ID   B0K397_THEPX            Unreviewed;       307 AA.
AC   B0K397;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN   OrderedLocusNames=Teth514_0459 {ECO:0000313|EMBL:ABY91769.1};
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=399726 {ECO:0000313|EMBL:ABY91769.1, ECO:0000313|Proteomes:UP000002155};
RN   [1] {ECO:0000313|EMBL:ABY91769.1, ECO:0000313|Proteomes:UP000002155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514 {ECO:0000313|EMBL:ABY91769.1,
RC   ECO:0000313|Proteomes:UP000002155};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000923; ABY91769.1; -; Genomic_DNA.
DR   RefSeq; WP_003866879.1; NC_010320.1.
DR   AlphaFoldDB; B0K397; -.
DR   REBASE; 16999; TspX514IP.
DR   KEGG; tex:Teth514_0459; -.
DR   HOGENOM; CLU_089327_0_0_9; -.
DR   Proteomes; UP000002155; 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:ABY91769.1};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT   DOMAIN          18..301
FT                   /note="Restriction endonuclease type II DpnII-like"
FT                   /evidence="ECO:0000259|Pfam:PF04556"
SQ   SEQUENCE   307 AA;  36166 MW;  E22C7D277AF85A6E CRC64;
     MKELYIEFLN VENEESVIEK FHDTLVDTNR SYDFFVDWDK VRKHVEEHKI EFNILNSLIG
     SNRFDNDLRK ILLNYPRVLP VIPILLAIRD LNFKVIRDFT DKNLDIVNYD FNTRTLTSED
     IDNIIEFFDK TGLKRFFLEM GTKSVQDYVI GVEVGMDTHA RKNRSGDAME LLLKPIIEDI
     ATKEKGFERV LFQKNFGYLE TNYGIEVNSS IKNRKADFIL IKDNKKVINI EVNFYSGTGS
     KPQEIVDSYI ERQNELKNNG FEFIWITDGE GWRGQKNQIH KGFEKIDYLL NLHFVRIGLL
     EEILCRI
//