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Database: UniProt
Entry: L0EUQ9_LIBCB
LinkDB: L0EUQ9_LIBCB
Original site: L0EUQ9_LIBCB 
ID   L0EUQ9_LIBCB            Unreviewed;      1085 AA.
AC   L0EUQ9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   OrderedLocusNames=B488_07050 {ECO:0000313|EMBL:AGA64697.1};
OS   Liberibacter crescens (strain BT-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA64697.1, ECO:0000313|Proteomes:UP000010799};
RN   [1] {ECO:0000313|EMBL:AGA64697.1, ECO:0000313|Proteomes:UP000010799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-1 {ECO:0000313|EMBL:AGA64697.1,
RC   ECO:0000313|Proteomes:UP000010799};
RX   PubMed=23408754; DOI=10.4056/sigs.3326772;
RA   Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT   "Complete genome sequence of Liberibacter crescens BT-1.";
RL   Stand. Genomic Sci. 7:271-283(2012).
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}.
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DR   EMBL; CP003789; AGA64697.1; -; Genomic_DNA.
DR   RefSeq; WP_015273124.1; NC_019907.1.
DR   AlphaFoldDB; L0EUQ9; -.
DR   STRING; 1215343.B488_07050; -.
DR   REBASE; 58213; LcrBT1ORF7030P.
DR   KEGG; lcc:B488_07050; -.
DR   PATRIC; fig|1215343.11.peg.726; -.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_010804_0_0_5; -.
DR   Proteomes; UP000010799; Chromosome.
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.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGA64697.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010799};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          292..527
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
SQ   SEQUENCE   1085 AA;  121690 MW;  2F42A4D5D326CB82 CRC64;
     MRASAHQEKH FQQYIIDRLV DQGWKLGDTK FYDTERAVYP EDLESWIKTS GQQEKWDKLE
     RLNGAKTLEV LIARLVKALE KQGTIKVLRQ GFSIAGCGLI EMTEAAPEDQ RNALIIERYQ
     ANILRVVPEL KYHPAQEFAI DLVLFINGLP VATVELKTDF TQSCEAAMDQ YRNDRLPYDS
     KTKRREPLLA FKRGAVVHFA MSDSEIMMAT KLDGENTFFL PFNKGRKDES GTVHAGNPPG
     DIKPDGNQEY PVAYFWESVC QPDAWLRIFH SFVYIEKKDV VDIQGNWLKK ETLIFPRFHQ
     WTAVNQMLAD ARQNGTGMTY LCDHSAGSGK TSTISWTAHD LVKLREDNGD AVFNSVIIVT
     DRNVLDGQLQ DAVKQIDHQF GVIAAIDRQK SSKPKSNQLS EALLAGTPIV IVTIQTFPYA
     MEAIITDKAL KGKNFAVIID EAHNSQTGST AAKLQAALGM SGQGKMSTMT VDELLEQLQK
     SRARPNNISY FAFTGTPKHS TLMLFGRPID PSQPASDDNP PKAFHLYTMR QAIEEKFILD
     VLKGYVPYKT AFNLSKQVED SKRVSGKAAK RALAQWMSLH PTNVTQKVQF IVEHFTKNVA
     HRLDGKAKAM VVTSSRAAAI RYKKAFDRYI EQHSEYGFIH SLIAFSGKMT GKQVIHQDDG
     EFNNDVFIVD ENDVFTEQSM NPDLHGQDLR FAFDRPEYRV ILVTDKFQTG FDQPKLVAMY
     VDKKIANHVE IVQTFARLNR IAPGKDEVFI IDFVNDPENV RKAFATYDNG AHIDEIQDLN
     VVYEIKARLD EHDLYDEKDL AAFKEARFKT IRDITHTQSP QHKALYAATA GATALYNDKL
     KMLRDGMATW EAAFEKAYAK GDEAGMKSAE HHQDEYAKQI KTLIGFKSDL GHFCRTYSYI
     AQLIDFGDPE LENFAAFAKL LQKRLLHEAP EIVDLTGLVL TGFDINARQD KTEDEGEAPV
     LKPTGAGGGG VAGDKPKFVK EIIERLNSLF GEATPIQDQV AFVNQISSIT GESDVVMAQV
     ESNTREQAMK GNLPGAVQQA VVRALSSHQK LATQVLKSDR QGMSALVDVI YDLLRGATNI
     DLDAD
//
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