ID A0A0G1KG44_9BACT Unreviewed; 858 AA.
AC A0A0G1KG44;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
DE Flags: Fragment;
GN ORFNames=UW39_C0016G0034 {ECO:0000313|EMBL:KKT46829.1};
OS Parcubacteria group bacterium GW2011_GWC2_44_17.
OC Bacteria.
OX NCBI_TaxID=1618929 {ECO:0000313|EMBL:KKT46829.1, ECO:0000313|Proteomes:UP000034811};
RN [1] {ECO:0000313|EMBL:KKT46829.1, ECO:0000313|Proteomes:UP000034811}
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:KKT46829.1}.
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DR EMBL; LCIC01000016; KKT46829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KG44; -.
DR STRING; 1618929.UW39_C0016G0034; -.
DR PATRIC; fig|1618929.3.peg.784; -.
DR Proteomes; UP000034811; 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 Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 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; 2.
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};
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 169..369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKT46829.1"
SQ SEQUENCE 858 AA; 98962 MW; 71FD5D5252B36D18 CRC64;
SLIRQVKFST KDEKSLDTVI FINGLPISTL ELKNYLTRQN VQHAIKQYRY TRDWREPLFM
FKRCLVHFAV DNDLVYMTTR LAGKSTYFLP FNKGFENGAG NPVNPSGFKS AYLWEEVLQK
DSLLQIIAEF MLVSIEVTTY EEGEQKEKEM LIFPRYHQLD AVRKMVAHAR EHDAGKNYLI
WHSAGSGKTK TISWLAHKLA SLQSSYNVKI FNSVIVVSDR RVIDKQLRDE VLQFQQVEGV
VQAVEKHSSQ LRDALDTSKK IIVTTLQKFP HIVDEISKQT DKKFAVIVDE AHSSQSGEST
KSLKKVLGSL EEAEKENTAE EELTAEDEIL RKLSGRGRQK NISFFAFTAT PKGKTMELFG
TKNADGTFSP FHLYSMRQAI DEGFILDVLK NYTTFQTYFN LIKKIEDDPQ YEKKKGIALL
KSYVELHDHA IGKKTELIIE HFLSHVARKI DGYAKVMVVT RSRLHAVRYK LAFDQYIKEH
KHPIKTLVAF SGTVNDGGKE YTEPGMNNLR SEKLTVETFK LPEYKILIVA NKFQTGFDQP
FLHTMYVDKK LGGVMAVQTL SRLNRTHKGK DDTMILDFAN HEEEIQKAFQ PYYDKAILTK
ATDPNKLYDL ERKLYEFNIF VKSDVEKFAK VFFKRGATQE KLHPLLDPIV EEYLKLEKKE
KTNFRDQLKN YIRLYAFLSQ IVSFKDVGLE KLYAFLRMLG RKLPADKERL PVEITDNVNM
DTYRVQQISS GSIELEKTTG ELKPAEGLGT GKRAGEEKEF LSRIIEEVNE RFGTDFTEGD
KVFFAELETR LAGNETLSES AKTNTKEALK LVFAHIFEDQ LHTMVESNFD IYKKIVENAE
FGQFIKEKIF EEVYSKLK
//