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Database: UniProt
Entry: A0A0G0CB37_9BACT
LinkDB: A0A0G0CB37_9BACT
Original site: A0A0G0CB37_9BACT 
ID   A0A0G0CB37_9BACT        Unreviewed;       854 AA.
AC   A0A0G0CB37;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=UR68_C0005G0035 {ECO:0000313|EMBL:KKP73301.1};
OS   Candidatus Roizmanbacteria bacterium GW2011_GWA2_35_19.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1618478 {ECO:0000313|EMBL:KKP73301.1, ECO:0000313|Proteomes:UP000034457};
RN   [1] {ECO:0000313|EMBL:KKP73301.1, ECO:0000313|Proteomes:UP000034457}
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   -!- 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}.
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:KKP73301.1}.
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DR   EMBL; LBQC01000005; KKP73301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0CB37; -.
DR   STRING; 1618478.UR68_C0005G0035; -.
DR   PATRIC; fig|1618478.3.peg.302; -.
DR   Proteomes; UP000034457; Unassembled WGS sequence.
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; 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   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          124..330
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          405..596
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   854 AA;  97182 MW;  FF033C84898A0DCC CRC64;
     MTTTGPADYA LFANGKLIAF VEAKKISLGP QNVLQQAHRY VKGAEEQGTT VPFIYSTNGE
     VIWFEDLRVT PSRSRQVQEF YTPKALIEYI INKAFENVTW FTNNPPANTK LRYYQRDAIT
     SIEKAITNNK RSMLVAMATG TGKTYTIASL VYRLLKSGVS KRILFLVDRK ALAAQAVMEF
     AAYEAESGLK FNQIYQVYSQ RFKVDDFEAN EKVDFNVIPT GYLTDPDGNQ VFIYISTIQR
     MQINLYGREG MFSYSGDYDP DDDADKIDMP INAFDTIIAD ECHRGYTSQE VSKWRGVLDH
     FDAIKIGLTA TPAAHTTSYF KEIAYRYGYE KAVQDGYLVD YDAVKIASGV RLQGIDLKEG
     EEVEQVDTDT GAQQLDLLED ERHFDVTDVE RDITAPDSNR KIVQELAKYA LEQEKETGRF
     PKTLIFADND LPHTSHSDQL VDICRDTFGR GDAFVQKITG SPTVDRPLTR IKEFRNRPEP
     HIVVTVDMLS TGVDIPSIEN IVFLRPVKSR ILFEQMLGRG TRLCTNFPNG LGTPAKTHFT
     VFDCFDGTLL EAFKNSTGIT QIAPINPTRS IDEIIKAIND NVDIEYNTRC LVKRLQRIAK
     NITAEGREMF AKNITDGDIS AFAKELPNKL SEDRVGTLKV LTDPKFIDLL KNYPRPPKRF
     IRAIEQEDTV TSEFVFRTTD GRELKPEDYL KQFEKFVKDN PEHIEAISIV LSKPQGWNTD
     ALKELRTSLA QQPERYTEDN LRRAYKYPLA DIISMVKHAA KDEPLLSAKE RVDLAIEKVI
     GKKQLNEKQE QWIELIKLHL AENLTIDQED FDEMPIFTNL GGSFKRINAD FDDRLLPFIT
     QLNTTIPQVY AYAN
//
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