ID A3CPJ3_STRSV Unreviewed; 308 AA.
AC A3CPJ3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN OrderedLocusNames=SSA_1716 {ECO:0000313|EMBL:ABN45098.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN45098.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN45098.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN45098.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45098.1; -; Genomic_DNA.
DR RefSeq; WP_002905092.1; NC_009009.1.
DR RefSeq; YP_001035648.1; NC_009009.1.
DR AlphaFoldDB; A3CPJ3; -.
DR STRING; 388919.SSA_1716; -.
DR REBASE; 14758; SsaSKORF1717P.
DR KEGG; ssa:SSA_1716; -.
DR PATRIC; fig|388919.9.peg.1625; -.
DR eggNOG; ENOG502Z7V5; Bacteria.
DR HOGENOM; CLU_089327_0_0_9; -.
DR OrthoDB; 9771872at2; -.
DR Proteomes; UP000002148; 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, ECO:0000313|EMBL:ABN45098.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:ABN45098.1};
KW Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT DOMAIN 15..296
FT /note="Restriction endonuclease type II DpnII-like"
FT /evidence="ECO:0000259|Pfam:PF04556"
SQ SEQUENCE 308 AA; 35697 MW; 8DFE125611BFA733 CRC64;
MKFSDFVTLS LDERLQYFLS TLSVTNRTPE YYVNWNKVRR ETKEFELELN TLNYLIGKDN
IYEEAFNLFS KQPDLLRAVP SLIASRDKVL DILSLDEDDN MSFHQLDFKK IDKSDIKVYV
DFIEQAGLLY FLQKEASRSL VDYVYGVEAG LDSNARKNRS GTTMEGILER SVAKVCQQHD
LEFKSQATPS FIKEKWNIEV PVDKSQRRFD VAVYSKEKHK IWLIETNYYG GGGSKLKAVA
GEFTELSQFV VNSPDDVEFV WVTDGLGWKT ARLPLAEAFA HIPYVFNLDM LKHGYLYDLL
MPKKLIRN
//
