ID A0A1T4RK27_9BACT Unreviewed; 951 AA.
AC A0A1T4RK27;
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 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=SAMN04488132_1137 {ECO:0000313|EMBL:SKA16323.1};
OS Sediminibacterium ginsengisoli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Sediminibacterium.
OX NCBI_TaxID=413434 {ECO:0000313|EMBL:SKA16323.1, ECO:0000313|Proteomes:UP000190888};
RN [1] {ECO:0000313|EMBL:SKA16323.1, ECO:0000313|Proteomes:UP000190888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22335 {ECO:0000313|EMBL:SKA16323.1,
RC ECO:0000313|Proteomes:UP000190888};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUWH01000013; SKA16323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4RK27; -.
DR STRING; 413434.SAMN04488132_1137; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000190888; 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:UP000190888};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 262..427
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 951 AA; 111242 MW; C2B1F9D4FC28B757 CRC64;
MSKESEQILE EKLIAQLQKL GYQFVSVPNE ASLIQNLKTQ LEKHNNLNFS DTEFEKVLNI
LNKGSVFEKA HTLRQKQHII KDNGDNLYFE FLNTEFWCQN QYQVTNQVSQ EGTYKNRYDV
TLLINGLPLV QIELKRRGLE LKEAFNQVDR YRKHSFGAGH GLFHFVQIFI ISNGVNTKYF
SNFGTSKQEY LQTFHWTDEN NKPLNNILNG FTDAFLEPCH VSKMICKYIV LHATEKKLMI
LRPYQYYAVE NIIKKVSENI ILNGYDINKN GYIWHTTGSG KTLTSFKASQ ILANIPAIKK
VVFVVDRKDL DYQTNQEYEK FSKGCVSSAD NTSELIQKFN DPTVRIIVTT IQKLNYAIAG
KNILRMKDIQ HQRMVFIFDE CHRSQFGDTH KKIVNYFTNI QLFGFTGTPI LAENSNGEKT
TNSLFGKCLH KYVITDAIRD ENVLRFSVEY IQTFKQKDHI IDLKVEEINE EEVFEAPERK
EAIVDYILQY HSQKTQNGAY CAMMCVQDID SVIKYYEIFK AKKKTSVHHL KIATIFSFAQ
NEDPLDFEIK SDTGRAQELK ESEQLIPHRR DLLDTYIQDF NEMYGTAYST KDSLSFYNYY
NDVAKKAKNK DLDILLVANM FLTGFDSKYV NTLYVDKNLQ YHGLIQAFSR TNRIHDKNKT
QGNIVCFRNL KEKTDEAITL FSNKDAIDEV IVEPYEKYVI QFNKAVDALS DITPTFDSVD
DLYSEEDQMQ FVLAFREVMR LFKKMEHYTE FDWNDLNIKE QIFKNFTGKY QDLKDKISLK
KDSTKISILE DIDFELELIR RDTINVTYIL QLLIKLKTNN KAKDKTAIET EISNLLNSEV
TLRSKRELID KFIKENFVRI ADVEDIKEEF DKFWDEEQRR ELSKIIVEEN LSVDKTEKLI
ENYLFAERVP LRDEVLELIE GAKPGLLERK SSGNRILKRI VDFVETFIKG L
//
