ID B0KC59_THEP3 Unreviewed; 307 AA. AC B0KC59; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 27-MAR-2024, entry version 65. DE RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080}; DE EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080}; GN OrderedLocusNames=Teth39_1776 {ECO:0000313|EMBL:ABY95413.1}; OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium OS thermohydrosulfuricum). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY95413.1, ECO:0000313|Proteomes:UP000002156}; RN [1] {ECO:0000313|Proteomes:UP000002156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33223 / DSM 2355 / 39E RC {ECO:0000313|Proteomes:UP000002156}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., RA Richardson P.; RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded unmethylated sequence 5'-GATC-3'. CC {ECO:0000256|PIRNR:PIRNR016080}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of DNA to give specific double- CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; CC Evidence={ECO:0000256|PIRNR:PIRNR016080}; CC -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease CC family. {ECO:0000256|PIRNR:PIRNR016080}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000924; ABY95413.1; -; Genomic_DNA. DR RefSeq; WP_003866879.1; NC_010321.1. DR AlphaFoldDB; B0KC59; -. DR STRING; 340099.Teth39_1776; -. DR REBASE; 17232; TpsORF1777P. DR KEGG; tpd:Teth39_1776; -. DR eggNOG; ENOG502Z7V5; Bacteria. DR HOGENOM; CLU_089327_0_0_9; -. DR Proteomes; UP000002156; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-UniRule. DR InterPro; IPR021191; Restrct_endonuc_II_DpnII. DR InterPro; IPR007637; Restrct_endonuc_II_DpnII-like. DR Pfam; PF04556; DpnII; 1. DR PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1. PE 3: Inferred from homology; KW Endonuclease {ECO:0000256|PIRNR:PIRNR016080}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:ABY95413.1}; KW Nuclease {ECO:0000256|PIRNR:PIRNR016080}; KW Reference proteome {ECO:0000313|Proteomes:UP000002156}; KW Restriction system {ECO:0000256|PIRNR:PIRNR016080}. FT DOMAIN 18..301 FT /note="Restriction endonuclease type II DpnII-like" FT /evidence="ECO:0000259|Pfam:PF04556" SQ SEQUENCE 307 AA; 36166 MW; E22C7D277AF85A6E CRC64; MKELYIEFLN VENEESVIEK FHDTLVDTNR SYDFFVDWDK VRKHVEEHKI EFNILNSLIG SNRFDNDLRK ILLNYPRVLP VIPILLAIRD LNFKVIRDFT DKNLDIVNYD FNTRTLTSED IDNIIEFFDK TGLKRFFLEM GTKSVQDYVI GVEVGMDTHA RKNRSGDAME LLLKPIIEDI ATKEKGFERV LFQKNFGYLE TNYGIEVNSS IKNRKADFIL IKDNKKVINI EVNFYSGTGS KPQEIVDSYI ERQNELKNNG FEFIWITDGE GWRGQKNQIH KGFEKIDYLL NLHFVRIGLL EEILCRI //