ID   I7J1N6_9BURK            Unreviewed;       293 AA.
AC   I7J1N6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 40.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN   ORFNames=KUM_0834 {ECO:0000313|EMBL:CCG19626.1};
OS   Taylorella asinigenitalis 14/45.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Taylorella.
OX   NCBI_TaxID=1091495 {ECO:0000313|EMBL:CCG19626.1};
RN   [1] {ECO:0000313|EMBL:CCG19626.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=14/45 {ECO:0000313|EMBL:CCG19626.1};
RX   PubMed=22541164; DOI=10.1016/j.vetmic.2012.03.041;
RA   Hauser H., Richter D.C., van Tonder A., Clark L., Preston A.;
RT   "Comparative genomic analyses of the Taylorellae.";
RL   Vet. Microbiol. 159:195-203(2012).
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; HE681424; CCG19626.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7J1N6; -.
DR   REBASE; 51623; Tas14ORF833P.
DR   KEGG; tat:KUM_0834; -.
DR   HOGENOM; CLU_089327_0_0_4; -.
DR   BioCyc; TASI1091495:G13GE-830-MONOMER; -.
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:CCG19626.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016080};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT   DOMAIN          3..289
FT                   /note="Restriction endonuclease type II DpnII-like"
FT                   /evidence="ECO:0000259|Pfam:PF04556"
SQ   SEQUENCE   293 AA;  33772 MW;  4102A7CF20F15BD4 CRC64;
     MRDFDEWFKT LQYGVTDYSY FIDFDKVYEN VEQWKPELHL INSLVGSKNI EEDFIKLVKK
     YPKVLECIPV LLAVRLKRNK NGYSEPIVIY DGGKNIEFDF SAKNFSSEIY LKFMDKTGLF
     ELLSNRIISN VVDYVTGVET GLNSNARKNR SGALMETKVE KILIENGFVE NSTYFKQMSD
     KKISDKWKID LSSITNNGIN PKKFDFVIFT NNKVFAVEVN YYGKSGSKPN ETARSYKFIA
     DASKNIENFQ FVWITDGPGW RSSTSKLMDT FANSDHVYNL KDLESGGVKK IFS
//