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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//