T1RE_ECOLX
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-AUG-2022, entry version 96.
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; Proteobacteria; 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}.
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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 PRIDE; Q47281; -.
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 Gene3D; 3.40.50.300; -; 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 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; SSF52540; 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
