ID E1IY27_ECOLX Unreviewed; 1038 AA.
AC E1IY27;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:EFO55755.1};
GN ORFNames=HMPREF9348_05127 {ECO:0000313|EMBL:EFO55755.1};
OS Escherichia coli MS 145-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO55755.1, ECO:0000313|Proteomes:UP000003691};
RN [1] {ECO:0000313|EMBL:EFO55755.1, ECO:0000313|Proteomes:UP000003691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO55755.1,
RC ECO:0000313|Proteomes:UP000003691};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO55755.1}.
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DR EMBL; ADWS01000048; EFO55755.1; -; Genomic_DNA.
DR RefSeq; WP_000149672.1; NZ_ADWS01000048.1.
DR AlphaFoldDB; E1IY27; -.
DR Proteomes; UP000003691; Unassembled WGS sequence.
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; 1.10.10.2110; -; 1.
DR Gene3D; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 294..439
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1038 AA; 120215 MW; 9082BA5E64DE7054 CRC64;
MTHQTHTIAE SNNFIVLDKY IKAEQTGDSY QSESDLEREL IQDLRNQGYE FISVKSQSAM
LANVREQLQN LNGVVFNDSE WRRFTEQYLD NPSDGILDKT RKIHIDYICD FIFDDERLEN
IYLIDKKNLM RNKVQIIQQF EQTGSHANRY DVTILVNGLP LVQIELKKRG VAIREAFNQI
HRYSKESFNS ENSLFKYLQL FVISNGTDTR YFANTTKRDK NSFDFTMNWA KSDNTLIKDL
KDFTATFFQK HTLLNVLVNY SVFDVSQTLL VMRPYQIAAT ERILWKIKSS FTAKNWSKPE
SGGYIWHTTG SGKTLTSFKA ARLATELDFI DKVFFVVDRK DLDYQTMNEY KRFSPDSVNG
SENTAGLKRN LDKDDNKIIV TTIQKLNNLM KAESDLPVYN QQVVFIFDEC HRSQFGEAQK
NLKKKFKRYY QFGFTGTPIF PENALGSETT ASVFGRELHS YVITDAIRDE KVLKFKVDYN
DVRPQFKSLE TETDEKKLSA AENQQAFLHP MRIQEITQYI LNNFRQKTHR TFPGSKGFNA
MLAVSSVDAA KAYYATFKRL QEEAANKSAT YKPLRVATIF SFAANEEQNA IGEISDETFD
TSAMDSSAKE FLDAAIREYN SYFKTNFSTD SNGFQNYYRD LAQRVKNQDI DLLIVVGMFL
TGFDAPTLNT LFVDKNLRFH GLMQAFSRTN RIYDATKTFG NIVTFRDLER STIDAITLFG
DKNTKNVVLE KSYAEYMEGF TDAATGEAKR GFMAVVSELE QRFPDPASIE SEKEKKDFVK
LFGEYLRAEN ILQNYDEFAT LKALQQIDLS DPVAVEKFKA EHYVDDEKFA ELQTIRLPAE
RKIQDYRSAY NDIRDWQRRE KEAEKKEKST TDWDDVVFEV DLLKSQEINL DYILGLIFEH
NRQNKGKGEM IEEVKRLIRS SLGNRAKEGL VVDFIQQTNL DDLPDKASII EAFFTFAQRE
QQREAEALIK EENLNEEAAK RYIRTSLKRE YATENGTELN ETLPKLSPLN PQYKTKKQTV
FQKIVTFIEK FKGVGGQI
//
