ID T2S9_STAAU Reviewed; 261 AA. AC P23736; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 02-SEP-2026, entry version 80. DE RecName: Full=Type II restriction enzyme Sau96I {ECO:0000303|PubMed:12654995}; DE Short=R.Sau96I; DE EC=3.1.21.4; DE AltName: Full=Endonuclease Sau96I; DE AltName: Full=Type-2 restriction enzyme Sau96I; GN Name=sau96IR {ECO:0000303|PubMed:2204026}; OS Staphylococcus aureus. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT. RC STRAIN=PS96; RX PubMed=2204026; DOI=10.1093/nar/18.16.4659; RA Szilak L., Venetianer P., Kiss A.; RT "Cloning and nucleotide sequence of the genes coding for the Sau96I RT restriction and modification enzymes."; RL Nucleic Acids Res. 18:4659-4664(1990). 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'-GGNCC-3' and cleaves after G-1. CC {ECO:0000269|PubMed:2204026, ECO:0000303|PubMed:12654995}. 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: Monomer. {ECO:0000305|PubMed:2204026}. 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; X53096; CAA37259.1; -; Genomic_DNA. DR PIR; S12706; S12706. DR RefSeq; WP_000182778.1; NZ_BDXL01000002.1. DR AlphaFoldDB; P23736; -. DR REBASE; 1607; Sau96I. DR PATRIC; fig|1280.3540.peg.2443; -. DR BRENDA; 3.1.21.4; 3352. DR PRO; PR:P23736; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR InterPro; IPR019057; Restrct_endonuc_II_Eco47II. DR Pfam; PF09553; RE_Eco47II; 1. PE 1: Evidence at protein level; KW Endonuclease; Hydrolase; Nuclease; Restriction system. FT CHAIN 1..261 FT /note="Type II restriction enzyme Sau96I" FT /id="PRO_0000077359" SQ SEQUENCE 261 AA; 30486 MW; 75338416FCD54677 CRC64; MTNKYLSFIT DEDLFECIEF LYTEYEKALE GIDFDKFFKN RIDTFKMTFD MGINNLSEQD WLAAELQRQV EKTITNHVGT FHEKLIGKIE GYTNYPVGYD YDVAKDDNTL FAEIKNKHNT LTGTHTKSLF QKICGYAEKY PDAICYYVRI IDTKSRNDIW EFRSGSIDEN TREKPRFSHP RVRIASGDQF YKIVTGEEDA FKQLAYNIPI ALDDWIETKR AKKGSSLGLF AELYQQAKAN NRTLSEEIIS INYPKSNYIS F //