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Database: UniProt
Entry: A0A0G1LKL0_9BACT
LinkDB: A0A0G1LKL0_9BACT
Original site: A0A0G1LKL0_9BACT 
ID   A0A0G1LKL0_9BACT        Unreviewed;       285 AA.
AC   A0A0G1LKL0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN   ORFNames=UW97_C0011G0005 {ECO:0000313|EMBL:KKT96451.1};
OS   Parcubacteria group bacterium GW2011_GWA2_45_15.
OC   Bacteria.
OX   NCBI_TaxID=1618833 {ECO:0000313|EMBL:KKT96451.1, ECO:0000313|Proteomes:UP000034700};
RN   [1] {ECO:0000313|EMBL:KKT96451.1, ECO:0000313|Proteomes:UP000034700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKT96451.1}.
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DR   EMBL; LCKK01000011; KKT96451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1LKL0; -.
DR   PATRIC; fig|1618833.3.peg.222; -.
DR   Proteomes; UP000034700; Unassembled WGS sequence.
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};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT   DOMAIN          4..281
FT                   /note="Restriction endonuclease type II DpnII-like"
FT                   /evidence="ECO:0000259|Pfam:PF04556"
SQ   SEQUENCE   285 AA;  32856 MW;  EDD5468CADDFFEE0 CRC64;
     MNKDFNNLIT TFKSSIKTWD YFVNWKKVFS NSSDLEISLN KLNYLLGKDN LEDEFRKLYA
     SNPDIVKALP VLLAVRENKL EVFDKATKNS EFFDFSGKEQ DPEKYLEFLN KSGLARLFQK
     DGVKNLVDYV MGVEVGLDSN GRKNRGGSLM EEIAGAFVSD FCNKNGYEYM AQARATNIKS
     KWGVDIKVDK SERSFDFAVY NPKNKKIKLF EANFYNGGGS KLKAVCGEFR SLYDELKAQD
     IDFIWITDGL GWHTTKRPLE ETYNHNEYVF NLNMLESGVL NELKW
//
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