ID T2P2_PROHU Reviewed; 157 AA. AC P23657; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 03-MAY-2023, entry version 126. DE RecName: Full=Type II restriction enzyme PvuII {ECO:0000303|PubMed:12654995}; DE Short=R.PvuII; DE EC=3.1.21.4; DE AltName: Full=Endonuclease PvuII; DE AltName: Full=Type-2 restriction enzyme PvuII; GN Name=pvuIIR; OS Proteus hauseri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=183417; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / RC NCTC 4175 / NRRL B-3405; RX PubMed=2243794; DOI=10.1093/nar/18.21.6434; RA Athanasiadis A., Gregoriu M., Thanos D., Kokkinidis M., Papamatheakis J.; RT "Complete nucleotide sequence of the PvuII restriction enzyme gene from RT Proteus vulgaris."; RL Nucleic Acids Res. 18:6434-6434(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). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT, AND DNA-BINDING. RX PubMed=8076590; DOI=10.1002/j.1460-2075.1994.tb06708.x; RA Cheng X., Balendiran K., Schildkraut I., Anderson J.E.; RT "Structure of PvuII endonuclease with cognate DNA."; RL EMBO J. 13:3927-3935(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=7664066; DOI=10.1038/nsb0794-469; RA Athanasiadis A., Vlassi M., Kotsifaki D., Tucker P.A., Wilson K.S., RA Kokkinidis M.; RT "Crystal structure of PvuII endonuclease reveals extensive structural RT homologies to EcoRV."; RL Nat. Struct. Biol. 1:469-475(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS). RX PubMed=9628337; DOI=10.1515/bchm.1998.379.4-5.451; RA Horton J.R., Bonventre J., Cheng X.; RT "How is modification of the DNA substrate recognized by the PvuII RT restriction endonuclease?"; RL Biol. Chem. 379:451-458(1998). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS). RX PubMed=9878366; DOI=10.1006/jmbi.1998.2269; RA Horton J.R., Nastri H.G., Riggs P.D., Cheng X.; RT "Asp34 of PvuII endonuclease is directly involved in DNA minor groove RT recognition and indirectly involved in catalysis."; RL J. Mol. Biol. 284:1491-1504(1998). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-CAGCTG-3' and cleaves after G-3. CC {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 Note=Binds 2 magnesium ions per subunit.; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8076590}. 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; X52681; CAA36904.1; -; Genomic_DNA. DR EMBL; AF305615; AAA96334.1; -; Genomic_DNA. DR PIR; S12163; S12163. DR RefSeq; WP_010904455.1; NZ_PGWU01000024.1. DR PDB; 1EYU; X-ray; 1.78 A; A/B=1-157. DR PDB; 1F0O; X-ray; 2.50 A; A/B=1-157. DR PDB; 1H56; X-ray; 3.00 A; A/B=2-157. DR PDB; 1K0Z; X-ray; 2.05 A; A/B=2-157. DR PDB; 1NI0; X-ray; 2.50 A; A/B/C=1-157. DR PDB; 1PVI; X-ray; 2.60 A; A/B=1-157. DR PDB; 1PVU; X-ray; 2.40 A; A/B=2-157. DR PDB; 2PVI; X-ray; 1.76 A; A/B=1-157. DR PDB; 3KSK; X-ray; 2.35 A; A/B=2-157. DR PDB; 3PVI; X-ray; 1.59 A; A/B=1-157. DR PDBsum; 1EYU; -. DR PDBsum; 1F0O; -. DR PDBsum; 1H56; -. DR PDBsum; 1K0Z; -. DR PDBsum; 1NI0; -. DR PDBsum; 1PVI; -. DR PDBsum; 1PVU; -. DR PDBsum; 2PVI; -. DR PDBsum; 3KSK; -. DR PDBsum; 3PVI; -. DR AlphaFoldDB; P23657; -. DR SMR; P23657; -. DR OrthoDB; 9814553at2; -. DR BRENDA; 3.1.21.4; 14542. DR EvolutionaryTrace; P23657; -. DR PRO; PR:P23657; -. 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; cd22351; PvuII-like; 1. DR Gene3D; 3.40.210.10; PVUII Endonuclease, subunit A; 1. DR InterPro; IPR038402; PvuII_sf. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR015306; Restrct_endonuc_II_PvuII. DR Pfam; PF09225; Endonuc-PvuII; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Restriction system. FT CHAIN 1..157 FT /note="Type II restriction enzyme PvuII" FT /id="PRO_0000077356" FT BINDING 58 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 58 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT HELIX 6..25 FT /evidence="ECO:0007829|PDB:3PVI" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:1PVU" FT HELIX 36..46 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:3KSK" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:3PVI" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1PVU" FT HELIX 88..95 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:3PVI" FT HELIX 117..133 FT /evidence="ECO:0007829|PDB:3PVI" FT HELIX 146..152 FT /evidence="ECO:0007829|PDB:3PVI" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:3PVI" SQ SEQUENCE 157 AA; 18345 MW; 2146453E04E65570 CRC64; MSHPDLNKLL ELWPHIQEYQ DLALKHGIND IFQDNGGKLL QVLLITGLTV LPGREGNDAV DNAGQEYELK SINIDLTKGF STHHHMNPVI IAKYRQVPWI FAIYRGIAIE AIYRLEPKDL EFYYDKWERK WYSDGHKDIN NPKIPVKYVM EHGTKIY //