ID T2B1_GEOSE Reviewed; 323 AA. AC P70985; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 03-MAY-2023, entry version 99. DE RecName: Full=Type II restriction enzyme BsoBI {ECO:0000303|PubMed:12654995}; DE Short=R.BsoBI; DE EC=3.1.21.4; DE AltName: Full=Endonuclease BsoBI; DE AltName: Full=Type-2 restriction enzyme BsoBI; GN Name=bsoBIR {ECO:0000303|PubMed:8917312}; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17, AND FUNCTION. RC STRAIN=JN209; RX PubMed=8917312; DOI=10.1007/s004380050278; RA Ruan H., Lunnen K.D., Scott M.E., Moran L.S., Slatko B.E., Pelletier J.J., RA Hess E.J., Benner J. II, Wilson G.G., Xu S.-Y.; RT "Cloning and sequence comparison of AvaI and BsoBI restriction-modification RT systems."; RL Mol. Gen. Genet. 252:695-699(1996). RN [2] RP FUNCTION, MUTAGENESIS OF ASP-212 AND ASP-246, AND DNA-BINDING. RC STRAIN=JN209; RX PubMed=9099856; DOI=10.1016/s0378-1119(96)00773-1; RA Ruan H., Lunnen K.D., Pelletier J.J., Xu S.-Y.; RT "Overexpression of BsoBI restriction endonuclease in E. coli, purification RT of the recombinant BsoBI, and identification of catalytic residues of BsoBI RT by random mutagenesis."; RL Gene 188:35-39(1997). RN [3] 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). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT. RX PubMed=11250198; DOI=10.1016/s0969-2126(01)00564-0; RA van der Woerd M.J., Pelletier J.J., Xu S.-Y., Friedman A.M.; RT "Restriction enzyme BsoBI-DNA complex: a tunnel for recognition of RT degenerate DNA sequences and potential histidine catalysis."; RL Structure 9:133-144(2001). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-CYCGRG-3' and cleaves after C-1. CC {ECO:0000269|PubMed:9099856, ECO:0000303|PubMed:12654995, CC ECO:0000305|PubMed:8917312}. 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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11250198}. 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; X98287; CAA66932.1; -; Genomic_DNA. DR PIR; S72473; S72473. DR PDB; 1DC1; X-ray; 1.70 A; A/B=1-323. DR PDBsum; 1DC1; -. DR AlphaFoldDB; P70985; -. DR SMR; P70985; -. DR EvolutionaryTrace; P70985; -. DR PRO; PR:P70985; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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. DR CDD; cd22315; BsoBI-like; 1. DR Gene3D; 3.40.91.10; -; 1. DR Gene3D; 1.10.238.90; Restriction endonuclease BsobI, helical domain; 1. DR InterPro; IPR043091; Restr_endonucII_AvaI/BsoBI_hel. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR015277; Restrct_endonuc_II_AvaI/BsoBI. DR Pfam; PF09194; Endonuc-BsobI; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; DNA-binding; Endonuclease; KW Hydrolase; Magnesium; Metal-binding; Nuclease; Restriction system. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8917312" FT CHAIN 2..323 FT /note="Type II restriction enzyme BsoBI" FT /id="PRO_0000077288" FT BINDING 212 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT SITE 81 FT /note="Interaction with DNA" FT SITE 131 FT /note="Interaction with DNA" FT MUTAGEN 212 FT /note="D->N: Loss of activity, still binds DNA." FT /evidence="ECO:0000269|PubMed:9099856" FT MUTAGEN 246 FT /note="D->N: Loss of activity, still binds DNA." FT /evidence="ECO:0000269|PubMed:9099856" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 14..17 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 21..53 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 59..64 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 69..75 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 88..101 FT /evidence="ECO:0007829|PDB:1DC1" FT TURN 102..106 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 110..152 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 194..204 FT /evidence="ECO:0007829|PDB:1DC1" FT TURN 205..208 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 209..218 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 247..270 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 276..283 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 286..297 FT /evidence="ECO:0007829|PDB:1DC1" FT STRAND 303..306 FT /evidence="ECO:0007829|PDB:1DC1" FT HELIX 310..321 FT /evidence="ECO:0007829|PDB:1DC1" SQ SEQUENCE 323 AA; 36706 MW; C5D71CA25DA95B27 CRC64; MNTQKPFENH LKSVDDLKTT YEEYRAGFIA FALEKNKRST PYIERARALK VAASVAKTPK DLLYLEDIQD ALLYASGISD KAKKFLTEDD KKESINNLIE NFLEPAGEEF IDELIFRYLL FQGDSLGGTM RNIAGALAQQ KLTRAIISAL DIANIPYKWL DSRDKKYTNW MDKPEDDYEL ETFAKGISWT INGKHRTLMY NITVPLVKKN VDICLFNCEP EIYTPQKVHQ QPEKYLLLGE LKGGIDPAGA DEHWKTANTA LTRIRNKFSE KGLSPKTIFI GAAIEHSMAE EIWDQLQSGS LTNSANLTKT EQVGSLCRWI INI //