ID A0A2R5FVD1_NOSCO Unreviewed; 368 AA.
AC A0A2R5FVD1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=NIES4072_64280 {ECO:0000313|EMBL:GBG22716.1};
OS Nostoc commune NIES-4072.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2005467 {ECO:0000313|EMBL:GBG22716.1, ECO:0000313|Proteomes:UP000245124};
RN [1] {ECO:0000313|EMBL:GBG22716.1, ECO:0000313|Proteomes:UP000245124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4072 {ECO:0000313|EMBL:GBG22716.1,
RC ECO:0000313|Proteomes:UP000245124};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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}.
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:GBG22716.1}.
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DR EMBL; BDUD01000002; GBG22716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5FVD1; -.
DR Proteomes; UP000245124; 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000245124};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 9..211
FT /note="Restriction endonuclease type I HsdR N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04313"
FT DOMAIN 292..364
FT /note="SWI2/SNF2 ATPase"
FT /evidence="ECO:0000259|Pfam:PF18766"
SQ SEQUENCE 368 AA; 41651 MW; 51D12BB97CD7790C CRC64;
MPESPEFTHV EKPTIDQLIS MGWHYVEGNW NDPQVTEREN FKQVLLTERL KAAIKRINLD
DNGNPWLDDL QVQTAVSQLE RLGANRLMEA NQAATELLLK GTTVLGQDGK QHTVHFIEFD
PEHCDRNDFL AINQYRVDPP WATGNRGFIV PDMVLFVNGI PLVVIECKSP NLDNPITEAI
QDLLKYSNQR GSSQPEGAEK LFHYNLLMIA ASRGRATAGT IGANYEHYVD WKDTIPSPQA
EIAAQLGVSE LNFRQTLIAG MLKPANLIDI FRNFTLFKTS GGRTIKIVPR YQQYRAVYKA
LYQLQHNQTR AEHGTDDQRG GIIWHTQGSG KSLTMVGATR FCEVLKSGTY IACFRMRSQL
KNQILLRI
//
