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Database: UniProt
Entry: A0A259U7Y5_9FIRM
LinkDB: A0A259U7Y5_9FIRM
Original site: A0A259U7Y5_9FIRM 
ID   A0A259U7Y5_9FIRM        Unreviewed;       711 AA.
AC   A0A259U7Y5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   Name=hsdR_2 {ECO:0000313|EMBL:OZC14239.1};
GN   ORFNames=SPSIL_49660 {ECO:0000313|EMBL:OZC14239.1};
OS   Sporomusa silvacetica DSM 10669.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=1123289 {ECO:0000313|EMBL:OZC14239.1, ECO:0000313|Proteomes:UP000216752};
RN   [1] {ECO:0000313|EMBL:OZC14239.1, ECO:0000313|Proteomes:UP000216752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10669 {ECO:0000313|EMBL:OZC14239.1,
RC   ECO:0000313|Proteomes:UP000216752};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Sporomusa silvacetica DSM 10669.";
RL   Submitted (FEB-2016) 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:OZC14239.1}.
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DR   EMBL; LSLK01000117; OZC14239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259U7Y5; -.
DR   REBASE; 234780; Ssi10669ORF49640P.
DR   Proteomes; UP000216752; 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; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OZC14239.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216752};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          289..496
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          421..455
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   711 AA;  81637 MW;  15931C214C1DD4BF CRC64;
     MDDNLKEKAF EEAIEEYLIT QGGYKKGNPS KFDRTTALAQ DTLLSFIKVT QPKKWEKYCT
     IYGSAAEDSF IKRFSKEVQV NGLLHVLRHG FKDRGILFKV CFFKPETSIN KDTMKLYEQN
     ILHCTRQLHY SVLNKNSIDI VLFLNGIPVV SLELKCQFTG QSAYNAINQY KFDRASKDAI
     FDFRNRVLVH FAVDLYEVYM TTRLNGDSTY FLPFNQGSNG AGNVGGKGNP LRQQGYQTAY
     LWEHVLCKDR LLEILHKFMH LKIDDKQAET LIFPRFHQLD VVTKLIVDVK ENGAGKNYLI
     QHSAGSGKSN SIAWLAYRLS GLHNIQDEKI FHSVIVVTDR KILDSQLQET IYQFDHVLGV
     VECIDEKKHA VDLRNAINAN KKIIITTLQK FPVIYEEVEK DGKSFAIIVD EAHSSQTGEA
     SKKLKKALGN IEEALEEYRQ MESEAEENTK DEEDKLVEEL TTHGQIPNLS FFAFTATPKA
     KTLQLFGEKQ KDDTYRAFHI YSMRQAIEEH FILDVLKNYT TYNMYYKIAK KVADDPALDA
     SKATKEISKY ESLHPHNLAQ KTAIIIEHFR NITKNKISGQ AKAMVVTASR LHAVRYLFEF
     RRYIKAKAYD DLDVLVAFSG TVKDNSAEWT EEKINIDKQG HPIKEKQLKR HFNSPDFNML
     IVAEKYQTGF DEPLLHTMFV DKKLTGVKAV QTLSRLNRTM KGKKDTFVLD S
//
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