T2P2_PROHU
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-AUG-2022, entry version 123.
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; Proteobacteria; 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 / NCTC
RC 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}.
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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 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 Gene3D; 3.40.210.10; -; 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; SSF52980; 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
