ID A0A1Q5PJW7_9ACTO Unreviewed; 1041 AA.
AC A0A1Q5PJW7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=BM477_07280 {ECO:0000313|EMBL:OKL46225.1};
OS Boudabousia marimammalium.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Boudabousia.
OX NCBI_TaxID=156892 {ECO:0000313|EMBL:OKL46225.1, ECO:0000313|Proteomes:UP000186465};
RN [1] {ECO:0000313|Proteomes:UP000186465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15383 {ECO:0000313|Proteomes:UP000186465};
RA Meng X.;
RT "Actinomyces gypaetusis sp. nov. isolated from Gypaetus barbatus in Qinghai
RT Tibet Plateau China.";
RL Submitted (NOV-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|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:OKL46225.1}.
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DR EMBL; MPDM01000009; OKL46225.1; -; Genomic_DNA.
DR RefSeq; WP_075362034.1; NZ_MPDM01000009.1.
DR AlphaFoldDB; A0A1Q5PJW7; -.
DR STRING; 156892.BM477_07280; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000186465; 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.
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:OKL46225.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000186465};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 257..459
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
SQ SEQUENCE 1041 AA; 119840 MW; 2D0A7C0886B63291 CRC64;
MVFANEAEFE NAVVAALLTK GWKELIQNPT EQDLINNWAN ILFQNNNTRD RLNDAPLTET
EMAQILEQVT QLRTPLKLNG FINGKTISIQ RDNPADPEHQ GKEISLKIFD PLEISGGQST
YQIVQQPRFA TDRHFPNRRG DLMLLINGMP VIHLELKHTG VDTKQAANQI AKYSREGVFT
GIFSLVQIFV AMSPEETIYF ANPGPDGKFN PDYYFHWADF NNEPVNKWED IVSGFLYIPM
VHQLIGAYTV ADDTDGMLKV MRSYQYYAAS RISDRVSKIK WGEGNQLGGY IWHTTGSGKT
MTSFKSAQLI ADSKDADKVV FLMDRIELGT QSLMEYRGFA AATQEVQETE DSHVLISKLK
SSKPQDTLIV TSIQKMSLVN NEDSAKLSDL REINKKRVVF IVDEAHRSTF GEMLAIIKRT
FPRAVFFGFT GTPIHMQNQR KHSTTATIFG DELHRYSIAD GIRDGNVLGF DPTLVETVRS
KDLREKVARI QAGVCDEDAP ITDPDQLEIY YHFMDTKAVP MAGTQMNNGD YVKGIEDYVK
ADLYQQTDHY QAVTKNINDN WARLSRNSKF HAILAVSSIP EAIEYYRILK ENYPHIKTTA
LFDANIDNSG EIDFKEDGLI EILEDYNERY GQDYTISSYY RFKKDVAARL AHKRPYQRIE
TEPEKQVDLL IVVNQMLTGF DSKWLNTLYL DKVMEYVDIV QAFSRTNRLF APGEKPFGSI
VYYRKPYTMK QKIEEAFELY SGNNKPGIFV EQLDQHLEHM NEGFRQITRI FTSAGIPDYS
KLPESITDCK EFARLFVIFH SHLEAALIQG FYWEKLTYKF KKPRREITVE CDYETYQILL
QRYKELDRAK SDPDTVPFDI ERHITEIDTD RIDSDYLDSR FKKYLKALAT DKATREELDE
LLDPLFSSFA TLSQEEQKYA RLLIHDIEAG EVQLVEGKTF RDYINEYQYA HQNHQVKQLV
AAFGIDEDKL TKLMNTPTTG SSLNEFGRYD DLKETVNKTA AREFFSKTRG ISLPPFKVNI
EVDKILKQFL LEGELPEEFD Q
//
