ID   A0A3S0XMC8_CHLFR        Unreviewed;      1011 AA.
AC   A0A3S0XMC8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   Name=hsdR2 {ECO:0000313|EMBL:RUR72716.1};
GN   ORFNames=PCC6912_60910 {ECO:0000313|EMBL:RUR72716.1};
OS   Chlorogloeopsis fritschii PCC 6912.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC   Chlorogloeopsis.
OX   NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR72716.1, ECO:0000313|Proteomes:UP000268857};
RN   [1] {ECO:0000313|EMBL:RUR72716.1, ECO:0000313|Proteomes:UP000268857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR72716.1,
RC   ECO:0000313|Proteomes:UP000268857};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2018).
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:RUR72716.1}.
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DR   EMBL; RSCJ01000043; RUR72716.1; -; Genomic_DNA.
DR   RefSeq; WP_016878817.1; NZ_RSCJ01000043.1.
DR   AlphaFoldDB; A0A3S0XMC8; -.
DR   STRING; 211165.GCA_000317285_02248; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000268857; 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; cd22332; HsdR_N; 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; 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; 2.
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:RUR72716.1};
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:UP000268857};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          291..511
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1011 AA;  115927 MW;  24380113E8A07ED5 CRC64;
     MHTEDKFEDI IEQELLKLSG YHQGNPGDYD ADTALFPTEI INFIQTTQPK QWQRLANTNP
     SDAQKIIIDS LTKELKSRGM LDVLRNGFKC YGKTLRVAYF QPNTGMNPET LALYEKNRLT
     ITRQVKIKTA GIPDILLSIN GLPIATIELK NPFTGQTYQN AIHQFRHHRD PQDPLFTFKQ
     RCLVHFAVDT EEVWMTTKLA GESTHFLPFN KGHNHGAGNP PGNNEEYRTS YFWLEVLQKD
     SLLDILARFL HIEIKETKIP TATGVNYQKK ETLIFPRYHQ LDVVRKLVNH AKQHKAGHNY
     LIQHSAGSGK SNSIAWLAHR LANLHDNQDE KIFHTVVVIT DRTVLDQQLQ NTIYQFEHKA
     GVVQKIDENT QQLATALSDG VPIIISTIQK FPFITKAIET LAKKGKTIDI TTKDKRFAVI
     VDEAHGSQTG ETATELRKIL NKDGIESAIA AQLLEDELEE DDLTDEAKQQ LLKEQLTRTK
     QPNLSYFAFS ATPKHKTLLI FDQPGENGKA PFHLYTMRQA IEEGYIKDVL ANYTCYERYY
     ELVRTCENNP DLPRRQAAKA IARFVELHPH NIAQKVEIII EHFRNHTRHK IGGRAKAMVV
     TRSREHAVKY KLAFDKYIKQ KGYSDIKSLV AFSGSITLDE FPGETFTEVN MNGGIKTSEI
     PDKFASDAYQ VLLVANKFQT GFDQPLLHTM FVDKRLDGVQ AVQTLSRLNR TTTGKEDTFV
     LDFVNKPEDI YQAFKPYYEE TPIGETAEPQ QLNELSYQLY EWQLFSQDDV KQWCEIWFRP
     KTSLTGSEHK KLNTLLDPII ENYKVLPDPD KEQFRSQLTS FRNLYLFLAQ IIPYQDSELE
     KLYAYGRFLL KKLPHSNQAP KIDLSGDIEL KFYRLEKISQ GKIDLNEGKA EPLRGAIALG
     TRQLDKEVPL SALIDSLNER FGTNFTPADQ LFFEQITETA IANDSIKQAA QVNTKENFAP
     VLEKHIENLF IERMDGNEKI FMQVMNNEEF KAIVFEKLLS SIYESIKSEN L
//