ID   K0NH64_DESTT            Unreviewed;       922 AA.
AC   K0NH64;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   OrderedLocusNames=TOL2_C01770 {ECO:0000313|EMBL:CCK78347.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK78347.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK78347.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC         fragments with terminal 5'-phosphates, ATP is simultaneously
CC         hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC   -!- SIMILARITY: Belongs to the HsdR family.
CC       {ECO:0000256|ARBA:ARBA00008598}.
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DR   EMBL; FO203503; CCK78347.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0NH64; -.
DR   STRING; 651182.TOL2_C01770; -.
DR   REBASE; 53430; DtoTol2ORF1790P.
DR   KEGG; dto:TOL2_C01770; -.
DR   PATRIC; fig|651182.5.peg.221; -.
DR   HOGENOM; CLU_009326_0_0_7; -.
DR   Proteomes; UP000007347; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   CDD; cd18799; SF2_C_EcoAI-like; 1.
DR   Gene3D; 3.90.1570.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013670; EcoEI_R_C_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF08463; EcoEI_R_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:CCK78347.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          162..318
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   922 AA;  105929 MW;  58E301808B5B974B CRC64;
     MIDRELAQSG WNVNDPTQVI EEFDILTSAP DGVAESVSNY GNHQFSDYVL LGKNGKPLAV
     VEAKSTSKDA AIGREQAKQY CYNIQIQIGG KLPFCFYTNG HEIFFWDLEN YPPRRVMGFP
     TREDLERFQY IRHNKKPLTH EFINKDIAGR DYQIRAIRSV LEAIEAKKRD FLLVMATGTG
     KTRTCIAVAD VLMRTSHVER VLFLVDRIAL REQALSAFKE HLPNEPRWPN VGEKLIAGDR
     RIYVSTYPTM LNILRENDRK LSPHFFDLIV VDESHRSIYN TFGEILDYFK TMTLGLTATP
     TDIIDHNTFK LFHCEDGLPT FAYTFEEAVN NVPPYLCSFQ VMKIQTRFQM EGISKRTISL
     EDQKRLILEG KEIEEINFEG TQLEKQVVNK GTNILIVKEF MDECIKDHNG VLPGKTIFFC
     SSKAHARRIE TIFDQLYPQY KGELAKVLVS DDPRVYGKGG LLDQFTNNDM PRIAISVDML
     DTGIDIRELV NLVFTKPVYS YTKFWQMIGR GTRLLEPKKI KPWCTQKDVF LIIDCWDNFE
     YFKLNPKGKE LTPQVPLPVK LVGLRIDKIE TALTKNKPDI VLREAGKLKE QIRLLPQTSV
     VIKEAAALLS DVGKASFWDT LTHEKLHWLR IHIKPLFKTF SDADFKAMRF ERDLLEYTLA
     VLNEETIKAE TLKTGIVEQI SELPLSVPFV KLEESLIRSA QGNHYWRSIS DHDLDSLCDK
     LGPLMKFCEQ EDPGANQVHL NLADKLHNKE MVEFGPQHEA VSISRYRDMV EALIMELTSS
     HPILQKLQNG KDVTAQEAQA LAEQLHSEHP HITERLLRQV YKNKKARFIQ FIRHILGLEV
     LKSFPESVSE AFEQFIQQHT TLSSRQLAFL NLLKEVVIER EAIEKKDLIH APFTVIHPQG
     IRGVFSPAEI KEILSLTQRL VA
//