ID A0A0N8H3T6_9FLAO Unreviewed; 998 AA.
AC A0A0N8H3T6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=I595_2743 {ECO:0000313|EMBL:KPM31476.1};
OS Croceitalea dokdonensis DOKDO 023.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceitalea.
OX NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM31476.1, ECO:0000313|Proteomes:UP000050280};
RN [1] {ECO:0000313|EMBL:KPM31476.1, ECO:0000313|Proteomes:UP000050280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM31476.1,
RC ECO:0000313|Proteomes:UP000050280};
RA Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT 023 that contains proton- and sodium-pumping rhodopsins.";
RL Submitted (SEP-2015) 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}.
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:KPM31476.1}.
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DR EMBL; LDJX01000005; KPM31476.1; -; Genomic_DNA.
DR RefSeq; WP_054559760.1; NZ_LDJX01000005.1.
DR AlphaFoldDB; A0A0N8H3T6; -.
DR STRING; 1300341.I595_2743; -.
DR PATRIC; fig|1300341.3.peg.2900; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000050280; 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 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 R PROTEIN; 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:UP000050280};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 262..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 998 AA; 114927 MW; F78A913485FC6B87 CRC64;
MDLVKEADIE YGLVGRLQDL KYTYRPDIRD LNALEQNFRE KFEKLNKVQL TDSEFEKLST
QIIDPDVFAA SNSLRKTNTF FREDGTPLHY TLVNIKDWCK NDFEVINQLR INTKNSNHRY
DVIVLINGVP VVQIELKTLE VSPNKAMQQI VDYKNDAGNG YTNSLMCFMQ LFIVSNKSKT
FYFANNNNEH FAFNADEQFL PVYTLATEDN KKINHLYDFA DKFLSKCTLG QMISRYMVLV
ASEQKILVMR PYQIYAVKAI VDCIHQNRGN GYIWHTTGSG KTLTSFKAST LLKDNPDIEK
CLFVVDRKDL DRQTRQEFNK FQEGSVEENT NTAILVNRML STDYADKVIV TTIQKLGLAL
NQNSKRNVKQ REENQKSYYD RLAPLRDKRV VFIFDECHRS QFGENHDAIK EFFPKAQLFG
FTGTPIFTEN ATYKTIEGDQ ASYKTTQDVF QQELHAYTIT NAIEDRNVLP FHIDYFTAEG
QPDFNDLSHK MAVIHAILKK HDKATDHRRF NAILATSSIA DAIEYYHLFK QNQREYAQVN
EDYAPLNIAC VFSPPAEGNR DILQLQDDLQ QEKADNQIEP NKKKAALTQI MADYNAQYGT
NHSIAEFDGY YQDIQQRIKS QKYPNKDVPH KDKIDIIIVV DMLLTGFDSK FLNTIYVDKN
LKYHGLIQAF SRTNRVINDN KPKGNILDFR QQEEAVDNAM VLFSGAHIER AKEIWLVEPA
PVVIEKYQEA VGNLKMVMES HGLECKAHEV ANLKGDEARA QFINTFKEVQ RLKTQLDQYT
DLEDAQADTI EATLPTDDFR SFKSNYLDTA KRLKEIQNKP DAPEAVKQLD FEFALFSSAV
IDYDYIIGLV AKHLHNAPSE KTKMTKEQII QLLSASANMQ DYREDIIAYI NALPIGEKLT
EKEIREGYQQ FKDKKAAKEL NAIAQKHQLE TQSLKAFIDE IMNRMIFDGE KLTDLLAPLE
LGWKDRRVAE LALMEDLVPL LNKLAQGREI AGLNAYTV
//