ID A0A0F2RPR1_9PROT Unreviewed; 1007 AA.
AC A0A0F2RPR1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=VR70_06970 {ECO:0000313|EMBL:KJS39991.1};
OS Rhodospirillaceae bacterium BRH_c57.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae.
OX NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS39991.1, ECO:0000313|Proteomes:UP000033468};
RN [1] {ECO:0000313|EMBL:KJS39991.1, ECO:0000313|Proteomes:UP000033468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS39991.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS39991.1}.
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DR EMBL; LAEA01000098; KJS39991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RPR1; -.
DR STRING; 1629718.VR70_06970; -.
DR PATRIC; fig|1629718.3.peg.746; -.
DR Proteomes; UP000033468; 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; 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; 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, ECO:0000313|EMBL:KJS39991.1};
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 267..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1007 AA; 113143 MW; B4B4FA0E2C182D8E CRC64;
MGMEWLLAEK PTITCLEGMG YVFVPPSEHA ALRDGDNQVL FRAYLVDALK RINGIGDADA
NAVYADLVSV ADNERWLSIL RGDFSRPVEG EARHRTIRVL DFLNPANNVF TVTHQFRVKA
ENTRIPDVVV HVNGIPLVVI ECKSPINAKD KSGEAFEQIR QYERDIPRLF LSNCFNIVTD
GTNCLYGATG SPSKFFGSWR DPWPRTAAEF ADALSLGLWS LLEPSRLLDL IAHFIVFERT
NDGGGAKVVK KMCRYQQFRA VNKIVDRVAE GKHRRGLVWH TQGSGKSLTM VYAALKLKTH
RTVSSPDLAN PNIMVLTDRV DLHNQISGTF TACGLPNPLV VDSIGDLHKL IHSGTDGLTI
LATIFKFQGS EKPIPNSANW IVMVDECHRT QEKDLGAFLR KTLPDARFFG FTGTPVKKTD
RDTYREFGVV GEGYLDKYGI DDAVADGATV PIFYTGRKTD WHIDEAKIDI LFDQWFADLP
DDQLAALKKK GVSVADLVKH PRRIALIAFD IWTHFKAYAR PDGFKAQVVA IDREAVILYK
RALDTVIAED LMRDGMTEDD AKVEAAALSA CVYSASQEDG KPSEDKRIED IRSGLRAYYL
DADAETQVKD RFGTRGERPD FLIVCDKLLT GFDAPIESVM YLDKPLQEHG LLQAIARTNR
VSDARKRNGL IVDYIGVSNH LDDALASYRA DDIKNAMRNI DDLRNQLRSA HAEVMRMMKG
LKRSGTLFKD DLKAEFDALV ILLKGEDQWF IFKSKVREFI AAYEAVSPDP AVLEFKDDLK
WLATFLRYAT QVFEKRETFD QADYSRKIRD MLDQHLDATG LSVTVKLRHI TDPDFWEDFD
TDGKSEADIK EAAIRKTTEL RRTVTEKIGQ NEHQYGKFSD RLRELLKRMD AAQLSWAEVL
KEAEDLAKDI QAEDTAHEGT GLSQGAYGVL QVIASFGEDA DGEGLATAIA DLYESDDAAP
RLWQEKEGLR KSLRQQVRML ANDAGFTALR DLPVQVEDFA LKHFAKP
//
