ID Q2YIX0_BRUA2 Unreviewed; 967 AA.
AC Q2YIX0;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
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 Name=hsdR {ECO:0000313|EMBL:CAJ12561.1};
GN OrderedLocusNames=BAB2_0395 {ECO:0000313|EMBL:CAJ12561.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12561.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ12561.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ12561.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ12561.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2YIX0; -.
DR STRING; 359391.BAB2_0395; -.
DR REBASE; 11672; BmeAORF397P.
DR KEGG; bmf:BAB2_0395; -.
DR HOGENOM; CLU_005762_0_0_5; -.
DR Proteomes; UP000002719; Chromosome II.
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; 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; 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 Helicase {ECO:0000313|EMBL:CAJ12561.1};
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:UP000002719};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 274..438
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 967 AA; 108003 MW; 277C47F59A12A55D CRC64;
MLFDYKPLSP EDVRRLRDGL ATEPVLTLRL AECLTRLNPW LDDDGVRRAV AAVTRVTAVD
VMEANESAYT ALTYGVTAPH TEGGRRQDRN MRFFDFDDPS ANTFEFARQV AIKGARQDII
PDIVVYVNGL PLAAIECKSP SLADPMGEAI RQFRRYENRD EFAGLGAPRL FETAQISIAL
ARDVAKYGTT LTPARQWAEW KDPYPLTLDA LAAQLGRTPT GQDILLAGLL APANLLDLIR
NFVVFETIGG RRIKKLARYQ QFVAVGKAIE RIRTAPNPQR RGGVIHHTQG SGKSLTMVFL
ATKLRRLPEA ENPTIVIVTD RTDLDDQITG QFQRSGFANP IQAESGDSLR KALSGGAGTT
VLTTVHKFHS AVPKRSSVIS KARNVFVMVD EAHRTQYGAL AARMRAGLPN ACMIAFTGTP
IDKKDRSTRE AFGDYLHRYL IDQAVKDGAT VPIYYEMRDA RIRIDGRDFE REVRAAFPEL
SEDEIAKLRR GTGLQEKLAG APVRVEAIAQ DILSHYRSTI EPNGFKAQIV TVSRDVAVTY
VEALERLGAP ECALIMSASN NDSARLQARH LSKRDRDSKI SRFKKRDDPL KILVVCDMLL
TGFDAPIEQV LYLDAPLREH TLLQAIARVN RTADGKTYGL VVDYWGDNRR IADALDMFSD
EDGIASALRP LSEKIQLLES RHRAAIRLFE GISHQNDTAC VELLRQDDIR AKFELDFLRF
AEAMDMVLPN PKALEDPYPS DLKWLSRIRV LARRAYHEEP FDPKDYGAKV GEIITSHLFV
TGVEQLLVKF DILDPAFRPH LESLRSSDTK AAEIEHAIRQ EIHVHRDENP TAYASLWEQL
ERIVNDRREA RVSAASALTQ LEAMVGQAAD IRSGATSRSD GLNGTAAAIL PFIDNDLPDA
ERSRSAAGIT KALEEYAEVV DWQHKEDVQR QMRRSIKEQL RSLGLDAHKI EATTAKIMDV
ARARYAG
//
