{PDOC51658}
{PS51658; BFN}
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* Bifunctional nuclease (BFN) domain profile *
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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
beta-sheet consisting of a four-stranded, antiparallel beta-sheet (B1, B2, B3,
B8), and  a  four-stranded  mixed  beta-sheet (B4, B5, B6, B7). The sheets are
intercalated by  three short alpha-helices (H1, H3, H4), while a longer alpha-
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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2012 / First entry.

[ 1] 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.
     "Novel bifunctional nucleases, OmBBD and AtBBD1, are involved in
     abscisic acid-mediated callose deposition in Arabidopsis."
     Plant Physiol. 152:1015-1029(2010).
     PubMed=20018603; DOI=10.1104/pp.109.147645
[ 2] Spraggon G., Pantazatos D., Klock H.E., Wilson I.A., Woods V.L. Jr.,
     Lesley S.A.
     "On the use of DXMS to produce more crystallizable proteins:
     structures of the T.  maritima proteins TM0160 and TM1171."
     Protein Sci. 13:3187-3199(2004).
     PubMed=15557262; DOI=10.1110/ps.04939904

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