ID   A0A117S130_9ACTN        Unreviewed;      1070 AA.
AC   A0A117S130;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=AQJ91_13240 {ECO:0000313|EMBL:KUO20857.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO20857.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO20857.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO20857.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-2015) 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:KUO20857.1}.
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DR   EMBL; LMXB01000031; KUO20857.1; -; Genomic_DNA.
DR   RefSeq; WP_067020120.1; NZ_KQ949080.1.
DR   AlphaFoldDB; A0A117S130; -.
DR   STRING; 909626.AQJ91_13240; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000053260; 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; 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:KUO20857.1};
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:UP000053260};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          300..536
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          473..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  118376 MW;  2CA964AC0543AA0A CRC64;
     MSPVHHESAF GDAIVAALRE HGWEEASPTG YRPELGFDTN QLFTFIGATQ PTPWNELLRY
     YGGDPNAAQR GFVKRLDRAI ADADGGVLQV LRDGVKDQGV RIRLAYFKPS LVESESILAN
     YHHNRLTVVR ELEYATKQAD RGHRLDLTLF LNGIPLATAE LKNPLTGQNV EDAKKQYRTE
     RDPSELIFTR RVVANFAVDP DLVFVATQLR GEKTWFLPFN TGSEGPGHPG GAGNPSATEP
     GTYATSHLWE QIWQRDNWLE LLERFVHLHK ETDGEGKAKK SLIFPRFHQW HAVRELTSHA
     ARHGSGHNYL VMASAGSGKS NTIAWLAHRL SSLHTLTDAS MLAPDAVAAG LLPGKPVFDK
     VVIITDRTVL DRQLQDTVGS FEQTAGLVVK VKKEGGAKSE QLAAALSQET GKIVIVTLQT
     FPALIDYLQR TPTEIKGRRF AIVIDEAHSS QSGDAATAVR KTLRDLGLDA DSEDDGAVEV
     EAEDGGKEAN STEARLKKNA ADRGQSPNLS YFAFTATPKA KTLELFGTLD MVEGKETYRP
     FHTYSMKQAI EEGFILDPLK NYVTYDTYWK LVNKNPDDRE VDPAKANPLL ARYALTHAST
     VAQHAQVIVE HFKEHTAGRL GGRAKAMVVT ASRQSAVQMA RSIKKYIGDR DYQGIGVLVA
     FSGTLTYDGD ERTESKENGG LAESALPKAF AYTRADDKSI KSGGPGKPEY RILVVAEKYQ
     TGFDQPLLTT MYVNKKLGGV SAVQTLSRLN RTAERKSQSD LAVLDFVNDA DDVQGAFIPY
     FAQAMTLPSD PNLLYTAQGK VMKAEIVVDA EMEAFVEAYL AAQDQAAGNT AKWERLHAEL
     YRLTDPARDR FAELLEDEGD KDKLKQAEDF RADLNGYVRM YGFLAQIVPY SDPELERLYL
     FGRHLLNRLP RREDAGVDIG QVDLTHLKVQ KTGEHDKSLT AEGPALMKGM GDGSGGAKEP
     EQSMLSELIE RFNDKFGTGL TTQDVLPAFE EAVADKDVRQ AALGNESEEK FGHVFEPVFE
     EKMMDHITLT AEMGRQYFSP QPDFRSSLNR SARSAAWRMI RDSAGLDDMT
//