ID   G4E2T9_9GAMM            Unreviewed;      1025 AA.
AC   G4E2T9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=ThisiDRAFT_0618 {ECO:0000313|EMBL:EGZ49455.1};
OS   Thiorhodospira sibirica ATCC 700588.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiorhodospira.
OX   NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ49455.1};
RN   [1] {ECO:0000313|EMBL:EGZ49455.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ49455.1};
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.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL   Submitted (SEP-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:EGZ49455.1}.
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DR   EMBL; AGFD01000007; EGZ49455.1; -; Genomic_DNA.
DR   RefSeq; WP_006786627.1; NZ_MU255056.1.
DR   AlphaFoldDB; G4E2T9; -.
DR   STRING; 765914.ThisiDRAFT_0618; -.
DR   PATRIC; fig|765914.3.peg.628; -.
DR   eggNOG; COG0610; Bacteria.
DR   OrthoDB; 9758243at2; -.
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; 1.
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:EGZ49455.1};
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   1025 AA;  115077 MW;  5AE635AF133E933A CRC64;
     MGGHSELAFE TAIEAGLTSV GGYDRREATG YDETLALFPE DVIGFLQDSQ AAKWGQLEAL
     LGDKTRATVL DSLAKELEIK GTLHVLRYGF KCYGKTFRLA HFRPNSGMNP EAAAAYALNR
     LTVTRQVAFT SVMKKADGKN RRCIIDVTLS LNGLPVVTAE LKNQLTGQRA ADAVKQYKQD
     RDERDLLFAF KKRALVHFAV DPDEAWMTTR LKGKDTVFLP FNRGHDHGAG NPPVENNWKT
     HYLWDDVLAK DSLMDILQRF MHLEVKERQV KTDKGARTVR KETMIFPRYH QLDAVRKLVD
     HARAHGSGHN YLVQHSAGSG KSNSIAWLAH RLASLHDAED QKVFHSVVVV TDRRVLDQQL
     QNTIYQFEHK TGVVEKIDEN TQQLAQALSG GTPIIITTLQ KFPFISQALS TLEKKGSGVK
     ISTAGKRFAV IVDEAHSSQS GETASELRGM LNKDGIEAAI AAQLSDEEDD ALSDEAKAAI
     LRDSLKRARQ PNLSFFAFTA TPKFKTKALF DEPGPSGSSP FHEYSMRQAI EEGFIMDVLQ
     NYITYKRFFG LIKQVENDPD VPRKKAAKAL SRYLELHPVN IGQVVSVIVE HFRLYVMSEM
     GGRAKAMVVT GSRLAAVKYK LAFDRYIKDN GYCGIRSLVA FSGSVEDPDD PGSAYTEVAM
     NDGLAESELP ETFEREDYRV LLVAEKYQTG FDQPLLQTMY VVKRLAGVQA VQTLSRLNRV
     APGKARTFVL DFANEEDDIY QAFKPYYEAT PVGENADPHQ LSELQHKLLG WAIFAPDDVN
     AFAEVWYRSK RDHSASDHRV MNAVLDAAVA RFSDREEAEQ EEFRGQLTAY RNLYAFLSQI
     IPYQDSELEK FYAFVRNLLS KLPPPGDGQA FALDDEVALR YFRLQQMTEG SIELGTGKAY
     PLKGPTDVGT SAVREEPVPL SSLVEKLNER FGTDFTEADQ LFFDQITASA EENEKIVEAA
     RANNLPNFSA FLERMLDELF IDRMENNEDI FSRVMTDKEF RSAAHEHLAE EIFKRVREEK
     RTGGG
//