ID A0A1T5EJT0_9FIRM Unreviewed; 614 AA.
AC A0A1T5EJT0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=SAMN06296386_106141 {ECO:0000313|EMBL:SKB84191.1};
OS Lachnospiraceae bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1898203 {ECO:0000313|EMBL:SKB84191.1, ECO:0000313|Proteomes:UP000191179};
RN [1] {ECO:0000313|EMBL:SKB84191.1, ECO:0000313|Proteomes:UP000191179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P17 {ECO:0000313|EMBL:SKB84191.1,
RC ECO:0000313|Proteomes:UP000191179};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; FUZG01000006; SKB84191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5EJT0; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000191179; 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 Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
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 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};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191179};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 313..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 614 AA; 70896 MW; 1C411386603AABD6 CRC64;
MAIIHNENSR VKIPALVHFT RLGYMYRSLK DTEGQYDEDT NIFIGSFRDG INKVNGTKLT
DRDVKDIIAD LKNTLNQDDL GQGFYKYLKK GYKGLKLIDF NTVAGDNNVY EVVTEFTCKN
GSEEFRPDIT VLINGMPLVF IEVKKPNNKN GIQAEYDRIN KRFANKKFRR FANITQFMIF
SNNSEYDDME VVPLEGAFYS TTDYERLFFS HFREEDEIIF EKISEIDEVV EKEILVDNNL
VSIKGSGEYA VNISPTSPTN RIITSMLSHE RLMFILKYAL CFVDKVDPDT GIRRLEKHIM
RYPQLFATKA IENKLTHGVK HGVIWHTQGS GKTELAYYNT HYLSDYYQKQ GVIAKFYFIV
DRLDLLRQAS DEFRSRGLVV DEVKNKAELE KMFEKPGDKN NTGELSITVV NIQKLSANAI
AKPLDYDLSI QRIYFLDEAH RSYDPKGSFL ANLMASDRDA VMIALTGTPL ISKEYKTKDV
FGDYIHKYYY NRSIADRYTL RLIREGIKTE YRMKLVSALE EIKAVKGSLP RKELYAHEAY
VQPLVRYITQ DFTKSRKMLN DDSIGGMIVC DSSEQARSVF EEIKSKNYKV VLADVQEKTI
LTENHIVQVV VRCI
//
