ID A0A0G0YXI6_9BACT Unreviewed; 493 AA.
AC A0A0G0YXI6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN ORFNames=UV05_C0057G0008 {ECO:0000313|EMBL:KKS41299.1};
OS candidate division CPR1 bacterium GW2011_GWA2_42_17.
OC Bacteria; candidate division CPR1.
OX NCBI_TaxID=1618341 {ECO:0000313|EMBL:KKS41299.1, ECO:0000313|Proteomes:UP000034875};
RN [1] {ECO:0000313|EMBL:KKS41299.1, ECO:0000313|Proteomes:UP000034875}
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 -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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 ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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:KKS41299.1}.
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DR EMBL; LCCZ01000057; KKS41299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0YXI6; -.
DR PATRIC; fig|1618341.3.peg.737; -.
DR Proteomes; UP000034875; 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; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 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, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 283..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 493 AA; 56601 MW; E9703A3685E6B59C CRC64;
MNEFSENNLI EQTAVKLFKE LWGSGCSINA YSDEGDALLG RENQGQVVLI GRLKQALEKL
NPDAPQEAIA QAITELTRDR STASMVSANH EIYKLIKDGV KAEIRDEHGS FETINIKVID
FNDPAKNDFL LVSQMWITGE LHKRRPDLIG FVNGLPLVLI ELKASHKNLR NAYQENIRDY
KDTIPQLFWH NAFVIISNGI ETKVGTLTSA YEHFNEWKKI KSEDEEGRVS LETVIKGTCE
PSRLLDIVEN FTLFDDSFRE RIKAISRYFQ LLGVNQAFEQ IKNRDKNNGR LGVFWHTQGS
GKSYSMIFLS QKVFRKMTGN FTFVVVTDRN ELDKQIYKTF SACGAVYEEE VHADSIQNLR
QLLSEDHRHI FTLIHKFGTK PEEKPPILSD RSDIIVMVDE AHRTQYDRLA QNMRIAMPKA
SFIGFTGTPL MAKGEEKTRE TFGDYVSTYN FAQSVEDGAT VPLYYENRVP KLENENPEIQ
KDLERVMDPR IRR
//
