ID   T1RA_ECOLX              Reviewed;         810 AA.
AC   Q07736;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Type I restriction enzyme EcoAI endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=EcoAI {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
GN   Name=hsdR {ECO:0000303|PubMed:6325176}; 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=15T;
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   FUNCTION, RECOGNITION SEQUENCE, AND SUBUNIT.
RC   STRAIN=15T;
RX   PubMed=6325176; DOI=10.1002/j.1460-2075.1984.tb01850.x;
RA   Suri B., Shepherd J.C., Bickle T.A.;
RT   "The EcoA restriction and modification system of Escherichia coli 15T-:
RT   enzyme structure and DNA recognition sequence.";
RL   EMBO J. 3:575-579(1984).
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
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 subtype B restriction (R) subunit of a type I restriction
CC       enzyme that recognizes 5'-GAGN(7)GTCA-3' and cleaves a random distance
CC       away. Subunit R is required for both nuclease and ATPase activities,
CC       but not for modification. After locating a non-methylated recognition
CC       site, the enzyme complex serves as a molecular motor that translocates
CC       DNA in an ATP-dependent manner until a collision occurs that triggers
CC       cleavage. {ECO:0000269|PubMed:6325176, 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 (PubMed:6325176). The restriction enzyme
CC       has stoichiometry R(2)M(2)S(1) while the methyltransferase is M(2)S(1)
CC       (By similarity). {ECO:0000250|UniProtKB:P08956,
CC       ECO:0000269|PubMed:6325176}.
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; L18758; AAA23983.1; -; Genomic_DNA.
DR   PIR; I41291; I41291.
DR   RefSeq; WP_000819019.1; NZ_WTVB01000071.1.
DR   AlphaFoldDB; Q07736; -.
DR   SMR; Q07736; -.
DR   REBASE; 233079; Sen4024ORF3807P.
DR   REBASE; 246643; Mmy2708ORF27P.
DR   REBASE; 256764; Ssp9304ORF612P.
DR   REBASE; 969; EcoAI.
DR   PRIDE; Q07736; -.
DR   OMA; DGFIFHD; -.
DR   BRENDA; 3.1.21.3; 2026.
DR   PRO; PR:Q07736; -.
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   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Restriction system.
FT   CHAIN           1..810
FT                   /note="Type I restriction enzyme EcoAI endonuclease
FT                   subunit"
FT                   /id="PRO_0000077257"
FT   DOMAIN          183..343
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          412..575
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          578..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         197..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   810 AA;  92071 MW;  C04E673C8C1DEA51 CRC64;
     MAELNLSNLT EADIITKCVM PAILNAGWDN TTQIRQEVKL RDGKVIVRGK VAARRTVKSA
     DIVLYHKPGI PLAVIEAKAN KHEIGKGMQQ GIEYARLLDV PFVFATNGDG FIFRDATAAE
     GECLEKQITL DDFPSPAELW QKFCLWKGYT QAQLPVITQD YYDDGSGKSP RYYQLQAINK
     TIEAVSNGQN RVLLVMATGT GKTYTAFQII WRLWKSKNKK RILFLADRNI LVDQTKNNDF
     QPFGTAMTKV SGRTIDPAYE IHLALYQAIT GPEEDQKAFK QVAPDFFDLI VIDECHRGSA
     SEDSAWREIL DYFSSATQIG LTATPKETHE VSSTDYFGDP VYVYSLKEGI EDGFLAPYKV
     VRVDIDVDLQ GWRPTKGQTD LNGEVIDDRI YNQKDFDRTM VIDERTELVA RTITDYLKRT
     NPMDKTIVFC NDIDHAERMR RALVNLNPEQ VKKNDKYVMK ITGDDEIGKA QLDNFINPKK
     PYPVIATTSE LMTTGVDAKT CKLVVLDQNI QSMTKFKQII GRGTRIDERY GKLWFTILDF
     KKATELFADE RFDGIPEKVM DTTPEDIADP ESDFEEKLEE ISEHDEEQVT GVDEPPAPPY
     QVTDTDDVGP LPEEDEKKIR KFHVNGVAVG VIAQRVQYYD ADGKLVTESF KDYTRKTLLK
     EYASLDDFTR KWQDADRKEA IIHELEQQGI IWEVLAEEVG KDLDPFDMLC HVVYGQPPLT
     RKERAENVRK RNYFTKYSEA AQAVLDNLLD KYADAGVQEI ESIQVLKLKP FDSMGTLPEI
     IKTGFGDRNG YNQALSELEN EIYQLPPRSA