ID A0A1Q8E949_9STRE Unreviewed; 1018 AA.
AC A0A1Q8E949;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=BU202_03655 {ECO:0000313|EMBL:OLF48316.1};
OS Streptococcus cuniculi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1432788 {ECO:0000313|EMBL:OLF48316.1, ECO:0000313|Proteomes:UP000186890};
RN [1] {ECO:0000313|EMBL:OLF48316.1, ECO:0000313|Proteomes:UP000186890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NED12-00049-6B {ECO:0000313|EMBL:OLF48316.1,
RC ECO:0000313|Proteomes:UP000186890};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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|ARBA:ARBA00011296,
CC 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:OLF48316.1}.
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DR EMBL; MSJM01000003; OLF48316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8E949; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000186890; 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:0004386; F:helicase activity; 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 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; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
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; 1.
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 Helicase {ECO:0000313|EMBL:OLF48316.1};
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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 281..456
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1018 AA; 117255 MW; 5573EA0AE6E3A43F CRC64;
MKSQSELAFE KEVIEYLTKI GGVKQWEYKK EIKTTDDLWK NFKQILEQNN RARLEDPLTE
TEFNQVKKVI SSLDTPYKAG QFLYGVNGFS QVEVDLDNGQ HVFLTIFDQE QVGGGNTVYQ
VVNQIERPKV VDGKSNRRFD VTLLINGLPM IQIELKKELH SATEALNQME QYIAEKQYSG
IFSTLQILIA MTPHEIRYMA NTTLDKFNRA FAFHWQNEED AHRVGDWKVF ADKVLSIPMA
HELSTRYMVL DGTKNKESIK VMRPYQVYAT KRVLDKVRAF DFQYDDGKLG YIWHTTGSGK
TITSFKTAWL ASRLSNVDKV IFLVDRIALT NQTVDAYQAY DPVSSFEGKT GVVSDTANIA
DLHRKLTKKS DKNIIVTSIQ KMSRYVAKER FKPVSDHILF IVDEAHRSTG DGSENEGMLE
SIRRAFPHAA WVGYTGTPKF PETPTIFGDL LHAYTIKEAI ADKNVLGFKV EFKETIEAPE
NPTEEEIDDR IRASVYDDSP EHVDLVVKDI FEHWEDRSNN RKYNALFTVH VGGSRASTPR
AMEYFDKFAE INETKSDEDK LKVAISFSAD TSNGANQLKT NENLHRAIKA YNQLFGTTFD
MTSVKQYAED LARRLNKTAD DGKYLDLAIV VDQLLTGFDA PEMNTLYVDR TLKGGNLIQA
YSRTNRMHNL LDKPQGNVVN YRWPKQNEYE MNKAFAIYSN RSSADEQLSL DELKKGNEEA
NIISKPFGAV QVEMQEVVQH LSTLTNAFMQ LPPSEKAQDE VFEELKEYNR LLSQLKQYTE
DEEGQTISAY EDPETFYQRI GITREQEIRL TTVIAGELKE RRAKRDNIDI SQVNLAMVHI
HDVKINYDYL VDLIAKMADE IHANQMEKAK HTHQEIQVEI AKSDNEKEKS KMRHFVERIF
DRSFVFDTYP APRDVETMNA AMERVQKESH LKLVTEFIRK WGLDNSTNPR ELMKLIGKHQ
FGQEDMDRQG ELTSLMNEAR ADYKEIAEEG VAQLSWVRYR IDLRKAFYDI ADKIKQGE
//
