ID R7LJZ8_9BACT Unreviewed; 953 AA.
AC R7LJZ8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BN805_00432 {ECO:0000313|EMBL:CDE87662.1};
OS Prevotella sp. CAG:891.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262937 {ECO:0000313|EMBL:CDE87662.1, ECO:0000313|Proteomes:UP000018147};
RN [1] {ECO:0000313|EMBL:CDE87662.1, ECO:0000313|Proteomes:UP000018147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:891 {ECO:0000313|Proteomes:UP000018147};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE87662.1}.
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DR EMBL; CBJT010000240; CDE87662.1; -; Genomic_DNA.
DR AlphaFoldDB; R7LJZ8; -.
DR Proteomes; UP000018147; 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:UP000018147};
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 953 AA; 110792 MW; 0B98BEEC2154A963 CRC64;
MPVQSEAALE NGLIDTLQKM NYEYVHIEEG QNLSANFKKQ LEKHNKKKLE ELGRTEFTEA
EFDKILIYLE GGTRFEKAKK LRDLFPLELE SGERLWLEFL NRTHWCQNEF QVSNQITVEG
RKKCRYDVTI LVNGLPLVQI ELKRRGVELK QAYNQIQRYH KTSFHGLFDY IQLFVISNGV
NTRYFANNPN SGYKFTFNWT DAANVPFNDL EKFATVFFDK CTLGKIIGKY IVLHEGDKCL
MVLRPYQFYA VEKILDRVEN SNDNGYIWHT TGAGKTLTSF KAAQLVSELD DVDKVMFVVD
RHDLDTQTQA EYEAFEPGAV DSTDNTDELV KRLHSNSKII ITTIQKLNAA VSKQWYSSRI
EEIRHSRIVM IFDECHRSHF GECHKNIVKF FDNTQIFGFT GTPIFVENAV DGHTTKEIFG
NCLHKYLIKD AIADENVLGF LVEYYHGNED VDNADQDRMT EIAKFILNNF NKSTFDGEFD
ALFAVQSVPM LIRYYKIFKS LNPKIRIGAV FTYAANSSQD DEQTGMNTGG FASESTGEAD
ELQAIMDDYN NMYGTSFTTE NFRAYYDDIN LRMKKKKADM KPLDLCLVVG MFLTGFDSKK
LNTLYVDKNM EYHGLLQAFS RTNRVLNEKK RFGKVVCFRD LKSKVDESIK LFSNSNNLED
IVRPPFDDIK THYQELTKNF LEHYPEPHYV DYLQSENDKK QFILAFRDII KKHAEIQVYD
EFEVDAPDLG MTEQQFMDFR SKYLDIYDSF AVQNKEQPAT YQVLEDNPSM VGEPDPFEEA
ATGMGDIDFC LELLHSDIIN VAYILELIAD LNPYSEDYEE RRKHIIDTMI KDVELRSKAK
LIDGFIQRNV DDDRDNFMAR KQKADGTSDL EERLNNYIVT ERNNAVNTLA KEEDLDASVL
NHYLSEYDYL QKEQPEIIQE ALKEKHLGLI KKRKALTRIL DKLRSIIRTF SWE
//
