ID   A0A0W0VSV5_9GAMM        Unreviewed;       989 AA.
AC   A0A0W0VSV5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=Llon_0031 {ECO:0000313|EMBL:KTD23146.1};
OS   Legionella londiniensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD23146.1, ECO:0000313|Proteomes:UP000054997};
RN   [1] {ECO:0000313|EMBL:KTD23146.1, ECO:0000313|Proteomes:UP000054997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD23146.1,
RC   ECO:0000313|Proteomes:UP000054997};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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:KTD23146.1}.
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DR   EMBL; LNYK01000001; KTD23146.1; -; Genomic_DNA.
DR   RefSeq; WP_058528056.1; NZ_UGON01000002.1.
DR   AlphaFoldDB; A0A0W0VSV5; -.
DR   STRING; 45068.Llon_0031; -.
DR   PATRIC; fig|45068.5.peg.32; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000054997; 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; 3.
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};
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:UP000054997};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          289..483
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   989 AA;  112558 MW;  C36629B2017B6BEB CRC64;
     MKFTNTSEAG FESTIVYSLI DGAGYQAGSP QDYDRSHAID LIKLTDFLWL TQPEIAENLN
     LSIDSPKKTK FLHRLQGEIA KHGIINVLRK GIKHGPNNIT LFYGSPSKQN VKARELFEQN
     IFSVTRQLRY SNNETQLALD MAIFINGLPI ATFELKNKLT KQTVEDAVQQ YKNDRDPKEL
     LFQFGRCLVH FAVDDHEVRM CTHLKGKASW FLPFNKGYND GAGNPPNPDG LATDYLWKEI
     LSRDRLTDII ENYAQVIEEK DEKTGKKKYK QIFPRYHQLT AVRKLLKHTS ENGAGKRYLI
     QHSAGSGKSN SIAWLSHQLV GLEHDSKPIF DSILVVTDRR ILDKQIRDTI KSFAQVGSIV
     GHAERSGDLR RFISEGKKII ITTVQKFPFI LSEIGNEHRQ NKFAIIIDEA HSSQGGRTAS
     KMNMALSGSV SDTDDDESIE DKINELMESR KMLTNSSYFA FTATPKNKTL EIFGDPDPQP
     DGTVKHLPFH SYTMKQAIQE GFILDVLKNY TPVASFYRLI KAVEDEPLFD SKKAQKKLRK
     FVESNTHAIR EKTEIMVDHF HTHVMGHRKI GGAARAMVIT SGIDRAIEYF HAINHYLKYM
     NFPYRAIVAF SGEHEYGGQK VTEASLNGFP SNLIADRIAE DPYRFLVVAD KFQTGYDEPL
     MHTMYVDKPL SGIKAVQTLS RLNRAHPKKY DTFVLDFYNS VDAIEKAFSN YYRTTILSEE
     TDPNKLHDLQ SDLDGYQVYS SEQIEHLIEL YLNGTEREKL DPILDNCVAV YSNDLDEDGQ
     VDFKGKAKAF IRTYGFLSSI LPYNNTEWEK LSLFLNFLTP KLPTPKEDDH SLGILETIDM
     DSYRAEVQAS ISIRLADEDA ELDAVPTSAG GRKPEPEMDQ LSNIIKTFND MFGNIEWKDK
     DKIRKMIAEE IPGKVAADTA YQNAMKNSDK HNARVEHDRA LARVMVELIA DHTELYKQFS
     DNPSFKKWLG DNIFGATYQS ESQNQSEQK
//