ID   A0A090HWA9_9FIRM        Unreviewed;       970 AA.
AC   A0A090HWA9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=ING2D1G_0222 {ECO:0000313|EMBL:CDZ74416.1};
OS   Peptoniphilus sp. ING2-D1G.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=1912856 {ECO:0000313|EMBL:CDZ74416.1, ECO:0000313|Proteomes:UP000032409};
RN   [1] {ECO:0000313|EMBL:CDZ74416.1, ECO:0000313|Proteomes:UP000032409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Peptoniphilus sp. ING2-D1G {ECO:0000313|Proteomes:UP000032409};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LM997412; CDZ74416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090HWA9; -.
DR   STRING; 1912856.ING2D1G_0222; -.
DR   REBASE; 92863; Psp11ORF224P.
DR   KEGG; ped:ING2D1G_0222; -.
DR   PATRIC; fig|875453.3.peg.216; -.
DR   HOGENOM; CLU_010804_0_0_9; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000032409; Chromosome.
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; cd22332; HsdR_N; 1.
DR   Gene3D; 3.90.1570.50; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000032409};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          294..487
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   970 AA;  111580 MW;  E3FA47659D542A4B CRC64;
     MGIRTEKAES ALESQIIEYL QTIGYDYVKP SEMKLSYNKK YAIDEKRLFS FIEKTQPTAY
     HNHRLDTDLG RQKFLNNLSS ALIRDGIAHV LKEGVKMYPT GVIFFYHALD KKRPSSFDEF
     NSNIFSVTNQ LTYSEANPGL ELDVCVFING LPIITMELKS RMSGTGWTCK DAEDQYKNDR
     DSREPLFMFK RCFAHFAVDE NYVSFTTKLN DKDTFFMPFN KGNGDGGAGN PIGEGTMTDY
     LWKDFLSKKT LRSLITQFVY IQRKKDTKTK KTKETLIFPR FHQYRVVTRL VEDVEKNSVG
     GRYLIQHSAG SGKSNSITWL AYRLVEAEKD YKKLFDSVIV VTDRKNLDKQ ISDNIRSFIS
     VSSNFAHSDS SKELEKLLVD GKKIITTTVQ KFPYIIETIG TKMKGKNFAV IIDEAHSSQS
     GKAAASLSTA ISGNYKVTDD MDSEDYINAI IEARKMPENA SYFAFTATPK AKTIEMFGSV
     FDLYSMKQAI EEGFILDVLK NYTTYGNYYK VYKTVEDNPL FESKKASRKI RNFVEGQEFP
     IRQKSEEIVN HFINNSSKKI NGKAKAMVVT SSILRAIEYY FAINDILNAY KSPFKALVAF
     SGEKEYKGKK VTESLLNEFS DKETPEVFKK DEYKFLIVAD KYQTGYDEPL LHTMYVDKIL
     NDVKAVQTLS RLNRCCENKI DTCVLDFAND ADDIKDAFQP FYKETKLIEG TDPNKLYEIL
     GKLDYLNVYE EDEVDRVIDM FFENKSREFI DPIMDTCVER YKGLDEEDQV EFKSGVKSFI
     RTYNFLSAIL PIGQIEWAKK SIFFELLVHR LPTPRDDEGI NEILESIDLE SYRLEKQNEL
     NIALENEDGE TSSNQAGTAR PFEPEMESLD IIIANFNDIF GNIDWNDKDN VARQIKELPD
     MVAKDERIIN AIKNSDKGNV KIEYENVLAD VMRAIMKDNM ELFLQFTSNQ QFKKWLSDSV
     FEEIMTVISK
//