A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of 1200 genomes originated from a Actinobacteria strain collection isolated from Trondheim fjord. Instead of the conserved GXXDG motif known for Dyp-type peroxidases, the enzyme contains a new conserved motif EXXDG which has been not reported before. The enzyme can oxidize an anthraquinone dye Remazol Brilliant Blue R (Reactive Blue 19) and other phenolic compounds such as ferulic acid, sinapic acid, caffeic acid, 3-methylcatechol, dopamine hydrochloride, and tannic acid. The acidic pH optimum (3 to 4) and the low temperature optimum (25 °C) were confirmed using both biochemical and electrochemical assays. Kinetic and thermodynamic parameters associated with the catalytic redox center were attained by electrochemistry. A novel dye-decolorizing peroxidase (Dyp) was discovered by data mining from Actinobacteria strain collection from Trondheim fjord, containing a new motif EXXDG. The biochemical characterization was performed. The best catalytic conditions found at pH 3 to 4; not thermostable. Electrochemical behavior in agreement with the biochemical characterization. Display omitted •A novel dye-decolorizing peroxidase (Dyp) found by data mining from Actinobacteria genome•The new Dyp seems to belong to type B and bears a new-found conserved motif EXXDG•Biochemical and electrochemical characterizations were performed•The new Dyp can oxidize anthraquinone dye and other phenolic substrates•The pH optimum was found in the acidic range (pH 3 to 4)