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Database: UniProt
Entry: D4BRB2_BIFBR
LinkDB: D4BRB2_BIFBR
Original site: D4BRB2_BIFBR 
ID   D4BRB2_BIFBR            Unreviewed;      1039 AA.
AC   D4BRB2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE            Short=R protein {ECO:0000256|RuleBase:RU364115};
DE            EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN   Name=hsdR {ECO:0000313|EMBL:EFE88757.1};
GN   ORFNames=BIFBRE_04648 {ECO:0000313|EMBL:EFE88757.1};
OS   Bifidobacterium breve DSM 20213 = JCM 1192.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE88757.1, ECO:0000313|Proteomes:UP000003191};
RN   [1] {ECO:0000313|EMBL:EFE88757.1, ECO:0000313|Proteomes:UP000003191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE88757.1,
RC   ECO:0000313|Proteomes:UP000003191};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC       activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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         ECO:0000256|RuleBase:RU364115};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC       ECO:0000256|RuleBase:RU364115}.
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:EFE88757.1}.
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DR   EMBL; ACCG02000012; EFE88757.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4BRB2; -.
DR   KEGG; bbrd:BBBR_1459; -.
DR   PATRIC; fig|518634.20.peg.1529; -.
DR   HOGENOM; CLU_005762_1_0_11; -.
DR   Proteomes; UP000003191; 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; cd18030; DEXHc_RE_I_HsdR; 1.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   InterPro; IPR021810; T1RH-like_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
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   Pfam; PF11867; T1RH-like_C; 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, ECO:0000256|RuleBase:RU364115};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003191};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          298..473
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1039 AA;  118449 MW;  5416F8A886FFFBD4 CRC64;
     MAVSKVESRT VSECSLNNIT SMDPLNEEWY ENLIVEHLTE KLGYEHLYGP DVRRADDSYR
     DVFLPDILPD ALRRINRNLP EAAVEEAIRK IQNVEIGSLE QRNEIFNDYL QSGVEVHFFD
     GKEERDDIVR LLDFDDPENN DFHVVNQWTF VEYSEKRPDV IIFVNGMPLV LFELKSPSRE
     ETDASHAYLQ LRQYMKQIPS MFVPNVFCVM SDMTQTRVGT ITSDEDRYVA WKSADGDYSG
     TKAAAWSTMI DGMLPKERLL DIIQNFVCFN DSSEKVVKII AAYHQYFAVR KAIVRAEEAV
     NGDGRIGVFW HTQGSGKSLS MVFFAHLLQR YLESPTIVVI TDRNDLDDQL FGQFSRCARF
     LRQKAVQAES RRNLQELLEG REANGIIFTT MQKFSDGDEP LCDRSNVVVM VDEAHRGQYG
     LTERINADGH VSVGAARVVR KALPNASYIG FTGTPISTDD RNTREIFGDY IDVYDMTQSV
     EDESTKPVYY ESRVVSLHLD ENALGRIDAV YKEFADQADE ASVEKSKHDL GGLDAIFDTP
     ETIDALCRDI VDHYENNRAD VLAGKALIVA YSRPIAMKIY YRIMELRPEW KDKVGVVMTM
     SNQDPEEWFD VCGGTTHKKE MERRFKDDSD SLKIAIVVDM WLTGFDVPSL STMYVFKPMK
     GHNLMQAIAR VNRVCKGKEG GLVVDYIGIA GALKRAMKDY TSRDQHNYGD MNIAETAYPK
     FLEKLDVCRD LMYGFNYRKL IFQNSREALA DAIAEGTDWL LDLERHEDTE SFLKQCQLMN
     QALSLCKSMV SEEDAHEAAY LSVLRVQVLR LTGRGSGGGS GMTYTEFNKQ VSEILQQSVH
     ADGVLNLFEK DSVEISLFDE AFLQEVAGMK EKNIAIESLK RLIKEKVRAY GRTSVVKSQK
     FSEMLQNTLN AYLNGMLTNA QVIEELVNMA KEIMKDRDDA QKLGLSDEEM AFYDAITQPQ
     AVKDFYDNDQ LVSIARELTD AMRSNATIDW QKKESARAGM RRAIKRLLRK YKYPPEGVED
     AMKTVMEQCE LWADTKISE
//
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