ID A0A095Z7H7_9BACT Unreviewed; 947 AA.
AC A0A095Z7H7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=HMPREF1640_12725 {ECO:0000313|EMBL:KGF14712.1};
OS Prevotella sp. S7-1-8.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF14712.1, ECO:0000313|Proteomes:UP000029597};
RN [1] {ECO:0000313|EMBL:KGF14712.1, ECO:0000313|Proteomes:UP000029597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF14712.1,
RC ECO:0000313|Proteomes:UP000029597};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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}.
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:KGF14712.1}.
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DR EMBL; JRNC01000092; KGF14712.1; -; Genomic_DNA.
DR RefSeq; WP_036894952.1; NZ_JRNC01000092.1.
DR AlphaFoldDB; A0A095Z7H7; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000029597; 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; 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; 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 ENDONUCLEASE SUBUNIT; 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, ECO:0000313|EMBL:KGF14712.1};
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:UP000029597};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 256..404
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 754..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 109996 MW; 48EEC0A5C7607740 CRC64;
MPVQSEAALE NGLIATLQQM NYEYVQIEEE KNLRTNFKSQ LEKHNRKRLE EIGRTEFTEA
EFDKILIYLE GGTRFEKAKK LRDLFPLELD DGERLWVEFL NRTHWCQNEF QVSHQITVEG
RKKCRYDVTI LINGLPLVQI ELKRRGVELK QAYNQIQRYH KTSFHGLFDY VQLFVISNGV
NTRYFANNPN SGYKFTFNWT DAANVPFNEL EKFATSFFDK CTLGKIIGKY IVLHEGDKCL
MVLRPYQFYA VEKILDRVKN SNNNGYIWHT TGAGKTLTSF KAAQLVAELN DVDKVMFVVD
RHDLDTQTQS EYEAFEPGAV DSTDNTDELV KRLHGNSKII ITTIQKLNAA VSKQWYSRRI
EEIRHSRIVM IFDECHRSHF GDCHKNIVRF FDNTQIFGFT GTPIFVENAV DGHTTKEIFG
NCLHKYLIKD AIADENVLGF LVEYYHGNAD VDNANQNRMT EIAKFILNNF NKSTFDGEFD
ALFAVQSVST LIRYYKIFKS LNPKIRIGAV FTYASNSSQD DALTGMNTGS YVSESTGEAD
ELQAIMDDYN DMFGTSFTTE NFRAYYDDIN LRMKKKKTDM KPLDLCLVVG MFLTGFDSKK
LNTLYVDKNM DYHGLLQAFS RTNRVLNEKK RFGKIVCFRD LKSNVDASIK LFSNSNNLED
IVRPPFNEVK KNYQELTTNF LEQYPTPSSI DLLQSEKDKK QFILAFRDVI KKHAEIQVYD
EFEEDTADLG MTEQQFMDFR SKYLDIYDTF AGGCKPSEEN QTPDEDTEST ETSTESGIDD
IDFCLELLHS DIINVTYILE LIADLNPYSA DYKEKRTYII DTMIKDAELR NKAKLIDGFI
QQNVDDDRDN FMARKQKFDG TSELEERLNN YITTERNNAV DKLAKEEGLD VSVLNHYLSE
YDYLQKEQPE IIQEALKEKH LGLIKKRKTL TRILERLKSI IRTFSWE
//
