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
//