ID   A0A1Y2KAF4_9PROT        Unreviewed;      1125 AA.
AC   A0A1Y2KAF4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=MAIT1_04532 {ECO:0000313|EMBL:OSM07698.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM07698.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM07698.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM07698.1,
RC   ECO:0000313|Proteomes:UP000194003};
RX   PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA   Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA   Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT   "Combined genomic and structural analyses of a cultured magnetotactic
RT   bacterium reveals its niche adaptation to a dynamic environment.";
RL   BMC Genomics 17:726-726(2016).
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:OSM07698.1}.
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DR   EMBL; LVJN01000012; OSM07698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2KAF4; -.
DR   STRING; 1434232.MAIT1_04532; -.
DR   OrthoDB; 9803459at2; -.
DR   Proteomes; UP000194003; 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; IPR025285; DUF4145.
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; PF13643; DUF4145; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000194003};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          369..520
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          147..195
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1125 AA;  127595 MW;  4CE5DAF30952F886 CRC64;
     MKSLNFEFLR PSWPQLAELG GFAESYAHPD PASSQVKLRA FAEQLVLWIY DRAGFPKPFK
     PNLNDLLNEH AFQTAVPKVV VDKLHAIRIH GNKAAHGEKA STDTALWLLK ESHEVGRWIF
     VTSGQGKTTD LDAYQDPPSG GLAGEARSQL KREKKTVLEQ LAAQEAQMQA LLEELDAARE
     KAQTAELKAG ELEALIQSGR HAADALNFDE ATTRARLIDS QLATAGWRVT QADEVGQEVE
     VDHQPTQTGK GYADYVLWND DGKPLAVVEA KKTAKSAELG RKQAQLYADG LEKMHGQRPV
     IFYTNGFDIW IWDDAGGYPP RKLYGFYSKD SLQYLVTFQR ISRRELDEIQ PSEIAGRLYQ
     LEAIKRVCER FTARHRRSLV VQATGTGKTR VAISLTDALI RAGWVKRVLF LCDRKELRKQ
     AKNAYADFLN EPLVVVGRHT AKDRDKRIYL ATYPAMMKVF ETFDVGFFDL IIADESHRSI
     YNRYRDLFFY FDALQVGLTA TPVGMINRNT FKLFGCEDDD PTFNYDFSRA VEEGHLVPFE
     LFTHTTEFLR RGIKYEQLSE EQRQQLEDDG EDPESFDYDA QQVDKAVFNK DTNKHVLRNL
     MENGLREATG SHPGKTIVFA RNHNHAVLLS QLFDELYPQY GGGFCQVIDN YDPRAEQLID
     DFKGVGSNPG LTIAISVDML DTGIDVPEVV NLVFAKPVKS RVKFWQMIGR GTRLCPDLFG
     PGQHKRHFRI FDHWGNFEFF AEEFEEADPA PSKSLMQQVF EARIDLAETT LDQSEPAAFT
     LAVELLARDL AALPEETIAV REKWREKRTV QQAHVLEQFA PETVIMLRQT MAPLMQWIDI
     RDHSAAWQFD RLIALMQIEL LKKTSRFEDY RDQALDQVAQ LQMHLNPVRE KGEVIKTFKD
     PAFWTGVTVA DLEAKRQELR GIMHHRRPGA PVVQQTKVVD VTDGGVEFAH RKANITANDL
     AAYRKRVEEV LAPLFESNPT LRKIRAGEPV TEADLNALNA LIHTERPDVD LNILLEFYQD
     TAGGLAQILR SIIGMDAAAV EQHFADFVRR HPKLNARQIR FLGLLKNHIS KFGVIAIDRL
     YEPPFTTVDS EGPDGVFRDE AQMDDLIAIL EAFKPPAQQE ARTTA
//