ID D2NT13_ROTMD Unreviewed; 1111 AA.
AC D2NT13;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=RMDY18_09570 {ECO:0000313|EMBL:BAI64789.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64789.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64789.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64789.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64789.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64789.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
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; AP011540; BAI64789.1; -; Genomic_DNA.
DR AlphaFoldDB; D2NT13; -.
DR STRING; 680646.RMDY18_09570; -.
DR REBASE; 23245; RmuORF9550P.
DR KEGG; rmu:RMDY18_09570; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_1_11; -.
DR Proteomes; UP000001883; 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; 1.20.58.2040; -; 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:UP000001883};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 358..520
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1111 AA; 126661 MW; 7FFFE5D202AE73EE CRC64;
MQRSTPVETV PDYSHPTEGF TERILSSDTF TVLGDRTEAP HYDEWAKANE KRKGLQTEAQ
LEAELIDTLR DQGYEYLSNL TDETALIRNL REQLERFNTR PEEGAYGPNS GFHFTDEEFD
RLLTEHLARS NDGILEKAKL IQEERFIDFR LDDGTLRNIM LIDAVYPARN RMQVVNQYRV
PAANGKTRNR YDVTILVNGL PLVHIELKKR SVGIQEAFQQ IERYQGAGFQ EDTHRFFEYA
QIFIISNGVK TKYYSNTVRH KHIEDLQEVR RKNPSGGSAG KSFEFTSYWA DAKNNRISDL
MLFARTFLAK NALANILTRY CILTVDQDLL VMRPYQIAAT ERIINCVKTA DKSKNSDKTF
GTKKAGGYIW HTTGSGKTLT SFKTARRLAE TGLVEKVIFV VDRKDLDYQT MLEYNNFQAD
SVSSSSSTRQ LSDRLADRGT SIVVTTIHKL SNLTNAEPKH PVYGQRVAII FDECHRSQFG
QMNANIKKYF KNYCMFGFTG TPIFDGNSAG GPGTTTGEVF GECLHTYTVV DAIRDGNVLP
FHLEYTNTSP TFACLEESVY AEEIAAERAA TPDAKELEKL AKAKAVLESP ERIEAIATYI
LDNYDRKTNQ KERDYDLKKS RTINKVTEHY VERVRGFNSI LATSSIDAAC TYYDALNTLQ
EERIAEGVLD PAKKLKVAII YSQGNGGQLI DTFGEGENYE FPTGDTGSRM DGFLEDYNTM
FGTNFSTDGD SFDNYYKDVS RRMKVRELDL LIVVNMFLTG FDSKTVNTLW VDKNLKMHGL
VQAYSRTNRI FNSVKRSGNV VCFRDLEQAT KDAFTLFGDT ENSDGQSALD IAFTRPYKEA
FEEYREAVTT LREEFGMDEG GSITVDTPEE KARYIKLMND VLELRQELRV HDEFIRDGGD
ELISDYDMQG YTGVYNDIYD EIREMRKARE EGTDEGEDRT DDVDLFANVH FLTELVKQQE
IGVDYILALI EAAHESNSDA TEDIERAVNS SSELRASADI ITDFSKEYRN TPNPGDVYEH
FNRYVTERRS REEDEIVRDE NLDPEETQRV VNRALKEGRR TISGKFTSLI KVKMPIFGGD
PSSEDAVSKT KRVKQRLEKH LDRFMSLLGG R
//
