ID   A0A0J1EK57_RHOIS        Unreviewed;      1142 AA.
AC   A0A0J1EK57;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=RISK_002511 {ECO:0000313|EMBL:KLU05879.1};
OS   Rhodopirellula islandica.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=595434 {ECO:0000313|EMBL:KLU05879.1, ECO:0000313|Proteomes:UP000036367};
RN   [1] {ECO:0000313|EMBL:KLU05879.1, ECO:0000313|Proteomes:UP000036367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24040 / K833 {ECO:0000313|Proteomes:UP000036367};
RA   Kizina J., Richter M., Glockner F.O., Harder J.;
RT   "Permanent draft genome of Rhodopirellula islandicus K833.";
RL   Submitted (MAY-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:KLU05879.1}.
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DR   EMBL; LECT01000017; KLU05879.1; -; Genomic_DNA.
DR   RefSeq; WP_047814122.1; NZ_LECT01000017.1.
DR   AlphaFoldDB; A0A0J1EK57; -.
DR   STRING; 595434.RISK_002511; -.
DR   PATRIC; fig|595434.4.peg.2395; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000036367; 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.
DR   PROSITE; PS51194; HELICASE_CTER; 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, ECO:0000313|EMBL:KLU05879.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          363..525
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          600..789
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          153..201
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1142 AA;  130673 MW;  6421DE5F9653DE97 CRC64;
     MSNFDFLTSE WKDIHEAASK AESAAIPDPR TSCFYARRTL ELAARWAYKF DRALKLPYQD
     NLSALIHEPT FKHTAGDAVF NKAKLINKRG NDAVHSHRDV SQADAVSTVQ ELFHFCYWFA
     RLYARRNRPD PSLTFDPALL PTTAIPKQTL NQLKLLESQL KEKDEKLSVL LADKDKLDAE
     IKLLRTEVAK AKKAAEKIQD DHDYNEDETR DRWIDELLKE SGWPLDQKRD REFPVTGMPN
     TKGEGKVDYV LWGDDGKPLA VVEAKRTRRD PRVGEQQAKL YADCLEAIYG QRPIIFYSNG
     YEHWIWDDAM YAPRRVQGFY KKAELELLIL RRSSRRDLAS ATIDEEIAGR YYQTRAIRRI
     GESFEKDNER KSLLVMATGS GKTRTVIALC DLLIRCNWAK RVLFLADRVA LVNQATNAFK
     AFLPDSSPVN LVTEKDSEGR VYLSTYPTMM GLIDTAKQDG GKDGQKRFGV GHFDLVVIDE
     AHRSVYQKYG AIFDYFDSLL VGLTATPKDE IDKNTYGLFD LETGVPTDAY DLDEAVDDKF
     LVPPKAVSVP LKFEREGIKY DDLSEEDKDE WDAKEWDEEG NIPDKVEAAA VNKWLFNIDT
     VDKVLEHLMT RGQYVAGGDL LGKTIIFAKN QDHADFIKER FDINYPHYKG EFARIITFKT
     EYAQNVINSF SNKDKLPQIA ISVDMLDTGI DVPEVVNLVF FKLVRSKTKF WQMVGRGTRL
     CPDLFGPGQH KEFFYIFDYC QNLEYFSQNP AGSAGSTAES LSTRLFKRRL ELIRFLDGKE
     LPVTTEAISE ADAGYEVDPT SETQVRALAA RFLHRQVASM NLENFLVRAH RRSVEKFAQK
     EAWEQLKEAE IQELADEVAP LPTQMERESE EAKRFDLLLL NLQLSLLNKE PAYERLRQQV
     VAIAGLLEEK HTIPMVNQQM IHIEAVQTEE WWADVTLPML EVIRRRLRDL VQFIEKAKRK
     PVYTNFDDML GDEVEVGLDE FVGADTFERF RSKAQAFLRE HLGIDAVRKL RTNETLTKAD
     LDDLERILLD NEIGNHEYIE QAKQESEGFG VFVRSLVGID REVAKRLFGE FLQGSVYNAN
     QIEFINLIVN QLVDHGIVDA SLLYESPFTD ISPQGPDAIF TSEEVDKIMQ LLDDIRATAI
     AA
//