ID T1RE_ECOLX Reviewed; 813 AA. AC Q47281; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-MAY-2023, entry version 100. DE RecName: Full=Type I restriction enzyme EcoEI endonuclease subunit {ECO:0000303|PubMed:12654995}; DE Short=EcoEI {ECO:0000303|PubMed:12654995}; DE Short=R protein; DE EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956}; GN Name=hsdR {ECO:0000303|PubMed:8412658}; Synonyms=hsr; OS Escherichia coli. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A58; RX PubMed=8412658; DOI=10.1111/j.1365-2958.1993.tb01675.x; RA Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.; RT "Conservation of motifs within the unusually variable polypeptide sequences RT of type I restriction and modification enzymes."; RL Mol. Microbiol. 9:133-143(1993). RN [2] RP NOMENCLATURE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). CC -!- FUNCTION: The restriction (R) subunit of a type I restriction enzyme CC that recognizes 5'-GAGN(7)ATGC-3' and cleaves a random distance away. CC Subunit R is required for both nuclease and ATPase activities, but not CC for modification. After locating a non-methylated recognition site, the CC enzyme complex serves as a molecular motor that translocates DNA in an CC ATP-dependent manner until a collision occurs that triggers cleavage. CC {ECO:0000250|UniProtKB:P08956, ECO:0000303|PubMed:12654995}. 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:0000250|UniProtKB:P08956}; CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S; the restriction enzyme has stoichiometry CC R(2)M(2)S(1) while the methyltransferase is M(2)S(1). CC {ECO:0000250|UniProtKB:P08956}. CC -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex, CC multifunctional systems which require ATP, S-adenosyl methionine and CC magnesium as cofactors and, in addition to their endonucleolytic and CC methylase activities, are potent DNA-dependent ATPases. CC {ECO:0000250|UniProtKB:P08956}. CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L18759; AAD15048.1; -; Genomic_DNA. DR PIR; I41292; I41292. DR RefSeq; WP_058649288.1; NZ_NMFU01000051.1. DR AlphaFoldDB; Q47281; -. DR SMR; Q47281; -. DR REBASE; 101118; Rga602ORF2367P. DR REBASE; 211744; RphB5ORF556P. DR REBASE; 211756; RspL182ORF1057P. DR REBASE; 976; EcoEI. DR BRENDA; 3.1.21.3; 2026. DR PRO; PR:Q47281; -. 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; cd18032; DEXHc_RE_I_III_res; 1. DR CDD; cd18799; SF2_C_EcoAI-like; 1. DR Gene3D; 3.90.1570.30; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR013670; EcoEI_R_C_dom. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR029464; HSDR_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1. DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1. DR Pfam; PF08463; EcoEI_R_C; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF13588; HSDR_N_2; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease; KW Nucleotide-binding; Restriction system. FT CHAIN 1..813 FT /note="Type I restriction enzyme EcoEI endonuclease FT subunit" FT /id="PRO_0000077258" FT DOMAIN 181..341 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 410..561 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 568..591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 195..201 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SQ SEQUENCE 813 AA; 92627 MW; A1EB1794123F0ADD CRC64; MAGVNKTHLT ETDIITKFIL PAVKDAGWDV MSQIRQEVKL RDGKIVVRGK LASRIKVKSA DIVLYHKPNL PLAVIEAKAN KHAISKGMQQ GLDYASLLDV PFVFASNGDG FIFHDKTNPQ QLESEIALSD FPTPEQLWQK YCAWKGFTQE QLPVISQDYF DDGSGKAPRY YQMQAINRTV DAVSAGKNRI LLVMATGTGK TYTAFQIIWR LWKAKNKKRI LFLADRNILV DQTKRNDFQP FGNAMTKVTG RTIDPAYEVH LALYQAITGP EEHQKAYKQV APDFFDLIVI DECHRGSASE DSAWREILEY FGSATQVGLT ATPKETEDVS NIDYFGEPVY TYSLKEGIED GFLAPYKVVR VDIDVDVQGW RPVKGQLDKY GEEIEDRIYN LKDFDRTLVI DERTMLVAQT ITDYLKRTNP MDKTIVFCND IDHADRMRHA LVVLNPEQVL KNEKYVMKIT GDDDIGKAQL DNFINPKKAY PVIATTSELM TTGVDAQTCK LVVLDQNIQS MTKFKQIIGR GTRINEKHGK LWFTILDFKK ATELFADPRF DGLPEKVLVV KPGDISDKDS DFNEQLDAEN NADGGDNDAS EAREDVADYQ VNRDKQAGNG EFHDDDENKV RKFYVNGVDV KVLAKRVQYY DSDGKLVTES FQDYTRKTML KDSEYASLDS FVRKWQDAPR KQVIIEELEQ LGILWDVLAE EVGKDLDPFD LLCHVVYGQP PLTRQERVAN VRKRNYFTKY AEPAQQVLNT LLDKYADEGV QEIEDVQVLK LKPFDTLGRP IEIIKTRFGD KKAYEQAVNE LENEIYQLPP RSA //