ID   B7R239_9EURY            Unreviewed;       983 AA.
AC   B7R239;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=TAM4_1568 {ECO:0000313|EMBL:EEB74201.1};
OS   Thermococcus sp. AM4.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74201.1, ECO:0000313|Proteomes:UP000009277};
RN   [1] {ECO:0000313|EMBL:EEB74201.1, ECO:0000313|Proteomes:UP000009277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM4 {ECO:0000313|EMBL:EEB74201.1,
RC   ECO:0000313|Proteomes:UP000009277};
RX   PubMed=22123768; DOI=10.1128/JB.06259-11;
RA   Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H.,
RA   Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
RT   "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus
RT   sp. Strain AM4, Capable of Organotrophic Growth and Growth at the Expense
RT   of Hydrogenogenic or Sulfidogenic Oxidation of Carbon Monoxide.";
RL   J. Bacteriol. 193:7019-7020(2011).
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; CP002952; EEB74201.1; -; Genomic_DNA.
DR   RefSeq; WP_014122264.1; NC_016051.1.
DR   AlphaFoldDB; B7R239; -.
DR   STRING; 246969.TAM4_1568; -.
DR   REBASE; 40670; TspAM4ORF1847P.
DR   GeneID; 7418825; -.
DR   KEGG; tha:TAM4_1568; -.
DR   eggNOG; arCOG00878; Archaea.
DR   HOGENOM; CLU_005762_0_0_2; -.
DR   OrthoDB; 11429at2157; -.
DR   Proteomes; UP000009277; 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:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd18030; DEXHc_RE_I_HsdR; 1.
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};
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   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          261..435
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   983 AA;  115910 MW;  3682FD49C207E39F CRC64;
     MPAQTPEYLQ CEKPIIERLE SKGWTYRRGI EVLENENEPL LISRLKRAIV RINKVSEKEA
     EEAINLLKAA PFGVEGSRRV LDYLKNGVPV KDEETGEPKR LMLIDYENLQ NNEFLVANQV
     GYPFKTKIPD VILYVNGIPL VIIECKKLDV SWKKAYEQIK GYEKEMPELF KYVQVGVAVG
     DKPVYFPIVP WLSSVPVYEW KWGNFDPLDD LVELLKPETL LDILRYFTFY RESGGAFTKV
     LPRYMQYRAV REIVNLAVGY ARGETERNRG LIWHWQGSGK TLTMIFSAYK IKRLLGNPTI
     FFIVDRRELE RQLSGELKAV GLSFEVIDSI EKLKEVLTHA DGKRGIFITL IHKFRPEELE
     DVLTELKKKS RRQRTIMNRR DVVVLIDEGH RTQYGELAST MRSILKSASF FAFTGTPIAK
     KGRDTYATFG YKDRPYLDRY FITQSIEDGF TVKIAYQARL EEDVHLKREL LEAFLSSKLE
     EIPEEYRGRV EEKLKKRLNA IRVFLKNPKR IEMIAQDIAR HYKESVEPFK AMVVAVDRES
     CVLYKRALDK YLPRGYTEIV MTFNRDDSEV IKEYQKELEE RFPGKDMAEI RERIREDFRN
     KEIPKILIVT DMLLTGFDAP ILQTMYLDQP LKEHRLLQAI ARTNRPFIKN GENIKPFGLV
     IDYVGIFKEL KRALEIYDEV DIEGAAYSVE EIKEELRKKI AKAMGYFDGL EPGRDRETIM
     NAVETLFRNN KGEEFQRLYR EIRHHYKLLM EDRDEFREAF KWLTEVYYAY RAKVDGVPPE
     VELKADEFFR EALKFIHETV DIEEIKTDFP IMELDEEFLK KVMRERDKRK AFTNLLFSVR
     HYVNTHKGPL TEDLVEQVER IIEAWRHKKE EIEKLYEELL GIAGEIEKRS QEQRKLGLNE
     LEYAILMVLK KHVKTNTNEL IKGIRKLLKE TEGLRFPRWT EKTEVVSEVS RKIMLFIVRE
     YKEECDDIIK TRNELLEVLK RWG
//