ID G7UT28_PSEUP Unreviewed; 1006 AA.
AC G7UT28;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 OrderedLocusNames=DSC_07210 {ECO:0000313|EMBL:AER56093.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56093.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER56093.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER56093.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
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}.
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DR EMBL; CP003093; AER56093.1; -; Genomic_DNA.
DR RefSeq; WP_014160269.1; NC_016147.2.
DR AlphaFoldDB; G7UT28; -.
DR STRING; 1045855.DSC_07210; -.
DR REBASE; 41730; Psp59ORF7230P.
DR KEGG; psd:DSC_07210; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000005870; Chromosome.
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; 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 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:UP000005870};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 261..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1006 AA; 114625 MW; 3FDAB36301C2F17D CRC64;
MHVKESSIEQ ELIDKLGELK YTLRPDIRDR AAMERNFREK FQALNRVSLT NAEFQRLLDE
IVTPDVFKAA QTLRHRNAFT RDDGTPLNYT LVNINDWCKN DFEVASQFRI NTEYSYHRYD
VLLLINGVPA VQIELKTLGI NPRRAIEQIV EYKNDPGNSY TRTLLCFIQL FIVSNRDFTY
YFANNNARHF AFNADERFLP IYQYAAPDNT KINGIDAFAE AFLAKCTLGQ MISRYMVLVA
SEQKLLMMRP YQIYAVKNIV ECIDKNLGNG YIWHTTGSGK TLTSFKASTL LKANPAIEKC
LFVVDRKDLD RQTREEFNRF QQGCVEENTN TGALVRRMLS DDAADKVIVC TIQKLGLALD
ENSKRNRSRE RRGLASHTEQ LEALRDKRIV FIFDECHRSQ FGDNHQAIKE FFPKAQLFGF
TGTPIFEANA SYKRIEGEEQ TLKTTEDLFQ QSLHEYTITH AIEDRNVLRF HVDYYKPDGK
RPPKPGETLA KRAIVDAILA KHDTATGGRR FNAILATASI NDAIEYFKLF AVAQAEKQQA
DPHWQPLNIA AVFSPPADVS PDVRQLQEDL PQEQEDNKHD PEAKKNALKA IIADYNARFS
TNHRIEEFDA YYQDVQQRIK DQQFPNADLP HKGREKLDIV IVVDMLLTGF DSKYLNTLYV
DKNLKHHGLI QAFSRTNRVL NDTKPYGNIL DFRGQQKEVD AAIALFSGAK ADKAREIWLV
DTAPVVIDKL KDARGRLDRF MASQGLSGKP DDIANLKGDA ARAAFVEHFK QVQKLKVQLD
QYTDLTPEQA QQIDQVLPRD EHNAFRGAYL ETAQRLRAQQ AKWSGQKDGA ADEQIDQLDF
EFVLFASSTI DYDYIMKLIA DYSAKAPGKA SMSREQLIGL IASDAKFMDE REDISEYVRG
LKAGEGLNEA AIRAGYERFK QDRAAQEMAA LSDKHGLPVT ALRAFVDAIL ARRIFDGEQL
TELLSPLDLG WKARTQKELA LMGDLLPLLN KRAGGREIAG LKAYEE
//
