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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//