ID A0A1Y4S5D9_9FIRM Unreviewed; 1055 AA.
AC A0A1Y4S5D9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=B5E77_12325 {ECO:0000313|EMBL:OUQ25086.1};
OS Lachnoclostridium sp. An131.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965555 {ECO:0000313|EMBL:OUQ25086.1, ECO:0000313|Proteomes:UP000199743};
RN [1] {ECO:0000313|Proteomes:UP000199743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An131 {ECO:0000313|Proteomes:UP000199743};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ25086.1}.
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DR EMBL; NFLI01000014; OUQ25086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4S5D9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000199743; 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; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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:OUQ25086.1};
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:UP000199743};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 310..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1055 AA; 120871 MW; 2EB08A3A47D61935 CRC64;
MSTYNIVLST NESTVVTEYE PQTKRSDAYQ SEAALEQAFI RMLCEQGYEY VTIHNSDALI
ANLRRQLELL NDYQFTDKEW DSFFKSKIAN ANEGIVQKTR KIQEDYVQNL TREDGTTMNI
SLIDKKNIHN NRLQVINQYE ESGGTHDTRY DVTILVNGLP LVHVELKRRG VAIKEAFNQI
NRYQRDSFWA GCGLYEYVQI FVISNGTFTK YYSNTTRASH IKENDRTGRK NSKKTSNSFE
FTSYWADGNN KVIADLVDFT KTFFAKHTIL NILTKYCVFT SEELLLVMRP YQIVATERIL
NRIEVSTNYK KTGTIEAGGY IWHTTGSGKT LTSFKTAQLA TGLPYIDKVL FVVDRKDLDY
QTIKEYDRFE KGAANGNKST AVLQRQLEDS TSRIIVTTIQ KLDVFITKNK THPIYNKHVV
LVFDECHRSQ FGQMHTNIIK HFKNYHIFGF TGTPIFAVNA GTGGNPELRT TEQAFGAKLH
TYTIVDAIND GNVLPFRIDY INTIKQKDSD KDKQVNAIDT EEALASQERI SEVVKYILEH
FDQKTMRNSY YSLKGQRVNG FNSMFAVSSI PVCKKYYLEL KKQIAEQHRE LTIATIFSFA
PNEADTADGI LEDESFDTEG LDQSSRDFLE MAISDYNKIF KTNFDTSSKG FQDYYKDLSD
KVKKREVDLL IVVNMFLTGF DATTLNTLWV DKNLKMHGLI QAFSRTNRIL NSVKTFGNIV
CFRDLEEATN DAIALFGDKD ANGIVLLKSY EDYYYGCVDD KGREQKGYEE RIAELLQKYP
LGQPIIGEQN KKDFIVLFGN ILRLRNILSA FDRFAGNEIL SPIDFQDYTG TYHDVYDEIK
PKPGSKDSIM DDVVFEMELV KQVEVNIDYI LMLVAKYHDG NCEDKEILVA IDKAIKSSLQ
LRSKKELIKN FIATINTSTD VNADWQRFVR EQRETDIQTL ITEEKLKPEE TRKFVENAFR
DGVLKTTGTD VDRLMPPVSR FGGGGSRDKK KQTVIEKLKA FFEKYFGLLN PTETITGSKV
VDYQYTTPQS SLGMVAEEPE PYGKRKTLPP TLPVC
//
