ID   A0A2V1IW60_9BACT        Unreviewed;      1190 AA.
AC   A0A2V1IW60;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=C5O25_09450 {ECO:0000313|EMBL:PWB06738.1};
OS   Paramuribaculum intestinale.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC   Paramuribaculum.
OX   NCBI_TaxID=2094151 {ECO:0000313|EMBL:PWB06738.1, ECO:0000313|Proteomes:UP000244925};
RN   [1] {ECO:0000313|Proteomes:UP000244925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100764 {ECO:0000313|Proteomes:UP000244925};
RA   Clavel T., Strowig T.;
RL   Submitted (FEB-2018) 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}.
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:PWB06738.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PUBV01000020; PWB06738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1IW60; -.
DR   Proteomes; UP000244925; 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; 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, ECO:0000313|EMBL:PWB06738.1};
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          281..486
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1190 AA;  136889 MW;  CED13D80822CE9DC CRC64;
     MNADNETRFE EHIEAALLAS PLYIGRSSKD FDIKRRVDPG MLWQFLHAQH ETWERLLKRF
     KTGDDALNAV IKDYNSKLDN GHSLVDILRN GLKIQGIPVK LMQTKPTLAG EDSNLHELYL
     ANRFAVVRQM RYSEDKADKG NELDLCILLN GFPIITAELK NEGTGQNYTN GIYQYRHDRD
     PKNAMLRTAL VHFVVDNNYA FMTTFLNGED TSFLPFNVDS VNPQVPGDYA TSYLWKDIWQ
     ADSLLNIIDH FIKSVTDNGK TVTFFPRYHQ LRVVRNLIKW VEQEGPGHNY LIEHSAGSGK
     TKSMAWLAHQ LVNLVNNDQT PVFDSIIMVT DRIVLNANMA DDVNAFATEA GVVKDIRRGS
     KKLAKAINDG GRIIVSTVQK FSYALSELKR DKHRNYAVII DEAHTAIGNE SAKDIVNALS
     TDEDIQALIA EMECEGYESN EMDALMAYMQ TMRQQMGHIS YFAFTATPKD KTYALFGKKT
     TEGYVAHDYY TMKQAIDEKF ILDVLRNYTT YKTMFEYIEK NSAHPTMAMT TEGVSGVNEP
     EELYGEKKSV ALILRKLNQE PENMTLKARL ALNYFMQHTR NKIGGKAKAM FVSDSRAAAV
     RYKKIFDNLL AEEYGSEFKT LVAFSGEVEL PDGTKYTEDK MNGWGIKDDK IRETFDTPEY
     RILIVADKFQ TGFDQPLLHT MYVDKMLGGI QCIQTLSRLN RCYDKGGVKK EDTMVIDFRN
     DADSVQKAFQ KYYQTTILTG EVDTQRLYTL LDDIKVFKLY NTAERDQVVA AMVKEDAASA
     VSICNTIVRE RETPLSNEDK DKFRKLVNRY IRSYGFMAQL LTYCDPELER EYIFLRALYP
     RLQYTKETLP MEILDRVDLN KLRLQMVMEG TIALENEDAE LSSSRIGDVK APVEDEKKTL
     REILDIVNEP YRGFLEDHDI VLRPLNHMML TDPSINEAVR SGNSYGVLRE LFSERAQDLV
     LDMSGKGIDL YEEFMNDTPF AREYIRNILD MALRNNQQSN IDLDLHRLSE KIIEEIRSEF
     AELAQTSRRL DEVAEYLINI IQKRTKPGLD GANDLLINSL NHLLCNDRLT ELDRRAHFNT
     LVGKFEPFLK KLYYLINNRE LTTREGAVDR TQFADCIFGH ESLRRLKHTT DPRYFRFRDY
     LEKVRAWRND EAHSAPEFTD EELKVAVHIL VTMYAYVTAK SITDLEMNGL
//