T2D2_STREE
ID T2D2_STREE Reviewed; 288 AA.
AC P09357;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Type II restriction enzyme DpnII {ECO:0000303|PubMed:12654995};
DE Short=R.DpnII;
DE EC=3.1.21.4 {ECO:0000269|PubMed:2824782};
DE AltName: Full=Endonuclease DpnII;
DE AltName: Full=Type-2 restriction enzyme DpnII;
GN Name=dpnB {ECO:0000303|PubMed:3019562};
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3019562; DOI=10.1016/0092-8674(86)90698-7;
RA Lacks S.A., Mannarelli B.M., Springhorn S.S., Greenberg B.;
RT "Genetic basis of the complementary DpnI and DpnII restriction systems of
RT S. pneumoniae: an intercellular cassette mechanism.";
RL Cell 46:993-1000(1986).
RN [2]
RP PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=2824782; DOI=10.1016/0022-2836(87)90024-6;
RA de la Campa A.G., Purushottam K., Springhorn S.S., Lacks S.A.;
RT "Proteins encoded by the DpnII restriction gene cassette. Two methylases
RT and an endonuclease.";
RL J. Mol. Biol. 196:457-469(1987).
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).
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded unmethylated sequence 5'-GATC-3' and cleaves before G-1.
CC {ECO:0000269|PubMed:2824782, 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 Evidence={ECO:0000269|PubMed:2824782};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:2824782}.
CC -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease
CC family. {ECO:0000305}.
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DR EMBL; M14339; AAA88582.1; -; Genomic_DNA.
DR PIR; B24372; B24372.
DR RefSeq; WP_000815111.1; NZ_WNIC01000007.1.
DR AlphaFoldDB; P09357; -.
DR REBASE; 777; DpnII.
DR GeneID; 66806922; -.
DR OMA; GLEQIFC; -.
DR PRO; PR:P09357; -.
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:UniProtKB-KW.
DR InterPro; IPR021191; Restrct_endonuc_II_DpnII.
DR InterPro; IPR007637; Restrct_endonuc_II_DpnII-like.
DR Pfam; PF04556; DpnII; 1.
DR PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW Restriction system.
FT CHAIN 1..288
FT /note="Type II restriction enzyme DpnII"
FT /id="PRO_0000077302"
SQ SEQUENCE 288 AA; 33585 MW; F7346EEA6940EB33 CRC64;
MKQTRNFDEW LSTMTDTVAD WTYYTDFPKV YKNVSSIKVA LNIMNSLIGS KNIQEDFLDL
YQNYPEILKV VPLLIAKRLR DTIIVKDPIK DFYFDFSKRN YSIEEYTMFL EKSGIFDLLQ
NHLVSNLVDY VTGVEVGMDT NGRKNRTGDA MENIVQSYLE AEGYILGENL FKEIEQNEIE
EIFSVDLSAI TNDGNTVKRF DFVIKNEQVL YLIEVNFYSG SGSKLNETAR SYKMIAEETK
AIPNVEFMWI TDGQGWYKAK NNLRETFDIL PFLYNINDLE HNILKNLK