ID   A0A2Z2HQK6_9EURY        Unreviewed;       989 AA.
AC   A0A2Z2HQK6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-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   ORFNames=B1756_05925 {ECO:0000313|EMBL:ARS89329.1};
OS   Natrarchaeobaculum aegyptiacum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrarchaeobaculum.
OX   NCBI_TaxID=745377 {ECO:0000313|EMBL:ARS89329.1, ECO:0000313|Proteomes:UP000250088};
RN   [1] {ECO:0000313|Proteomes:UP000250088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW/NM-HA 15 {ECO:0000313|Proteomes:UP000250088};
RA   Zhao B.;
RT   "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely
RT   halophilic alkalithermophilic archaeon isolated from the athalassohaline
RT   Wadi An Natrun, Egypt.";
RL   Submitted (FEB-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; CP019893; ARS89329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2HQK6; -.
DR   REBASE; 202755; NarHA15ORF5915P.
DR   KEGG; naj:B1756_05925; -.
DR   OrthoDB; 11429at2157; -.
DR   Proteomes; UP000250088; 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   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:ARS89329.1};
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:UP000250088};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          294..491
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          860..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  112750 MW;  FCAA6F049CB23715 CRC64;
     MTYGTYDEES FEDLIASNLV EHSDYGYLPS EEFDRERGIF PDVVVSFVKE TQPEKWEKLE
     TAYKGNARKR FLQDLTSAME GRGTLELLRH GLRTTGTTID LAAFKPNTGL NPEVQKRYEA
     NRLGVTQQFY YSTTDPKKSI DLALTVNGIP VATAELKNKF TDQSVIDAKV QYKSDRDSGE
     PALKFKRGAL VHFAVDQDEV EYTTELDGDD THFLPFNKGH NGGAGNPPRE DSHRTAYLWE
     EVWEKDSWME ILQRFIHIDT EEIRKGGVKV DEEETIIFPR YHQLECVRQL VDAAQENGAG
     EDYLVQHSTG SGKSKSIAWL VHRLVSLHND ADEAVFDGVV VVTDRTVLDE QLRNTIYELD
     HKTGVVHAVK GEQGSKSQEL AEAIEAGKPV IITTLQTFPH VIEHAKRLPE RDYAVVVDEA
     HSSQSGEMAH EMKQILSGID IDEDDDAEDL IVKSAETRGN QENLSFFAFT ATPKGKTLEA
     FGTVPEGGDK PEPFHLYSMR QAIEEGFILD VLQHYTTYDT FYNVAKVIKE DPQVPQKKAV
     KAVSKFLKLH PHNISQKVEI IVEHFREHAQ HKIGGKAKAM VVTSSRVHAV RYKKAIDEYI
     EKNGYNLSAL VAFSGTVEDD GFEYTEREMN NGIKESELPS KFDTPEYQVL VVADKYQTGF
     DQPLLHTMYV DKKLSGIQAV QTLSRLNRTH PGKEDTFVLD FENDREDIYE AFEPYYEKTT
     LEEATDPQHI YQLESDLNAS QIYTQQEVDQ FAEAFFSPEN KGTEQAHAKL SSLIQPARDR
     FMVSDEETQD EFRSQLRSFL RLYKFQSQVV NYSDTTLEKL YTFGRFLYKE LPRDSRESRV
     EFNDELALQY YRLEKSDEGS IELDSSGGGV SSPTETGTGS QDDEEVELST IVEKINEKLG
     TDFTEADQLF LDQIKEDALE DDHIRRSAQV NTKENFALEF DDVLTGMFID RMDQNQDLFA
     KFMDNEEVQE AITKHLRREV YKESQQANG
//