ID D3PM95_MEIRD Unreviewed; 1042 AA.
AC D3PM95;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Mrub_2450 {ECO:0000313|EMBL:ADD29201.1};
GN ORFNames=K649_10280 {ECO:0000313|EMBL:AGK05348.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK05348.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:ADD29201.1, ECO:0000313|Proteomes:UP000006655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC {ECO:0000313|EMBL:ADD29201.1};
RX PubMed=21304689; DOI=10.4056/sigs.1032748;
RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Meiothermus ruber type strain (21).";
RL Stand. Genomic Sci. 3:26-36(2010).
RN [2] {ECO:0000313|EMBL:AGK05348.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK05348.1};
RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA Eichler E., Turner S.W.;
RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT Sequencing Data.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGK05348.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC {ECO:0000313|EMBL:AGK05348.1};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) 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; CP001743; ADD29201.1; -; Genomic_DNA.
DR EMBL; CP005385; AGK05348.1; -; Genomic_DNA.
DR AlphaFoldDB; D3PM95; -.
DR STRING; 504728.K649_10280; -.
DR REBASE; 24772; Mru1279IP.
DR KEGG; mrb:Mrub_2450; -.
DR KEGG; mre:K649_10280; -.
DR PATRIC; fig|504728.9.peg.2119; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000006655; Chromosome.
DR Proteomes; UP000013026; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 306..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 906..943
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1042 AA; 117396 MW; 710C93C135C62B7A CRC64;
MAQMTESVVE EAALAWLEAA GWQVVHGPEI APDQPQAERA DYGQVVLEQR LRDALVRLNP
GLPAETLEDA SRKLTQPEGS DLIQRNRALH RLLVNGVNVE YRDKDGEIRG AQARVIDFDN
PANNDWLAVN QFSVVERGTL QRAPSMQRAS TRRPDVVLFV NGLPLAVVEL KNAADEDATI
WTAWQQLQTY QAEIPSLFVP NAVLVISDGV EARVGVVGAG REWFKPWRTV AGDRLADSHV
PELQVVLEGV FAPRRFLDLV RDFIVFEDDG SGRLIKKMAG YHQFHAVQVA VQETLRAALA
LREGRGGQSG DRRIGVVWHT QGSGKSLTMA FYAGRIIREP AMENPTLVVL TDRNDLDDQL
YSTFARCHEL LRQPPVQAES RAHLRELLSV QSGGVVFTTI QKFMPEEKGD RHPRLSERRN
IVVIADEAHR SQYDFIDGFA RHMRDALPNA SFIGFTGTPI ELQDANTRAV FGDYISIYDI
QRAVEDGATV PIYYESRQAK LDLPEELKPK IDEEFEEVTE GEELERKEKL KSKWAQLEAI
VGAERRLRLV AKDIVQHFEQ RLEALDGKAM IVCMSRRICV ELYREIVRLR PQWHHDDDDK
GAIKIVMTGS ASDPPDWQPH IRNKPRREAL AKRFRDPEDA FKLVIVRDMW LTGFDAPSLH
TMYLDKPMRG HGLMQAIARV NRVFRDKPGG LVVDYLGLAT ELKAALATYT ESGGTGRTAL
NQEEAVALMR EKYEICRGLF YGFDWSRWVT GTPAERLSLL PAAQEHILAQ ENGKDRLLRA
ARELSQAFAL AVPHEEALRI RDDVAFFQAV QAVLAKRAPG QARPEEELEQ AVRQIIARAV
APEGVVDIFA AAGLKRPDIS ILSDEFLSEV RGMPQKNLAV ELLQKLLKGE IRARGQKNLV
QARSFAEMLE RTIRRYQNRA IEAAQVIEEL IALARDMREA NARGEKLGLS EDELAFYDAL
EANDSAVKVL GDATLREIAR ELVQTVRNNV TLDWTLRENV RAQLRVLVKR TLRKYGYPPD
KQEKATQTVL EQAALLSAQW AA
//
