ID A8ZS37_DESOH Unreviewed; 1038 AA.
AC A8ZS37;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN OrderedLocusNames=Dole_0245 {ECO:0000313|EMBL:ABW66055.1};
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:ABW66055.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW66055.1, 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 -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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 ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; CP000859; ABW66055.1; -; Genomic_DNA.
DR RefSeq; WP_012173674.1; NC_009943.1.
DR AlphaFoldDB; A8ZS37; -.
DR STRING; 96561.Dole_0245; -.
DR REBASE; 16449; DolHORF251P.
DR KEGG; dol:Dole_0245; -.
DR eggNOG; COG0610; Bacteria.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_005762_0_1_7; -.
DR OrthoDB; 9758243at2; -.
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; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 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, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Reference proteome {ECO:0000313|Proteomes:UP000008561};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 270..435
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1038 AA; 118041 MW; 3BD1ABC9959B8FE8 CRC64;
MPEKPRPERI TQNRVIALFT DKSRPDCLGY QYLGDWSKRD NNRPVEAEYL RANLKKRGYS
DAHISAALLQ LEIAAGTTGV TLYQANLRTY NLLRYPVKVL LAPGQPHEDV HLIDWEHPEN
NDFALAEEVT LKGGYERRPD LVLYINGMAI GVIELKRSSV EVADGVRQLI TNQEKIFNEG
FFSTVQLVFA GSDSQGLRYG TTGTPEQFFV QWKDEEGDSA LAPGTLLDKP LAQMCNKKRL
LDLIRNCIIF DAGQKKVPRP HQYFGFKAAQ ERIRRREGGV IWHTQGSGKS ILMVLIAKWL
MEHDPDARIL VITDRDELDK QIVDVMRNAG VVGEDAPSPR ITSRAQFVEK IGATTPRLLC
ALIHKFETTD LKGNPPPIHG RFYIFVDECH RTQGGDMNRQ MKRWMQDAIF IGFTGTPLLR
RDKLMTRDVF GTYIHTYKFH QGVADKVILD LKYEARNVPQ RLTSQKAIDA WFEQKTKNLN
NFQKAIVRKT WATMEKLMSA GERKQRIIAD IIQDFSLKPR LNNDRGTAIL VTASIYDACH
YFRLFQNTGF GAYCGIITSY EPNANAISKE PANSNERYKF DTYKQCVLDA FTTTEKYEAE
TRRRFIEEPA NCKLLIVVSK LLTGFDAPSC TYIYLDNEMH DHTLFQAICR TNRLDGDDKE
YGHIVDFKEL FGDVQQAIAV YNSDELDIDE GGGGENNIHL KDWLKEGKKK LDDTREALKY
LCAPVPEPRE MEQYLFYFCG NADNPNALTD TEALRVSFYK SVATFVRAFA AVSQYLAEAG
YSAAEIATLN NEVKFFSDTR AAIKKHSGEE LDIKPYEADM RHLLNTYIQA DPADPLGEMD
RYSLVELIIK TGIHDAIAKK LNEKGKLSKT AVAEGIIHNI RKTIIREQLA DPRFYEEMSK
LLDDLIKQRQ DDTKSYEEFL KQAEALVKKM SKGQPGKNIP QELHGRPEAT VIYNNLPDIL
MHLASEDMVQ DPVTGFGATR LGLALEIDRA MREHAPAGWK GDDTREKQVL NALFPLLKRN
RKATMAAFEL IKNMSGYA
//
