ID C2ES17_9LACO Unreviewed; 1037 AA.
AC C2ES17;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN Name=hsdR {ECO:0000313|EMBL:EEJ41377.1};
GN ORFNames=HMPREF0549_0253 {ECO:0000313|EMBL:EEJ41377.1};
OS Limosilactobacillus vaginalis DSM 5837 = ATCC 49540.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ41377.1, ECO:0000313|Proteomes:UP000004483};
RN [1] {ECO:0000313|EMBL:EEJ41377.1, ECO:0000313|Proteomes:UP000004483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ41377.1,
RC ECO:0000313|Proteomes:UP000004483};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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|ARBA:ARBA00011296,
CC 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:EEJ41377.1}.
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DR EMBL; ACGV01000018; EEJ41377.1; -; Genomic_DNA.
DR RefSeq; WP_003716898.1; NZ_GG693413.1.
DR AlphaFoldDB; C2ES17; -.
DR STRING; 1423814.HMPREF0549_0253; -.
DR REBASE; 440815; Lva49540ORF254P.
DR PATRIC; fig|1423814.6.peg.1764; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_2_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000004483; 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; 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 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; 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 282..451
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1037 AA; 120190 MW; D4BC385C38902ADB CRC64;
MTVEHKELEF ENKLINHLVN LGGSKQWEYR PEIKTTPQLW DNFKQILERN NQDRLEQPLS
DNEFNQVKSI ISKLNTPYEA GQFLYGINGI SQVEIDRDDG KHVYLTIFDQ DQIGAGNTVY
QIVNQIERPA VIPGRKERRF DITLLINGLP IIQIEEKADG HRVSEALNQM HQYIDEEQYT
DIFSTLQILV AMTPHDARYM ANTTSDKFNT DFAFEWQRAN DNKIVSDAYE FANSMLSIPI
AHQMATNYMI LDGTPHHQMI KIMRPYQMYA TKRVIEKIRN HQFGYEDQRI GYVWHTTGSG
KTISSFKAAW LASRLPNVNK VVFMVDRVAL TNQTVDEYKA YDPENTEDSN GGVVTDTANR
WALSHKLRKK GKGIIVTSTQ KMDAMVRNKD FKPVDQNIVF IVDEAHRSTS GDMLKRIKEA
FPKSAWVGYT GTPVFPDKNG KSNGPTTQEI FGDVIHIYTI QDAIKDGNVL GFKVDFRTTL
TDQVMKDEYL PKYFQYRYPK MSAEDIQDRI NNLHDEDMDD MIEPSVYDEN QQHVKKVVQD
IIEHWDRRSV HGKYNAILTT HVGGGRPSTP MAMMYYREFK RQNKNAAHPL RVGITFSWDT
SNSNGQLDTN NSLREAITDY NQMFGTSFDD NSVKEYTEQV VSRLNGTIDD GKYFDIVIVV
DQLLTGFNAP QLNTLYVDRT LRGSALIQAY SRTNRVYDNQ TKPYGRIVNY RWPVHTEKLM
DDALEEYANR QSANIQLKID DINDDSGILA PSFGKVKKKL HQIVDRLANF TDDFKEIPAS
ENERGQMLQD LRQYNHWMAL AKQDDLYDEK KPEKLLKELG MSIDDEEMLT TTLSNQLKDK
IVADRKLLDV SQINLQMERV KEVKVNWDYL EELIAEVLNK YHDQDIEGAK KSAQQVQEIS
DQLEDRSYAD KIKRFIKSIF KNKVKSYNYP VKQNHIHSLI DKNNENNMRS EIFDYKKKWG
LADIEDAQLV NKIIENHVVG ADDLNSAGEL DSIVREAQAV YKTDAEADEV KKLSRFKYRT
HLRRNMMEFA DKLKKDY
//
