ID   A0A2K8XPQ0_9FLAO        Unreviewed;       790 AA.
AC   A0A2K8XPQ0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=CW731_06260 {ECO:0000313|EMBL:AUC84919.1};
OS   Polaribacter sp. ALD11.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=2058137 {ECO:0000313|EMBL:AUC84919.1, ECO:0000313|Proteomes:UP000232878};
RN   [1] {ECO:0000313|EMBL:AUC84919.1, ECO:0000313|Proteomes:UP000232878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALD11 {ECO:0000313|EMBL:AUC84919.1,
RC   ECO:0000313|Proteomes:UP000232878};
RA   Collins E., Ducluzeau A.-L.;
RT   "Pharmacopeia of the Arctic Ocean.";
RL   Submitted (DEC-2017) 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   ---------------------------------------------------------------------------
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; CP025119; AUC84919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8XPQ0; -.
DR   REBASE; 226909; PspALD11ORF6270P.
DR   KEGG; poa:CW731_06260; -.
DR   OrthoDB; 9759819at2; -.
DR   Proteomes; UP000232878; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   CDD; cd18799; SF2_C_EcoAI-like; 1.
DR   Gene3D; 3.90.1570.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013670; EcoEI_R_C_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF08463; EcoEI_R_C; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF04851; ResIII; 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:AUC84919.1};
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:UP000232878};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          180..341
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   790 AA;  90795 MW;  65DE96D90E373339 CRC64;
     MNKKNLSERD ICTKFINPAI EKAGWNMRTQ VREEVSFTDG RIIVQGKLYT RGKSKRADYI
     LYYKSNIPIA IIEAKDNKKA VGHGMQQALE YSEILQIPFI FTSNGDSFVF HDKTRKEGNL
     EQELTLDSFP SPEELWQKYL VHNKIETPKA KEIVAKDYYA DDSGMTPRYY QQNAVNRTLE
     AIAKEQNRII LVMATGTGKT YTAFNIIWRL WKTGIKKRIL FLADRNALLT QTKNGDFSPF
     GNDIMHIIKN RKIDKSYQIY FALYQGLTST DDSKNAYKEF SKDFFDLVVI DECHRGSASE
     ASAWREVLDY FSSATQIGLT ATPKETKDVS NMEYFGEPVY TYSLKQGIDD GFLAPYKVVR
     ITTSVDEGWR PTAGLVDKYG HEIEDRIYNL KDYDKKLAID ERTEIVAKKI TEYLKATDRY
     AKTIVFCVDI DHANRMRQAL INENADLVAK NWNYCVKITG DDEVGKQELD NFTDVEERFP
     VIATSSKMLT TGIDTKMVKF IVLESNIQSV TEFKQIIGRG TRIREAEGKV FFTIMDFRKA
     TNIFARPDFD GDPVQIYEPT DGQPVVPPEE DDITLPSDGE EPLIPDDFRP TTPDINIDNE
     ETEVRKYYVN QVPVSIVNER VQYYGKDGKL ITESLKDYSR KNITKEFSSL DDFLQKWNAS
     EKKEELIKEL AEHGVLLEAL REDVGLDLDD FDLICHIAFD QPALTRTERA NNVRKRNYFS
     KYSDTAQKVL KSLLDKYEQE GIVSIEQGSI LKVKPLNEMG SPVELVRAFG KRKDFEKAVK
     ELENEIYNIA
//