PROSITE documentation PDOC51658Bifunctional nuclease (BFN) domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | You 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. |
| Title | Novel bifunctional nucleases, OmBBD and AtBBD1, are involved in abscisic acid-mediated callose deposition in Arabidopsis. | |
| Source | Plant Physiol. 152:1015-1029(2010). | |
| PubMed ID | 20018603 | |
| DOI | 10.1104/pp.109.147645 |
| 2 | Authors | Spraggon G. Pantazatos D. Klock H.E. Wilson I.A. Woods V.L. Jr. Lesley S.A. |
| Title | On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171. | |
| Source | Protein Sci. 13:3187-3199(2004). | |
| PubMed ID | 15557262 | |
| DOI | 10.1110/ps.04939904 |
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