ID T2PS_PROST Reviewed; 326 AA. AC P00640; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 03-MAY-2023, entry version 88. DE RecName: Full=Type II restriction enzyme PstI {ECO:0000303|PubMed:12654995}; DE Short=R.PstI; DE EC=3.1.21.4; DE AltName: Full=Endonuclease PstI; DE AltName: Full=Type-2 restriction enzyme PstI; GN Name=pstIR; OS Providencia stuartii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Providencia. OX NCBI_TaxID=588; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, AND RP SUBUNIT. RC STRAIN=164; RX PubMed=6330092; DOI=10.1016/s0021-9258(17)42896-1; RA Walder R.Y., Walder J.A., Donelson J.E.; RT "The organization and complete nucleotide sequence of the PstI restriction- RT modification system."; RL J. Biol. Chem. 259:8015-8026(1984). 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'-CTGCAG-3' and cleaves after A-5. CC {ECO:0000269|PubMed:6330092, 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:6330092}. CC -!- SIMILARITY: Belongs to the BsuBI/PstI type II restriction endonuclease CC family. {ECO:0000305}. 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; K02081; AAA25673.1; -; Genomic_DNA. DR PIR; A00783; NDOFS. DR AlphaFoldDB; P00640; -. DR SMR; P00640; -. DR BindingDB; P00640; -. DR ChEMBL; CHEMBL5713; -. DR BRENDA; 3.1.21.4; 5058. DR PRO; PR:P00640; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion 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:UniProtKB-KW. DR Gene3D; 3.40.1350.80; -; 1. DR Gene3D; 1.10.10.1820; BsuBI/PstI restriction endonuclease-like; 1. DR InterPro; IPR041963; BsuBI/PstI_C_sf. DR InterPro; IPR041454; BsuBI/PstI_N. DR InterPro; IPR041962; BsuBI/PstI_N_sf. DR InterPro; IPR009528; Restrct_endonuc_II_BsuBI_C. DR Pfam; PF06616; BsuBI_PstI_RE; 1. DR Pfam; PF17728; BsuBI_PstI_RE_N; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease; KW Restriction system. FT CHAIN 1..326 FT /note="Type II restriction enzyme PstI" FT /id="PRO_0000077354" SQ SEQUENCE 326 AA; 37414 MW; 475841183B414504 CRC64; MKELKLKEAK EILKALGLPP QQYNDRSGWV LLALANIKPE DSWKEAKAPL LPTVSIMEFI RTEYGKDYKP NSRETIRRQT LHQFEQARIV DRNRDLPSRA TNSKDNNYSL NQVIIDILHN YPNGNWKELI QQFLTHVPSL QELYERALAR DRIPIKLLDG TQISLSPGEH NQLHADIVHE FCPRFVGDMG KILYIGDTAS SRNEGGKLMV LDSEYLKKLG VPPMSHDKLP DVVVYDEKRK WLFLIEAVTS HGPISPKRWL ELEAALSSCT VGKVYVTAFP TRTEFRKNAA NIAWETEVWI ADNPDHMVHF NGDRFLGPHD KKPELS //