ID A8ZTW7_DESOH Unreviewed; 889 AA.
AC A8ZTW7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=Dole_2096 {ECO:0000313|EMBL:ABW67900.1};
OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS oleovorans).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW67900.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW67900.1, ECO:0000313|Proteomes:UP000008561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC {ECO:0000313|Proteomes:UP000008561};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) 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; CP000859; ABW67900.1; -; Genomic_DNA.
DR RefSeq; WP_012175512.1; NC_009943.1.
DR AlphaFoldDB; A8ZTW7; -.
DR STRING; 96561.Dole_2096; -.
DR REBASE; 16472; DolHORF2095P.
DR KEGG; dol:Dole_2096; -.
DR eggNOG; COG4096; Bacteria.
DR HOGENOM; CLU_007363_1_0_7; -.
DR Proteomes; UP000008561; Chromosome.
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; 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; 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; 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 SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008561};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 176..378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 453..632
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 416..467
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 889 AA; 101709 MW; 62CD76B971D720F6 CRC64;
MTESERTTRK KRIDTRLSSS LLNWTIIHND DVTDQSLLTH HAVEEYSTKT GPADYALFVD
GKLLGIIEAK KIAVGAGNVL EQAKRYSKGA PDSIGDWRGY KVPFLYSTNG ELIFHLDVRN
NQNTACRLID FHSPRALLDK FNRDTQSAEA WLAEKPIEDI TRLRPYQKEA IAAIETAIGN
GKKTMLVAMA TGTGKTFTLV SSIYRLLKSG YARRILFLVD RRSLAAQAVQ AISSFETPEG
LKLDNAYEVY SQKFRRDDFD DENNFDPKVL PEAYLTDPQE KHTFIYVSTI QRMSINLLGK
EAVGDFEYEV DAGKLDIPIH AFDVIIADEC HRGYSARETG RWKYVLDYFD AVKIGLTATP
ATHTLAMFKH KVFSYSTEQA VLDGFLVDYE AVKIKSGIHI NGAFLKEGEL VGVIDRESGA
EKLDELEDER EFVATEIEVK ITSPDSIKKI ISALKKYTDE HEKENNRFPK TLIFAVNDLP
HVSHADEIVK TCKEVYGRGD DFVMKITGSP TVDRPLQKIR QFRNRPEPNI VVTVDMLTTG
VDIPAIEMVV FMRMVKSRIL WVQMLGRGTR LCEEIHKEKF TIFDCFDGSL IKYFKDATDF
NVSLQREATP LSEIIEAIYD NQDREYNINR LIKRLRRIEK NMGAEAREAF TKYIPAGDMK
AFADRLKDNL AEQFTETMKL LRDKDFQDLL LNYPRPKKVF FKGYDIVDTV EHEVMFRVGG
DYQKPEDYLK LFEEFVRRNP EHIDAIDILL SRPKQWGTDA LDELRKQLRQ SDFSEKDLQR
GHALVYKKPL ADIISMIKHA SDYDVPILTA AERVDAAVEK IVRNHDFNDD QRAWLAYIKE
HLIENLAIAE EDFALMPVFE RQGGIGAARR VFGDRFEPLI CELNEALAA
//
