ID E4TDW4_RIEAD Unreviewed; 279 AA. AC E4TDW4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 24-JAN-2024, entry version 56. DE RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080}; DE EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080}; GN ORFNames=RA0C_0017 {ECO:0000313|EMBL:AFD55042.1}; OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / OS NCTC 11014). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Riemerella. OX NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD55042.1, ECO:0000313|Proteomes:UP000010093}; RN [1] {ECO:0000313|EMBL:AFD55042.1, ECO:0000313|Proteomes:UP000010093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093}; RX PubMed=22628503; DOI=10.1128/JB.00366-12; RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q., RA Liu F., Wang Y., Chen X.Y.; RT "Complete genome sequence of Riemerella anatipestifer reference strain."; RL J. Bacteriol. 194:3270-3271(2012). 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; CP003388; AFD55042.1; -; Genomic_DNA. DR RefSeq; WP_004920743.1; NC_017045.1. DR AlphaFoldDB; E4TDW4; -. DR REBASE; 46596; Ran15868CORF16P. DR REBASE; 46862; Ran15868ORF1817P. DR GeneID; 66849472; -. DR KEGG; rai:RA0C_0017; -. DR KEGG; ran:Riean_1818; -. DR PATRIC; fig|693978.17.peg.18; -. DR HOGENOM; CLU_089327_0_0_10; -. DR Proteomes; UP000010093; 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; IPR011335; Restrct_endonuc-II-like. 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. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. PE 3: Inferred from homology; KW Endonuclease {ECO:0000256|PIRNR:PIRNR016080}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR016080}; KW Nuclease {ECO:0000256|PIRNR:PIRNR016080}; KW Restriction system {ECO:0000256|PIRNR:PIRNR016080}. FT DOMAIN 4..269 FT /note="Restriction endonuclease type II DpnII-like" FT /evidence="ECO:0000259|Pfam:PF04556" SQ SEQUENCE 279 AA; 32137 MW; D1D54513F1E774BE CRC64; MSEQFKIFLS QLSETNATLD YFADFKKIRN NVNKIAIKLN QLNYLIGKEN LKEAVIELYE ENSKVFEVLD ILIAIRKNKN AKTFNNKGEI VLLDTYFTSP ELILEYIEET GLAEVFRNKD VTNLVDYVFG IEVGLDTNAR KNRGGDNMSK AVSLIFDKAG VFYKKEVNNT IFPEIISLGA DVKRFDFVIK TKKKTYLIET NYYNSGGSKL NETARSYSDV APKINLYEGY EFVWITDGQG WFSAKNKLEE AYNIIPSLYN LITLEDFIKK IQEETVIEF //