ID   A0A208Y6G0_9BURK        Unreviewed;       999 AA.
AC   A0A208Y6G0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=CDO44_03075 {ECO:0000313|EMBL:OVZ63781.1};
OS   Pigmentiphaga sp. NML080357.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pigmentiphaga.
OX   NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ63781.1, ECO:0000313|Proteomes:UP000196551};
RN   [1] {ECO:0000313|EMBL:OVZ63781.1, ECO:0000313|Proteomes:UP000196551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML080357 {ECO:0000313|EMBL:OVZ63781.1,
RC   ECO:0000313|Proteomes:UP000196551};
RA   Bernier A.-M., Bernard K.;
RT   "Pigmentiphaga species Genome sequencing and assembly.";
RL   Submitted (MAY-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   -!- 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:OVZ63781.1}.
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DR   EMBL; NINW01000011; OVZ63781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A208Y6G0; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000196551; 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:0004386; F:helicase activity; 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; 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   Helicase {ECO:0000313|EMBL:OVZ63781.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          291..489
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   999 AA;  111684 MW;  945F9E7633728898 CRC64;
     MATTDTSEKG LEALIVRDLV ARGYVQGHAA DYHRDVALDL TQLLAFLRAT QPKAVETLNL
     DADGIQRTQF LHRLQGEIAK RGVVDVLRKG VDHGPVHVDL YKLLPTPGNA AATEAFGKNL
     FSVTRQVRYS NDESQRALDM VVFINGLPVL TFELKNSLTK QTVADAVVQY QTDRNPAELL
     FQLGRCIAHV AVDDAEVRFC THLTGKTSWF LPFNQGWNSG AGNPPNPNGL RTDYLWKQVL
     AKESLANIIE NYAQVIEEEE EDTNGRKRRT RKQIFPRFHQ LRTVRALLRR SRTDGVGKRY
     LIQHSAGSGK SNTIAWLAHQ LVELKTAADD TQAQFDSVIV ITDRRALDAQ IARTIKAYDH
     VASIYGHSES ADELRTFLRR GKKIIVTTVQ KFPFILDELG DLGDKKFALL IDEAHSSQGG
     KTTAKMHLAL SSQAAEGAEE EEESVEDKVN ALIESRRMLA NASYYAFTAT PKTKTLELFG
     ERQVVGDTVQ FRSPEELTYT TKQAIQEGFI LDVIANYTPV SSFYHVAKTV EHDPEVDKAK
     ALKKIRRYVE SHDKAIRRKA EIMVDHFAEQ VIGAKKIGGK ARAMIVCNGI ARAIDYFREV
     SDYLTEIKSP YKAIVAYSGE FEVGGSKKTE ADLNGFPSKD IPAKLKQEPY RFLIVANKFV
     TGFDEPLLHT MYVDKPLAGV LAVQTLSRLN RAHPQKADTF VLDFADNAEA VKAAFQEYYR
     ATIQEGETDP NKLHDLKGDL DAQQVYSWQQ VEDLVAQYLG GAERDRLDPI LDACVAEYVE
     KLSEDDQVKF KGKAKAFVRS YSFLSAILPY GHPAWEKLSI FLNFLIPKLP APKEEDLSKG
     VLEAIDMDSY RAQAQASMRM AMDDADAFVE PPPPGGGGGG GEPELDRLSN IIKQFNDLFG
     NIEWHDADKI RKVVTEEIPA RVAQDKAYQN AQAHSGKQNA RLEHDKALNR VVLELLDDHT
     ELFKQFSDNP NFKRWLADMV FDSTYRPGAT PPTPPQGSA
//