ID   A0A1C5E142_9ACTN        Unreviewed;      1073 AA.
AC   A0A1C5E142;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=GA0115259_1042415 {ECO:0000313|EMBL:SCF88912.1};
OS   Streptomyces sp. MnatMP-M17.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839780 {ECO:0000313|EMBL:SCF88912.1, ECO:0000313|Proteomes:UP000198886};
RN   [1] {ECO:0000313|EMBL:SCF88912.1, ECO:0000313|Proteomes:UP000198886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MnatMP-M17 {ECO:0000313|EMBL:SCF88912.1,
RC   ECO:0000313|Proteomes:UP000198886};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; FMDK01000408; SCF88912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5E142; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000198886; 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.
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};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198886};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          295..527
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
FT   REGION          1043..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1073 AA;  119206 MW;  D2D6300E4B13BFCB CRC64;
     MTPTPRPRRV DNEAAFEIAV EDALLTRGWE RGLANAYNHE LGIDTSELAI FLGATQNDAW
     LRLQAEYGAD EKISIQRFAK RIAQQIDSRG VLDVLRHGVV DQRVKFQLAY FRPAHTLAVG
     VLDNYDANRL TVVRQFHYSA KTPAKSVDLA FFLNGLPLAS AELKNHTTDH PQTAEDAIRQ
     YRTDRDPKET FFAKRTLVHF AVDPTLAFLT TRLAGPKTRF LPFNMGSGGP GQIGGAGNPS
     RAETDGTYPV SYLWQQVWAR DNWLELLERF LHIEDAQAKA GKAPSHRPGS AHTQPMIFPR
     FHQWHAVRQL TAHAAQHGAG ENYLIQHSAG SGKSNTIAWL AHRLSSLHTP EDPAHLGEAV
     RAKGLGTNEP VFDKVIVITD RRVLDKQLQD TIFQFTHTPG VVQRIDEDSA QLAEALTGST
     ARIVITTLQK FPYVLKKVGG LGTLRYAVII DEAHSSQGGD GSAALKKALG AHTVDEDGDP
     LTAEALARGQ QPNMSFFAFT ATPKPKTLHL FGVPVPDSDE YAPFHVYSMR QAIEEGFILD
     VLGTYSTYAT YFKLQQAAAE EAERQVDPRK ARAKLVRAAL MSDASMASRA KIIVEHFRSH
     TAAKLGGRAK AMVVTPSREH AVRLYQAIRS YIEERGLTDC GTLVAFSGAV NVDSIEYTEP
     KLNGFPEKEL PGRFGYVRAD DPSAPTIPKP EYRLLVVAEK YQTGFDQPLL TTMYVDKPLA
     GVAAVQTLSR LNRTHPLKSQ EDLFVLDFAN KPEVILDAFQ KYYEASLTEI TDPNLLFDRL
     DEAMAYQLLV ESEMDALVKA YFEALDGGRA TEEQIKKVHA KLYHYTAPAV DRFNALAAQE
     RDKAEEFRRA LESYVKAYGW LSHVIGFDST ELERLFQYGR FLLRRLPRRT GAAAADIGET
     APSHMRVQQT GTPELKLEAV GAQVLPGLVP EAAGSAPEVE ERSLMEIIDE LNEEHGAGLT
     TADQILLGQL VVTIAEDPDM QQLALAQDSE IYGRELARDM DSFVIRQAQS NDALMVRYFD
     DDNVNRLFKK VATAQSYNLI RRPARREADR QATAERAAQL KNGTHKRTEP PAP
//