ID T2BR_BACIU Reviewed; 576 AA. AC P06529; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 03-MAY-2023, entry version 75. DE RecName: Full=Type II restriction enzyme BsuRI {ECO:0000303|PubMed:12654995}; DE Short=R.BsuRI; DE EC=3.1.21.4 {ECO:0000305|PubMed:2997708}; DE AltName: Full=Endonuclease BsuRI; DE AltName: Full=Type-2 restriction enzyme BsuRI; GN Name=hsdRR; Synonyms=hsrR; OS Bacillus subtilis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=R; RX PubMed=2997708; DOI=10.1093/nar/13.18.6403; RA Kiss A., Posfai G., Keller C.C., Venetianer P., Roberts R.J.; RT "Nucleotide sequence of the BsuRI restriction-modification system."; RL Nucleic Acids Res. 13:6403-6421(1985). RN [2] RP NOMENCLATURE, AND SUBTYPE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-GGCC-3' and cleaves after G-2. CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2997708}. 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:0000305|PubMed:2997708}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Monomer. 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; X02988; CAA26730.1; -; Genomic_DNA. DR PIR; A23488; NDBSR1. DR AlphaFoldDB; P06529; -. DR REBASE; 11067; V.BsuRIP. DR REBASE; 620; BsuRI. DR PRO; PR:P06529; -. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. PE 4: Predicted; KW Endonuclease; Hydrolase; Magnesium; Nuclease; Restriction system. FT CHAIN 1..576 FT /note="Type II restriction enzyme BsuRI" FT /id="PRO_0000077292" SQ SEQUENCE 576 AA; 66304 MW; 054D1182E510E12F CRC64; MGKNSKAIGN NHVKSVYQAL LQSLKSKSVN GFSKITIETI SFIKNLYPEI DSVTSKFDNS RPDQSKDLTL YLKSGETISL NLFLIKKGRR IQPKNAGAKS FLEKYFLSAE MQKIFNKEFE RYYLDYLKEV VEHKKGTHYI TDKRELKRLV SSHFPKFTEE INLYRDKFLF NLRETCFTLL QQFYNEKNIG FTHAFNVFFM VNDTNIITSY GKDENDVKVE KFAPASPSLK DIELYKTGKS TVGIKFGEVG LTLRFKFESD PWKSIKLATG YHEFPKEKER VNVNLKTMRR MEKLLNKHEY AKTSNNSNAI GKCHEAWTYY YFLKAFPDVI QVDPKQCVEL INTYFSSINQ NTLKKLYSST STIVDAITEK LRQKYHDYII ESIELIPDAY IKDRLDTGDL QLVLKVNNNI IVENISLKAL AKRNSKITTK NPGMGSILGP TYFNMGSMES VINEVKNKFT IGEFNHRKSL EILSYEFGMK LDSATQEQLR RGIHNLLGKA MIAITIYGEG ISFCKEPSEI DGEVKVHVNV PSAIQNTLTW NNELESISLR AKFSKSQKHG WSSIKLTSEC QLESRK //