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PROSITE documentation PDOC51658

Bifunctional nuclease (BFN) domain profile





Description

The bifunctional nuclease (BFN) domain is specific to bacteria and plant organisms. It has both RNase and DNase activities [1].

The dimer of the BFN domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an eight-stranded, distorted β-sheet consisting of a four-stranded, antiparallel β-sheet (B1, B2, B3, B8), and a four-stranded mixed β-sheet (B4, B5, B6, B7). The sheets are intercalated by three short α-helices (H1, H3, H4), while a longer α-helix (H2) forms the central core of the dimer interface [2].

Some proteins known to contain a BFN domain are listed below:

  • Thermotoga maritima TM0160, a conserved hypothetical protein.
  • Plant bifunctional nuclease in basal defense response (BBD) proteins, regulators in abscisic acid (ABA)-mediated defense responses.

The profile we developed covers the entire BFN domain.

Last update:

October 2012 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

BFN, PS51658; Bifunctional nuclease (BFN) domain profile  (MATRIX)


References

1AuthorsYou M.K. Shin H.Y. Kim Y.J. Ok S.H. Cho S.K. Jeung J.U. Yoo S.D. Kim J.K. Shin J.S.
TitleNovel bifunctional nucleases, OmBBD and AtBBD1, are involved in abscisic acid-mediated callose deposition in Arabidopsis.
SourcePlant Physiol. 152:1015-1029(2010).
PubMed ID20018603
DOI10.1104/pp.109.147645

2AuthorsSpraggon G. Pantazatos D. Klock H.E. Wilson I.A. Woods V.L. Jr. Lesley S.A.
TitleOn the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.
SourceProtein Sci. 13:3187-3199(2004).
PubMed ID15557262
DOI10.1110/ps.04939904



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