ID   B1I859_STRPI            Unreviewed;       288 AA.
AC   B1I859;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN   OrderedLocusNames=SPH_1964 {ECO:0000313|EMBL:ACA36447.1};
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214 {ECO:0000313|EMBL:ACA36447.1, ECO:0000313|Proteomes:UP000002163};
RN   [1] {ECO:0000313|Proteomes:UP000002163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6 {ECO:0000313|Proteomes:UP000002163};
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded unmethylated sequence 5'-GATC-3'.
CC       {ECO:0000256|PIRNR:PIRNR016080}.
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:0000256|PIRNR:PIRNR016080};
CC   -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease
CC       family. {ECO:0000256|PIRNR:PIRNR016080}.
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DR   EMBL; CP000936; ACA36447.1; -; Genomic_DNA.
DR   RefSeq; WP_000815111.1; NC_010380.1.
DR   AlphaFoldDB; B1I859; -.
DR   REBASE; 17280; SpnH19ORF1965P.
DR   GeneID; 66806922; -.
DR   KEGG; spv:SPH_1964; -.
DR   HOGENOM; CLU_089327_0_0_9; -.
DR   Proteomes; UP000002163; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:ACA36447.1};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT   DOMAIN          6..285
FT                   /note="Restriction endonuclease type II DpnII-like"
FT                   /evidence="ECO:0000259|Pfam:PF04556"
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
//