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45  structures 945  species 5  interactions 62472  sequences 1517  architectures

Clan: beta_Roll (CL0592)

Summary

beta-strand roll of R-module, superfamily Add an annotation

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 62472. The clan was built by P Coggill.

Literature references

  1. 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_C

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
HemolysinCabind (PF00353) 61817 (99.0%) View
Peptidase_M10_C (PF08548) 655 (1.0%) View
Total: 2 Total: 62472 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 5 interactions for this clan. More...

Interacting families
A B
HemolysinCabind HemolysinCabind
Peptidase_M10 Peptidase_M10_C
Peptidase_M10_C HemolysinCabind
Inh
Reprolysin_2 Peptidase_M10_C

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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