summary
Peptidase clan CD
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 9 families and the total number of domains in the clan is 45615. The clan was built by RD Finn.
Literature references
- 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. PUBMED:9891971 EPMC:9891971
Members
This clan contains the following 9 member families:
CHAT DUF4347 Peptidase_C11 Peptidase_C13 Peptidase_C14 Peptidase_C25 Peptidase_C50 Peptidase_C80 Raptor_NExternal database links
MEROPS: | CD |
SCOP: | 52129 |
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) | 20750 (45.5%) | View |
CHAT (PF12770) | 12007 (26.3%) | View |
Peptidase_C13 (PF01650) | 4980 (10.9%) | View |
Raptor_N (PF14538) | 2263 (5.0%) | View |
Peptidase_C50 (PF03568) | 2075 (4.5%) | View |
DUF4347 (PF14252) | 1320 (2.9%) | View |
Peptidase_C25 (PF01364) | 1270 (2.8%) | View |
Peptidase_C11 (PF03415) | 738 (1.6%) | View |
Peptidase_C80 (PF11713) | 212 (0.5%) | View |
Total: 9 | Total: 45615 | 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
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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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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