Summary
beta-strand roll of R-module, superfamily
This superfamily is characterised by families of a short nonarepeat unit. The beta-roll is made up of a super-helix of beta-strand-turns of two short strands each, and the loops are stabilised by Ca2+ ions. The region of a protein with this beta-roll is often termed the R-module, and it can frequently be found in metalloproteases of the serralysin type and in epimerases [1]. The nonarepeat is also found multiple times in haemolysins, where the structure is again stabilised by binding Ca2+ ions.
This clan contains 2 families and the total number of domains in the clan is 129323. The clan was built by P Coggill.
Literature references
- Aachmann FL, Svanem BI, Guntert P, Petersen SB, Valla S, Wimmer R;, J Biol Chem. 2006;281:7350-7356.: NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase. PUBMED:16407237 EPMC:16407237
Members
This clan contains the following 2 member families:
HemolysinCabind Peptidase_M10_CExternal database links
SCOP: | 51120 |
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 |
---|---|---|
HemolysinCabind (PF00353) | 127693 (98.7%) | View |
Peptidase_M10_C (PF08548) | 1630 (1.3%) | View |
Total: 2 | Total: 129323 | 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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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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