no 5 other engineered dna binding domains are modular base per base specific nucleic acid binding domains mbbbd pct us2013 051783 said mbbbd can be engineered for instance from the newly identified proteins namely eav36_burrh e5aw43_burrh e5aw45_burrh and e5aw46_burrh proteins from the recently sequenced genome of the endosymbiont fungi burkholderia rhizoxinica lackner moebius et al 2011 mbbbd proteins comprise modules of about 31 to 33 amino acids that are base specific these modules display less than 40 sequence identity with xanthomonas tale common repeats whereas they present more polypeptides sequence variability when they are assembled together these modular polypeptides can although target specific nucleic acid sequences in a quite similar fashion as xanthomonas tal nucleases according to a preferred embodiment of the present invention said dna binding domain is an engineered mbbbd binding domain comprising between 10 and 30 modules preferably between 16 and 20 modules the different domains from the above proteins modules n and c terminals from burkholderia and xanthomonas are useful to engineer new proteins or scaffolds having binding properties to specific nucleic acid sequences in particular additional n terminal and c terminal domains of engineered mbbbd can be derived from natural tale like avrbs3 pthxo1 avrhah1 ptha tal1c as non limiting examples u201c tale nuclease u201d or u201c mbbbd nuclease u201d refers to engineered proteins resulting from the fusion of a dna binding domain typically derived from transcription activator like effector proteins tale or mbbbd binding domain with an endonuclease catalytic domain such catalytic domain is preferably a nuclease domain and more preferably a domain having endonuclease activity like for instance i tevi cole7 nuca and fok i in a particular embodiment said nuclease is a monomeric tale nuclease or mbbbd nuclease a monomeric nuclease is a nuclease that does not require dimerization.