ID F0SL90_RUBBR Unreviewed; 1030 AA.
AC F0SL90;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Plabr_4424 {ECO:0000313|EMBL:ADY61996.1};
OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Rubinisphaera.
OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY61996.1, ECO:0000313|Proteomes:UP000006860};
RN [1] {ECO:0000313|Proteomes:UP000006860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC {ECO:0000313|Proteomes:UP000006860};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL Submitted (FEB-2011) 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}.
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DR EMBL; CP002546; ADY61996.1; -; Genomic_DNA.
DR RefSeq; WP_013630701.1; NC_015174.1.
DR AlphaFoldDB; F0SL90; -.
DR STRING; 756272.Plabr_4424; -.
DR REBASE; 33836; Pbr5305ORF4421P.
DR KEGG; pbs:Plabr_4424; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_0; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000006860; 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; 3.
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 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:UP000006860};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 287..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1030 AA; 114244 MW; 4695018D3C79854D CRC64;
MTGRISEAAI ENAALNQLES LNIEVIRRGD LTPSFSSKHD LGVVLTDAIH SSIEKFNPHL
PEATIATVVV SLSRPPHSIL VENSRWFHKL LIEGVPVEYK DGETGEIRGG RARLIDFENP
ANNDFLVVRQ LAIQGPSGNK IRPDLVLYVN GLPLVVIELK DPANTTATLD MAIDQLVRYK
EIAPDLFVPN LLLVVSDGLL TRVGSITSGR QRFTPWRPEK GGEPTLEALI RELLTPAALL
DYLRSCVAFE EDERGNIVKK VAGYHQFRAV RKARESVIDA VKTPDRQNDE AAGKGGVVWH
TQGSGKSLTM LMLAGTLVRA AEMANPTVVI VTDRNDLDDQ LFHTFAMGRE LLRQEPVQAG
SREHLKQLLD RASGGVIFTT IHKFAESHGM ISERSNVVVM ADEAHRSQYG FIEGGARWMR
EALPNATFVG FTGTPLMAGD KVTRHVFGEY ADVYDIHQAV ADGATVPIYY EPRIVKLTID
EAGARKAEAT IAEAAKADEN GEEMEENIRI PLEELYGAPE RLERVAKFLV EHWEQRRSAM
EGKAIVVTMS RGIAARLYDE IAKLRPSWAD DDDDKGMLKV IMTGTPADPE HIARHVRSKA
QRKALGARFK DPADEFRLAI VVDMWLTGFD VPCAHTMYLD KPLAGHNLMQ AIARVNRVYG
AKPGGLIVDL IGLADPLADA LATYAKATGD SDKPVKELQD EAIPAMQSAF EQLRDFFHGF
DYSPALDADP RTVIRTYLGA VDHVMDVNQT VGEETGWKRF RGMVKRLSTA FALAVPREET
KEITPHLAFF QNVVRMIRKR LAEDAAPTSG TGASRDIDEA VRQVVGNAVD ADDVIDLFAA
AGLDTARLDI LSDEFLNRVC ALEQQNLALE TLRKLLTDQI KISERTNLVQ AQKFREALEN
AMLSYTNKQI STAEMIARLL ELAKWVREAK QHGHDLGLST EEIAFYDALA ENGSAKEVMK
SDKLRLMARE LAEMVKKMPK LDWTQRESVR ADLRRKVRRL LAMYGYPPDL SEDATQLVLK
QAELSTEAGA
//
