ID   A0A1X7AHK9_9GAMM        Unreviewed;       831 AA.
AC   A0A1X7AHK9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   Name=hsdR_1 {ECO:0000313|EMBL:SMA36371.1};
GN   ORFNames=EHSB41UT_00631 {ECO:0000313|EMBL:SMA36371.1};
OS   Parendozoicomonas haliclonae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Parendozoicomonas.
OX   NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA36371.1, ECO:0000313|Proteomes:UP000196573};
RN   [1] {ECO:0000313|EMBL:SMA36371.1, ECO:0000313|Proteomes:UP000196573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA36371.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-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}.
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DR   EMBL; FWPT01000001; SMA36371.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7AHK9; -.
DR   Proteomes; UP000196573; 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; 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; IPR001650; Helicase_C.
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; PF00271; Helicase_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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SMA36371.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196573};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          210..370
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          576..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..619
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  94547 MW;  EAC363456DBF54CE CRC64;
     MRLKGYSQIP TCITITNKTT MVTVQEEQLE KGEKQKLSER DICTKFITPA IKQAGWDINT
     QVREEVTFTA GRIIVRGKLH TRGKQRRADY ILYHQKNQPI AVIEAKDNKQ SVGAGMQQAL
     AYAEALDVPF VFSSNGDGFL FHDRTGNAAQ TETELTLEQF PSPAELWQRY CAWKGFSEAA
     MPAVESPYYD DGSGRTPRYY QTIAVNRAVE AVAKGQDRIL LVMATGTGKT YTAFQIIWRL
     WKAGQKKRIL FLADRNILVD QTKNNDFKPF GQAMTKITKR QINKSYEIYL SLYQAVTGNE
     EEKNVYKQFS PDFFDLIVID ECHRGSANED SAWREILEYF SGATHIGLTA TPKETKDVSN
     IDYFGQPVYT YSLKQGIEDG FLAPYKVVRV DFDLDLKGWR PRKGQKDKHG NLIEDRIYNQ
     RDMDRNITFD ERTQLVAMKV TEFLQQSGEY QKTIVFCDNI DHAERMRQAL VNLNPERVQE
     NRKYVVRITG DNEEGKAELD NFIDPESRYP VIATTSKLMT TGVDAKTCKL VVLDQRIQSM
     TEFKQIIGRG TRIDEDYGKH WFTIMDFKKA TELFADPNFD GDPVQIHNPK PGEPVTPPED
     ETDETDDTGN GDDETVSGDP DWPESGPGEG GLGEGGEGPA EPRIKYHVKG EQVTIIGERV
     QYLGADGKLI TESMRDYTKG CVTKEYASMD DFLRRWSDAD QKKAVIDELA EQGVFWEEVQ
     AEVSAKYGSE LDPFDMICHI VFDQPPLTRR ERAENVRKRD YFTKYGEEAR KVLEALLEKY
     ADAGIENIED IKVLKLEPFT DLGTPVQLIS LFGGKKQYLQ AVQDLETALY G
//