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Database: UniProt
Entry: G2E1E6_9GAMM
LinkDB: G2E1E6_9GAMM
Original site: G2E1E6_9GAMM 
ID   G2E1E6_9GAMM            Unreviewed;      1023 AA.
AC   G2E1E6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=ThidrDRAFT_2109 {ECO:0000313|EMBL:EGV31243.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV31243.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV31243.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV31243.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) 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:EGV31243.1}.
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DR   EMBL; AFWT01000013; EGV31243.1; -; Genomic_DNA.
DR   RefSeq; WP_007040823.1; NZ_AFWT01000013.1.
DR   AlphaFoldDB; G2E1E6; -.
DR   STRING; 765913.ThidrDRAFT_2109; -.
DR   PATRIC; fig|765913.3.peg.2147; -.
DR   eggNOG; COG0610; Bacteria.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000004200; 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   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; IPR040980; SWI2_SNF2.
DR   PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 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, ECO:0000313|EMBL:EGV31243.1};
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          302..520
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1023 AA;  115388 MW;  34192CCB8DC1820B CRC64;
     MSGHRERDFE IAIEAGLTSA GGYEKRAPTD YEESLALFPE DVTGFLQDSQ PAKWAALEAL
     LGPKTTSTVL DNLAKELELK GTLHVLRHGF KCYGKTFRMA YFRPNTRMNP EAAEQYARNR
     LTITRQVGFA SVMKKTGGGH KRCVIDLTLA VNGIPVVTAE LKNPLTGQRA TDAIHQYAQE
     RDERDLLFAF KKRALVHFAV DPDEVWMTTR LAGKETRFLP FNRGHDQGAG NPPVEGNWKT
     HYLWDEVLRA DSLLEILQRF MHLEVKEKPV KTDNGVRTLR KETMIFPRYH QLDAVRRLVA
     HAQSHGAGRN YLIQHSAGSG KSNSIAWLAH RLASLHDAQD EKVFHSVIVV TDRRVLDQQL
     QATIHQFEHK TGVVEKIDED TQQLARALSQ GTPIVITTIQ KFPFISQALS TLEKNGGGVT
     IDTAGRRFAV IVDEAHSSQS GETATALKGM LNQDGIEAAI AAQLSGEEDE ALSEEARAAV
     LRDALRRARQ PNLSFFAFTA TPKFKTKALF NEPGPSGAAP FHLYSMRQAI EEGFILDVLQ
     NYTTYKRFFG LIKQIEDDPD VPRKKAAKAL ARYLELHPVN IEQVVSVIVE HFRLTVMHEL
     GGRAKAMVVT GSRLAAVRYK RAFDRYIEEQ GYGGIRSLVA FSGAVEDPDD PGSSYTEVAM
     NDGLAESELP ETFERDDYRV LLVADKYQTG FDQPLLQTMY VVKRLAGVQA VQTLSRLNRT
     APGKSRTFVL DFANEEDDIY QAFKPYYETT PVGENADPHR LSELQHRLLE WAIFTPTDVD
     AFAEVWYRAK RDHSAKDHRL MNAVLDAVVE RFQEHDEEAR EEFRGQLTAY RNLYAFLSQI
     IPYQDSDLER LYAFVRNLLA KLPPPGDGQG FVLDDEVALR FFRLQQMTEG SIDLSQGEPY
     PLKGPTDVGT GGVRDEAVAL SSLIERLNER FGTDFTEADQ LFFDQIRVSA EIDEDIVEAA
     RANNFSNFAA YLDRMLDELF IARMEGNEEI FSRVMTDAEF RSAAHEHLAH EIFRRVREND
     DVH
//
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