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Database: UniProt
Entry: A0A1T1H8I0_OCELI
LinkDB: A0A1T1H8I0_OCELI
Original site: A0A1T1H8I0_OCELI 
ID   A0A1T1H8I0_OCELI        Unreviewed;      1036 AA.
AC   A0A1T1H8I0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=BTA35_0214315 {ECO:0000313|EMBL:OOV86153.1};
OS   Oceanospirillum linum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oceanospirillum.
OX   NCBI_TaxID=966 {ECO:0000313|EMBL:OOV86153.1, ECO:0000313|Proteomes:UP000190064};
RN   [1] {ECO:0000313|EMBL:OOV86153.1, ECO:0000313|Proteomes:UP000190064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV86153.1,
RC   ECO:0000313|Proteomes:UP000190064};
RA   Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA   Mykles D.L., Maclea K.S.;
RT   "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT   ATCC 11336.";
RL   Submitted (FEB-2017) 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:OOV86153.1}.
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DR   EMBL; MTSD02000008; OOV86153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1H8I0; -.
DR   STRING; 966.BTA35_0214315; -.
DR   REBASE; 203500; Oli11336ORF214320P.
DR   Proteomes; UP000190064; 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   CDD; cd22332; HsdR_N; 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; IPR040980; SWI2_SNF2.
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, ECO:0000313|EMBL:OOV86153.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190064};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          300..476
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1036 AA;  120169 MW;  873220AC4716E586 CRC64;
     MKFNEDSRVK IPAILHLMRL GYQYLSLKDQ SWDLDTNIFP AIFKAAIGKI NPGIEAAEAG
     RLLEDVKLLL DNEDLGKAFF ERLSERSNTK LIDFESFNNN TFHVVTELTC QNGDEEFRPD
     ITLLINGMPL VFIEVKKPNN REGILAERDR INKRFQNPKF KRFANITQFM IFSNNMEYDD
     GDPEPVQGAF YTSSSYHKPV FNYFREEEIL NLTALLKPVS DDDELKVLKD SNLEVIRSNP
     EFQINKQPER PTNRICTSLL SRERLAFILR YALAYVSESD GLQKHIMRYP QLFATKAIEQ
     KLSEGVKKGI IWHTQGSGKT ALTFYNVRFL TDYFQQQHVI PKFYFIVDRL DLLQQAQREF
     TARGLTVHTI NSRDAFTRDI KATQVIHNHS GKPEITVVNI QKFKDDPDVV STKDYNVAIQ
     RVYFLDEVHR SYNPKGSFLA NLSQSDSNAI KIGLTGTPLL GDDYNSRALF GDYIHKYYYN
     ASIADGYTLR LIREEISIQY KIELQKALEE AEVKMGDVDR KLIYAHPSFV EPMLTYIVND
     FEKSRGTLND TTIGGMVICD SSEQAKQMFE IFNGVYAQHI SSPYELKDSA QALIKAAKPD
     SYAAKAKQDN KVKSAALILH DIGTKEDRKN WVENFKAGKI DFLFVYNMLL TGFDAKRLKK
     LYLGRVIRKH NLLQALTRVN RTYKDFRYGY VVDFADIRKE FDATNKAYFD ELQSELGDEM
     EHYSHLFKSQ EEIKQEIEHI KDVLFRFDTD NMEEFCNQIS QIQDRDTVLA LKKALADARS
     LYNLIRLQGE YDFLDELDFA KLNVLYRETS NHLDLLNLKN DLETGQDTSN LLNRALEDVI
     FKFVKIGEEE LVLADKLKNT LRQTREALAS NFDQQDPQFI SLKEELERLF KKKNLSEVTQ
     DEMVANIDAL NKIHDRVKEL NRQNNQLRQK YLGDAKYTRI HKRLQERQQS QSDISESERK
     IFAALAGVKQ DADEQVLNNS QVLDNESYFE RQMMPLVIGR FKKEQQIKLN ADASRYINHL
     VVAEYLKEFN TGSQAW
//
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