ID F3PUY6_9BACE Unreviewed; 942 AA.
AC F3PUY6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
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};
GN ORFNames=HMPREF9446_02560 {ECO:0000313|EMBL:EGF55866.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF55866.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF55866.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF55866.1,
RC ECO:0000313|Proteomes:UP000003416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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|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:EGF55866.1}.
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DR EMBL; AFBN01000049; EGF55866.1; -; Genomic_DNA.
DR RefSeq; WP_009125813.1; NZ_GL882646.1.
DR AlphaFoldDB; F3PUY6; -.
DR STRING; 763034.HMPREF9446_02560; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_10; -.
DR Proteomes; UP000003416; 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; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.910; -; 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; IPR022625; TypeI_RM_Rsu_C.
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; PF12008; EcoR124_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000003416};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 256..404
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 942 AA; 109231 MW; 3C7EC37A689484CA CRC64;
MSTQSEAALE AGLIATLRQM DYEYVQIVEE DNLYVNFKRQ LEIHNKKQLA EVGRTSFTDE
EFEKILIYLE GGTRFEKAKK LRDLYPLDMV NGQRIWVEFL NRTQWCQNEF QVSNQITVEG
RKKCRYDVTI LINGLPLVQI ELKRRGVELK QAYNQIQRYH KTSFHGLFDY IQLFVISNGV
NTRYFANNPN SGYKFTFNWT DAANHPFNEL DKFAVFFLEK CTLGKIIGKY IVLHEGDKCL
MVLRPYQFYA VEKILDRVQN SNDNGYIWHT TGAGKTLTSF KAAQLVSELD DVDKVMFVVD
RHDLDTQTQS EYEAFEPGAV DSTDNTDELV KRLQSNSKII ITTIQKLNAA VSKTWYSNKI
ETIRHSRIVM IFDECHRSHF GDSHKKIMKF FDNAQIFGFT GTPIFTENAV DGHTTKEIFG
NCLHKYLIKD AIADENVLGF LVEYYHGNEV VDNDNQARME EIAKFILNNF NKSTFDGEFD
ALFAVQSVSM LIRYYKIFKS LNPKIRIGAV FTYAANNSLD DEQTGMGTGQ YAKEGVGEAD
ELQTIMDDYN NMFGTAFTTE NFRAYYDDIN LRMKKKKADM KPLDLCLVVG MFLTGFDSKK
LNTLYVDKNM EYHGLLQAFS RTNRVLNEKK RFGKIVCFRD LKNNVDTSIK LFSNSDNSED
IVRPPFEDVK KEYKCLATEF LKKYPTPSSI DFLQSENDKK NFVLAFRDII RKHAEIQIYE
DYSEDAEDLG MTEQQFNDYK SKYLDITVGF IEPPVIPSVV AEDPVPYGNS QGLEDIDFCL
ELLHSDIINV AYILELIAEL DPYSNDYSEK RQHIIDTMIK DAGMRGKAKL IDGFIRKNVD
EDKENFMSGR SKADGTSELE ERLNQYIVSE RNKAVKDLSD DEQIPTEVLN LYIKEYDYLQ
KEQPEIIQKA LKEKHLGLIK TRKALTRIME RLRNIIRTFN WE
//