10.1371/journal.pone.0094166.g002 Taichi E. Takasuka Taichi E. Takasuka Justin F. Acheson Justin F. Acheson Christopher M. Bianchetti Christopher M. Bianchetti Ben M. Prom Ben M. Prom Lai F. Bergeman Lai F. Bergeman Adam J. Book Adam J. Book Cameron R. Currie Cameron R. Currie Brian G. Fox Brian G. Fox Schematics of the domain structure in three variants of SACTE_2347. Public Library of Science 2014 agriculture Biochemistry enzymology Enzyme kinetics enzymes Enzyme structure proteins Recombinant proteins glycobiology proteomics molecular biology Molecular biology techniques Sequencing techniques Sequence analysis Energy and power fuels biofuels chemistry Chemical compounds Organic compounds carbohydrates physics Condensed matter physics Solid state physics crystallography variants 2014-04-07 03:25:00 Figure https://plos.figshare.com/articles/figure/_Schematics_of_the_domain_structure_in_three_variants_of_SACTE_2347_/989468 <p>A, SACTE_2347_FL; B, SACTE_2347_42kDa; C, SACTE_2347_34kDa. Residues 1–41 correspond to the annotated twin arginine translocation peptide. Residue 51 corresponds to the experimentally determined N-terminus in the three variants. The GH5 domain spans residues 63–308, and boundaries of the Fn3 and CBM2 domains are as indicated. The location of C-terminal tryptic-digest polypeptides for each variant is shown (GH5, 34kDa-C, Fn3, 42kDa-C, CBM2; also shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0094166#pone-0094166-t002" target="_blank">Table 2</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0094166#pone.0094166.s001" target="_blank">Figure S1</a>).</p>