ID D7NG41_9BACT Unreviewed; 947 AA.
AC D7NG41;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=HMPREF0665_02545 {ECO:0000313|EMBL:EFI47429.1};
OS Segatella oris C735.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=563008 {ECO:0000313|EMBL:EFI47429.1, ECO:0000313|Proteomes:UP000003805};
RN [1] {ECO:0000313|EMBL:EFI47429.1, ECO:0000313|Proteomes:UP000003805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|EMBL:EFI47429.1,
RC ECO:0000313|Proteomes:UP000003805};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella oris strain C735.";
RL Submitted (FEB-2010) 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}.
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DR EMBL; GL349576; EFI47429.1; -; Genomic_DNA.
DR RefSeq; WP_004378794.1; NZ_GL349576.1.
DR AlphaFoldDB; D7NG41; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_10; -.
DR Proteomes; UP000003805; 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:UP000003805};
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"
FT REGION 755..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 109858 MW; 21BC44CA0BBE7A01 CRC64;
MPVQSEAALE NGLIATLQQM NYEYVQIEEE KNLRTNFKSQ LEKHNRKRLE ETGRTEFTEA
EFEKILIYLE GGTRFEKAKK LRDLFPLELD DGEHLWVEFL NRTHWCQNEF QVSNQITVEG
RKKCRYDVTI LINGLPLVQI ELKRRGVELK QAYNQIQRYH KTSFHGLFDY IQLFVISNGV
NTRYFANNPN SGYKFTFNWT DAANIPFNDL EKFATSFFDK CTLGKIIGKY IVLHEGDKCL
MVLRPYQFYA VEKILDRVKN SNNNGYIWHT TGAGKTLTSF KAAQLVAESD DVDKVMFVVD
RHDLDTQTQS EYEAFEPGAV DSTDNTDELV KRLHGNSKII ITTIQKLNAA ASKQWYSRRI
EEIRHSRIVM IFDECHRSHF GDCHKNIVRF FDNTQIFGFT GTPIFVENAV DGHTTKEIFG
NCLHKYLIKD AIADENVLGF LVEYYHGNAD VDNASQNRMT EIAKFILNNF NKSTFDGEFD
ALFAVQSVPT LIRYYKIFKS LDPKIRIGAV FTYASNSSQD DALTGMNTGS YVSESTGEAD
ELQAIMDDYN DMFGTSFTTE NFRAYYDDIN LRMKKKKTDM KPLDLCLVVG MFLTGFDSKK
LNTLYVDKNM DYHGLLQAFS RTNRVLNEKK RFGKIVCFRD LKSNVDASIK LFSNSNNLED
IVRPPFNEVK KNYQELTTNF LEQYPTLSSI DLLQSEKDKK LFILAFRDVI KKHAEIQVYD
EFEEDAADLG MTEQQFMDFR SKYLDIYDTF AGGCKPSEGN QMPDEDTEST ETSTESGIDD
IDFCLELLHS DIINVTYILE LIADLNPYSA DYKEKRTYII DTMIKDAELR NKAKLIDGFI
QQNVDDDRDN FMARKQKFDG TSDLEERLNN YITTERNNAV DRLAKEEGLD VSVLNHYLSE
YDYLQKEQPE IIQEALKEKH LGLIKRRKTL TRILDRLQSI IRTFSWE
//
