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Database: UniProt
Entry: A0A3P2AJ13_9FIRM
LinkDB: A0A3P2AJ13_9FIRM
Original site: A0A3P2AJ13_9FIRM 
ID   A0A3P2AJ13_9FIRM        Unreviewed;      1023 AA.
AC   A0A3P2AJ13;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=EII17_09590 {ECO:0000313|EMBL:RRD94200.1};
OS   Clostridiales bacterium COT073_COT-073.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=2491044 {ECO:0000313|EMBL:RRD94200.1, ECO:0000313|Proteomes:UP000266937};
RN   [1] {ECO:0000313|EMBL:RRD94200.1, ECO:0000313|Proteomes:UP000266937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT073_COT-073 {ECO:0000313|EMBL:RRD94200.1,
RC   ECO:0000313|Proteomes:UP000266937};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-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:RRD94200.1}.
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DR   EMBL; RQYD01000020; RRD94200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P2AJ13; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000266937; 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:RRD94200.1};
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:UP000266937};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          296..501
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1023 AA;  117870 MW;  547814FD4D5B2BB4 CRC64;
     MSDFDVKEKR FEEDIEAYLC TYGGYSKGSP SKFDRELALD KETFLKFIKE SQPKAWERYQ
     TIYGKDSEKQ VVDRFDREVK MNGVLKVLRQ GFKDRGITFR AIYWKPETSI NKTSQLQYNA
     NIFHCTRQLH YSLNNQNSID IVLFINGIPL ISMELKCQFA GQNTANAISQ YKFDRAGKEA
     IFRFKERVLV HFAVDLSNVY MTTKLEGDKT YFLPFNQGSN GAGNVGGAGN PTNANGYDTS
     YLWEEVLHKD RLLEIIHKYL HLQIEKDEAT GQIISERIIF PRYHQLDVVT KLLKDVKENG
     SGKNYLIQHS AGSGKSNSIA WLSHRLSGLH NEKDEKIFKS VIIVTDRRVL DSQLQNTVYQ
     FDHVEGVVQK IDKNAKQLKE AIEVGTGIII TTLQKFPVIY KEVNSGNHRF AVIVDEAHSS
     QTGDAAKKLK RALADTEKVL EEYADLEYEE EVIRKDDEDK LVEELAAQGS HENLSFFAFT
     ATPKDKTLNM FGQKDSAGRY HPFHVYSMRQ AIEEGFILDV LKNYMTYKMY YKIAKAIPDN
     PEIDTTAGIK AIKHFETLHP HNISQKTAVM LEHFIHVTSS KIGGKAKAMV VTPSRLHAVR
     YVHEFKRQIM QKGYKDLDVL VAFSGEIEDD GIIYTEEKIN KDKNGETIKE KALPEAFHKD
     DFGMLIVAEK YQTGFDEPLL HTMFVDKKLS GVKAVQTLSR LNRIARGKKD TFVLDFVNSA
     EDIKNSFEPY FEETVLEEET NPNVIYDLKN TLDEYRVYQE IEIRKFAEVF YSGKEQAAGD
     LGKLQAQIKP ALDRYQALAE DSKDLFKSTL ARFNRIYAFI TQVCRLFDKD IHKFSVYVKF
     LLMQLPKGDI EQIDVSDKVM LEYYRLEKDF EGEIQLEPTE QGFTPITGEA GRRERKKDPL
     SEVIDKINTQ FGTSFTEMDK VLLQIANDYA DDNKWKSYAG NDYKTFMLLF QQDFPKMAAK
     RYEQNEEFFV KMFNNEDMMK EVMDAVGGVL YDQLRGGVKY VPHEPRDYMA ADAGKGKYRE
     RKI
//
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