ID A0A1G7Q8E3_9BACT Unreviewed; 1049 AA.
AC A0A1G7Q8E3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05216518_11619 {ECO:0000313|EMBL:SDF94792.1};
OS Bacteroidales bacterium KHT7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1855373 {ECO:0000313|EMBL:SDF94792.1, ECO:0000313|Proteomes:UP000198526};
RN [1] {ECO:0000313|EMBL:SDF94792.1, ECO:0000313|Proteomes:UP000198526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHT7 {ECO:0000313|EMBL:SDF94792.1,
RC ECO:0000313|Proteomes:UP000198526};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNBQ01000016; SDF94792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7Q8E3; -.
DR STRING; 1855373.SAMN05216518_11619; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000198526; 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 CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME R PROTEIN; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000198526};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 317..465
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1049 AA; 120394 MW; B9EE4D5C778C3BCA CRC64;
MNQSIIIEEQ HRTVVAQYSP IPRNDDDYQS EAKLEKELIS TLSAQGYGTP AIHTEADMLA
NLRRQLEALN SITFTDAEWA RFFKQNIQCE PNNGQSVSND VIEQCTIKIQ KTRTFSLTRD
DGTVKNIDII DAANPYRNTL QVINQYVPEG GAHANRYDVT ILVNGLPLVH IELKRRGVNI
KEAFNQINRY GRDSFWAGSG LFNYVQIFVV SNGTNTKYYA NTTRYAHVKE QNGQKQGKVK
KDCNSWEFTS FWADEQNNII ADLADFARTF FAKSTILNIL TRFCVFTVDK NLMVMRPYQI
AATENILLRI RRALNLHHEG TRDAGGYIWH TTGSGKTLTS FKTAQLASCM PEIDKVLFVV
DRKDLDYQTM KEYDNFQKDS ANSNTNIGVL HRQLNDSQCH IIITTIQKLS ILLGKKDPRY
SLNCLDSRIV IIFDECHRSQ FGDMHKVIVR KFKRYMIFGF TGTPIFAENA GSARKTTADL
FGDKLHTYTI IDAIRDKNVL KFHVDYISTM HMKDGVKDEQ VWGINTKEAL HDSRRIHNNV
AYVLDHYAAK TKRDETYIVS RIENVEEVIK RGKKVDEVKQ KHRVRGFNSI FAADSVEMAI
AYYNEFKLQQ ANTPENERLK IATIFTYGSN EEETDADDDI IDDTNESPEN VEQLKQKSPV
AYEALSSAID DYNRMFSTQY SLDGDNFQSY YKDVSQRVKN RELDMVIVVG MFLTGFDAKT
LNTLWVDKNL KMHGLLQSYS RTNRILNSIK NCGNIVNFRN LEEETDRALS LFGDKDAAGV
VLLRPFGDYY YGYDTPDGKH HPGYTEIVSE LLEKFEPTEA FFLSLSVEQK KDFVRLFGAF
LKMNNLLSIF DQFTEDKRVI KVGQVQDFTS LYQEVREELQ GNKTKGDSTN INDDLVFEME
LVKQIQVSIE YILMLVKEYH DSNCTDKEIR VKISKAVKAS PDLRDKIELI ERFIERMTAS
SGDVFDEWDK YVAEQKEEEL KAIIAQFNLN EEKTRAYLAQ SESDGFISAS GTALAEVLPP
LNPFLPQRAE VKAKVFEALE NLFNKYRSV
//