ID   A0A087B3T8_9BIFI        Unreviewed;      1056 AA.
AC   A0A087B3T8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=BCUN_0183 {ECO:0000313|EMBL:KFI65688.1};
OS   Bifidobacterium cuniculi.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65688.1, ECO:0000313|Proteomes:UP000029067};
RN   [1] {ECO:0000313|EMBL:KFI65688.1, ECO:0000313|Proteomes:UP000029067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65688.1,
RC   ECO:0000313|Proteomes:UP000029067};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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:KFI65688.1}.
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DR   EMBL; JGYV01000001; KFI65688.1; -; Genomic_DNA.
DR   RefSeq; WP_033517198.1; NZ_JGYV01000001.1.
DR   AlphaFoldDB; A0A087B3T8; -.
DR   STRING; 1688.BCUN_0183; -.
DR   REBASE; 384778; Bcu10738ORF179P.
DR   eggNOG; COG0610; Bacteria.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000029067; 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   InterPro; IPR022625; TypeI_RM_Rsu_C.
DR   PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR   Pfam; PF12008; EcoR124_C; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI65688.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          293..465
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1056 AA;  120064 MW;  C5BA0C456D73BA99 CRC64;
     MYYQEESDFE EAVIKVLQQN GWQDGLLKSP SEQDLIDNWA RILYRNNKGI DRLNNQPLTS
     GEMAQVLEQV ETLGTPLALN SFINGRTVAI TRDNPADPDH LGKEISLKIY DRKEIAAGYS
     SYQIAQQPRY AAADRMLNSR RGDLCLLING MPVIHLELKR SGIPISQACN QIEKYTHEGV
     FNGIFRLVQI FVAMNPDDAV YFANPGKATF NPDFFFHWED FNNEPMADGS EVGKDSWKLF
     TEKLLNIPMA HQLIGFYTIA DHTDGILKVL RSYQYYAASA ISDRVRECKW DEPEPTPGRR
     GGYIWHTTGS GKTMTSFKSA QLIADSRDAD KVVFLMDRVE LGTQSLEDYQ AFADDADDVQ
     GTENTGDLKA KLASSDPKDT LIVTSIQKMS NIKAGYGKIT QAEIDRLGEQ RIVFIIDECH
     RSTFGDMLQD IRRSFPNALF FGFTGTPIHE ENRKQGGTTS DVFGDCLHRY SIADGIRDGN
     VLGFDPYMVT TYRDRDVRQA VALEQAKARS LDEVNADPSK SKVFYHYMDP KAVPMGPMET
     PAGEHIKGIE DFLSSSQYGI GSPHEGRVVE DILEQFPILS HGNKFHAIFA TSSIPQAIHY
     YHLLRTQAPD MHITALFDPN IDNKDGAIAK EDALVEIIGD YNRLYGKDFT IPTWGAMKRD
     IAARLAHKVP YLGVDAHRKE RLDLLIVVDQ MLTGFDSKWV NALYLDKVID YESIIQAFSR
     TNRLFGPDKP FGVIRYYRKP HTMRGYIEAA VKLYSGDRPL DLFAQKLPQN IRLMDARLEE
     ITAIFQAAGI DDFMQLPEST EACRAFAKCF IELNQFLEMA KVQGFEWGRK QYVFIDDDGN
     QETVIPRIDE HTYMVLVARY KEMFQKGVGS GVPPDTPYEL DGHITEIDTG LIDTDYMNVN
     FDKWLKTLNE HDEEWRLATQ ELHRSFATLN QDEQRYAELF LHDVESGDVQ PEPGKTFRDY
     ITEYARRDQD KRVMKIHDAF GVDVSLLEEA MALHLTADNI NEFGRFNKLM GTIDRERARH
     YYAERDGNPS ITMFAAFSQA RQDLKQFILN GGGDFG
//