ID   T1RH_HAEIN              Reviewed;        1055 AA.
AC   O05052;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Type I restriction enzyme HindI endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=HindI {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
DE   AltName: Full=Type I restriction enzyme HindVIIP endonuclease subunit;
GN   Name=hsdR {ECO:0000303|PubMed:7542800}; OrderedLocusNames=HI_1285;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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'-RAACN(5)TAG-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; L42023; AAC22934.1; -; Genomic_DNA.
DR   PIR; F64114; F64114.
DR   RefSeq; NP_439437.1; NC_000907.1.
DR   AlphaFoldDB; O05052; -.
DR   SMR; O05052; -.
DR   STRING; 71421.HI_1285; -.
DR   REBASE; 1149; HindI.
DR   REBASE; 155512; VscVS05ORF3158P.
DR   REBASE; 188608; AsoACEORF2359P.
DR   REBASE; 191851; Apa1447ORF2799P.
DR   REBASE; 191855; Apa1447ORF3031P.
DR   REBASE; 191867; Apa1342ORF2943P.
DR   REBASE; 191871; Apa1342ORF3157P.
DR   REBASE; 191887; Apa1468ORF3072P.
DR   REBASE; 203813; Lbr1106ORF30P.
DR   REBASE; 231749; Sen4839ORF3820P.
DR   REBASE; 290904; Msa27082ORF3559P.
DR   DNASU; 950228; -.
DR   EnsemblBacteria; AAC22934; AAC22934; HI_1285.
DR   KEGG; hin:HI_1285; -.
DR   PATRIC; fig|71421.8.peg.1337; -.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_005762_1_0_6; -.
DR   OrthoDB; 9758243at2; -.
DR   PhylomeDB; O05052; -.
DR   BioCyc; HINF71421:G1GJ1-1311-MONOMER; -.
DR   PRO; PR:O05052; -.
DR   Proteomes; UP000000579; 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; 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; 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; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome; Restriction system.
FT   CHAIN           1..1055
FT                   /note="Type I restriction enzyme HindI endonuclease
FT                   subunit"
FT                   /id="PRO_0000077262"
FT   DOMAIN          287..468
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1055 AA;  120710 MW;  C5BEF298E7E05C67 CRC64;
     MLNENDIEQL TLQRLQSLGW EYRYGKDLPV HEGKFARGDL SGVVFVEQLR EAVRKLNPQL
     PESAVDSVVK SATKSDIGDL VVRNQTFYKL LRDGVRVEYT QNGEQKIEMV RLVDFEHWGN
     NRFVAVNQLE IRSRKGGKRI PDIIGFVNGL PLVVFELKNP LRESADLLQA FNQFETYKDE
     IAELFVYNQA LIISDGIVAR LGSLSADFQR FTPWKVVDEK NKSARLYFDD ELQSLLNGLM
     QPEDLLDYIR YFVLFERDSV GKTIKKIAAY HQYYGVNEAV DSTIWATSEK GDRRIGVMWH
     TQGSGKSISM LFYAGKLLAQ PELKNPTIVV VTDRNDLDGQ LFQTFSSGKD LIKQTPQQVE
     DRDQLRQLLA QNEVGGVFFT TIQKFALNEE ESRFPILNER NNIIVISDEA HRSQYGFTQK
     LHNGKFQTGY ARHLRDALPN ASFIGFTGTP ISLEDKDTQD VFGRYVSIYD LQDAVEDGAT
     VPIVYDDARQ IRLNKKDHDA LFAEIDALLE EEPSTSLRLR EKLLGSQERL IELAADFVQH
     FAKRNEVVDS KAMMVVSSRQ ICVDLYNQII ALHPEWHSDN INEGAIKIVM TGSASDTPEM
     QKHIYSKQEK QTLERRFKDP NDPLKVVIVR DMWLTGFDAP CCNTMYLDKP MKGHNLMQAI
     ARVNRVFANK SRENGGLIVD YVGLAKELRA ATQQYTNSTG KGQLAEDVQS VFFKMKEQLE
     FIRTLFATPI EGKTFDVQAA LEKDNPNDLL MAIRFAANHI LSLDQLSFDG KAHEQHWFNK
     KETEPRKKAF LKTAGLVKKG YMLCGTLAEV EPYNQEIAFY DAVRAILTKR EQKGTGTNER
     QILLKKLVNQ TVYSEGVIDL FDLLEKPQPQ ISLLSEEFLQ TVKNSPTKNL WVSAMERYLA
     SEIKVKSGTN LTLQKDFERR LKEALNQYHN HNLTVVEILD ELFKMSQDFQ ERLALGKKLG
     LTKEELAFYE ALSQNQSAKD LMGDEVLSKL AKEITETLRK SVTIDWQYKE AVRARIRLLV
     RRALQKYKYP PDKQEEAVTY VIKQAEEIAE DLTGL
//