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Database: UniProt
Entry: A0A380K0G5_9STRE
LinkDB: A0A380K0G5_9STRE
Original site: A0A380K0G5_9STRE 
ID   A0A380K0G5_9STRE        Unreviewed;       327 AA.
AC   A0A380K0G5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   Name=hsdR_5 {ECO:0000313|EMBL:SUN58235.1};
GN   ORFNames=NCTC12224_00264 {ECO:0000313|EMBL:SUN58235.1};
OS   Streptococcus hyointestinalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1337 {ECO:0000313|EMBL:SUN58235.1, ECO:0000313|Proteomes:UP000254924};
RN   [1] {ECO:0000313|EMBL:SUN58235.1, ECO:0000313|Proteomes:UP000254924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12224 {ECO:0000313|EMBL:SUN58235.1,
RC   ECO:0000313|Proteomes:UP000254924};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; UHFN01000005; SUN58235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A380K0G5; -.
DR   Proteomes; UP000254924; 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:SF16; TYPE I RESTRICTION ENZYME 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; 2.
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, ECO:0000313|EMBL:SUN58235.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254924};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          5..199
FT                   /note="Restriction endonuclease type I HsdR N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04313"
FT   DOMAIN          257..322
FT                   /note="SWI2/SNF2 ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF18766"
SQ   SEQUENCE   327 AA;  37749 MW;  46E3134718C39C47 CRC64;
     MAELESVLEQ KLIDQLCQGE SQWTYRPDIR TEEELWDNFR YILEQNNKAK LNDGRLTDSE
     FAKIKNDLSH ASFYDAGKWL VGENGQVYVH VQRGNEPLHL LVLNNEHIAG GTSVYEVINQ
     YQAFGEDDAR DRRFDVTLLI NGIPMIHIEL KNKDHSYMDG FHQIKKYIAE GKFRGLFSNV
     QMFVISNGVD TKYFSAARDN ELNKKFLTGW IDHDNQPVPD FIDFAKAVLK IPEAHEMVTK
     YIVLDNDKKK LLILRPYQIH AIEAMRDASK KGKSGFIWHT TGSGKTMTSY KATRNLLMDI
     PSIEKTIFLI DRKDLDVQTK TRLSVLC
//
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