ID D3UXZ2_XENBS Unreviewed; 1029 AA.
AC D3UXZ2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=XBJ1_0015 {ECO:0000313|EMBL:CBJ79170.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79170.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ79170.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79170.1};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
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; FN667741; CBJ79170.1; -; Genomic_DNA.
DR RefSeq; WP_012986643.1; NC_013892.1.
DR AlphaFoldDB; D3UXZ2; -.
DR STRING; 406818.XBJ1_0015; -.
DR REBASE; 24503; XboSSORF17P.
DR KEGG; xbo:XBJ1_0015; -.
DR PATRIC; fig|406818.4.peg.11; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_6; -.
DR Proteomes; UP000002045; 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; cd18030; DEXHc_RE_I_HsdR; 1.
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 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 SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 262..427
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1029 AA; 118571 MW; 7D9A28B82F02EF40 CRC64;
MSTVGQRERV TQDRIVKFFQ TELGYRYLGN LQDRDNKNID VDILTAWLKK RGISGTLIGR
VLRQLINTAA LGDGNKLYHA NKNVYNLLRY GIKEKEDVGE QHQTIWLIDW HNPEANDFAI
AEEVSIKGEN KKRPDIVLYV NGIALGIIEL KRSSVSVSEG IRQNLDNQKK EFIRDFFSTM
QLVMAGNDTQ GLSYGTIGTP EKYYLEWKER IDNPYPYRLD FHLSRICSKP RFLQLIHDFI
VFDAGVKKAC RHNQFFGVEA AKKRILQREG GIIWHTQGSG KSLTMVWLAK WIRENVPNSR
VLIVTDRTEL DAQIEKVFTG VEENIYRTKS GADLIFNLNR PNPWLICSLV HKFGHRSEAE
DDAATDEYIK ELKKSLPSDF RAKGDLFVFV DECHRTQSGK LHDAMKSILA EAVFIGFTGT
PLMKKDKKKS IEVFGSFIHT YKFDEAVSDG VILDLRYEAR DIDQYLTSQK RIDEWFEANT
QGLSRLGKTQ LKQKWGTMQK VLSSKSRLEM IVMDIRLDMM KRPRLMDGRG NAMLVCSSIH
QACTVYDLFS QTDLAGKVAI ITSYKPDSAS IKGEETGEGL TEQLAKYKTY RKMLADYFEQ
PEDKVANRVE EFETKVKQQF IDEPGQMRLL IVVDKLLTGF DAPSATYLYI DKHMSDHNLF
QAICRVNRLD GDDKEYGYII DYKDLFRSLN KAISDYTKEV FDGYDKKDID GLLKNRLEQA
RLNLDAALEM VRALCEPVKA PRNTIDYIHY FCCESGADPE LLSEKEALRL ALYQCVAKLL
RAFANIANEM TIAGYSPAQM EKIRAEVAHY EKVRDEIKLA SKDKVEMKRY EPAMRSLIDM
YIRADDSEVL IDFEEIGLLE LIIQKGAAVG EDLPEGIRKD PEAMAETIEN NVRKTIVDEN
PVNPRYYEHM SVLLDELIAL RRQNALNYQE YLEKIRDLAK KVVRPNQNTA AYPPDIDTPP
KRAFYDNFDQ NTDLAICIDK TIRDTKKADW VNDRFKEREI ANALRDETAE YKVDIDKIME
LAKAQRDYR
//
