ID   B5Y630_COPPD            Unreviewed;       310 AA.
AC   B5Y630;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN   Name=hsdR {ECO:0000313|EMBL:ACI17600.1};
GN   OrderedLocusNames=COPRO5265_1446 {ECO:0000313|EMBL:ACI17600.1};
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS   BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC   Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI17600.1, ECO:0000313|Proteomes:UP000001732};
RN   [1] {ECO:0000313|Proteomes:UP000001732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC   {ECO:0000313|Proteomes:UP000001732};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus strain
RT   ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI17600.1, ECO:0000313|Proteomes:UP000001732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC   {ECO:0000313|Proteomes:UP000001732};
RX   PubMed=24831154;
RA   Alexiev A., Coil D.A., Badger J.H., Enticknap J., Ward N., Robb F.T.,
RA   Eisen J.A.;
RT   "Complete Genome Sequence of Coprothermobacter proteolyticus DSM 5265.";
RL   Genome Announc. 2:e00470-14(2014).
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; CP001145; ACI17600.1; -; Genomic_DNA.
DR   RefSeq; WP_012544252.1; NC_011295.1.
DR   AlphaFoldDB; B5Y630; -.
DR   STRING; 309798.COPRO5265_1446; -.
DR   REBASE; 18906; Cpr5265ORF1447P.
DR   KEGG; cpo:COPRO5265_1446; -.
DR   eggNOG; ENOG502Z7V5; Bacteria.
DR   HOGENOM; CLU_089327_0_0_9; -.
DR   OrthoDB; 9771872at2; -.
DR   Proteomes; UP000001732; 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};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001732};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT   DOMAIN          20..303
FT                   /note="Restriction endonuclease type II DpnII-like"
FT                   /evidence="ECO:0000259|Pfam:PF04556"
SQ   SEQUENCE   310 AA;  35679 MW;  BA5EA283488D44EA CRC64;
     MKYSNLFYKL ISCKDEDDVF EYLIRNLKET IISWDFFVAW EKVINKVEDI EISLNLLNYL
     VGKENITEKF AELVSKYPEV IDVLPVLVAW RAKNVKVLDP LDDNIFNYKE YSFEKKSSYT
     TEEIASLTEF ADKTGLLAMF KNENIKSVVD YVTGVEVGLD TNARKNRSGA AMEMITELLI
     KRICAKNRYN YISQATAHKI NELFGYEVKV DKSERSFDFA IDNGDKLYLV ETNYYGGGGS
     KLKAVAGEFV TLCRFLKRET PQHTFIWITD GLGWKTAKKP LREAFDEVDY ILNLSMLENG
     VLENIILEGL
//