ID A0A2U2J7T5_9FLAO Unreviewed; 958 AA.
AC A0A2U2J7T5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=DIS07_13420 {ECO:0000313|EMBL:PWG04399.1};
OS Polaribacter aquimarinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2100726 {ECO:0000313|EMBL:PWG04399.1, ECO:0000313|Proteomes:UP000245670};
RN [1] {ECO:0000313|EMBL:PWG04399.1, ECO:0000313|Proteomes:UP000245670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY113 {ECO:0000313|EMBL:PWG04399.1,
RC ECO:0000313|Proteomes:UP000245670};
RA Lu D.;
RT "Polaribacter aquimarinus sp. nov., isolated from sediment in a sediment of
RT sea.";
RL Submitted (MAY-2018) 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:PWG04399.1}.
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DR EMBL; QFFG01000006; PWG04399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2J7T5; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000245670; 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:UP000245670};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 251..416
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 958 AA; 111093 MW; 7C0F525ED9DA415C CRC64;
MSKQSELQLE NNLIKQLVGL DYKKATILDG SALVANLKSQ LERFNQLTFS NKEFQKILNH
LEKGNVFEKS KTLRGRFQFE NDNGEATYIR FFNSENWNDN LFQVTNQITQ EGTYKNRYDV
TLLVNGLPLV QIELKRRGLE IKEAFHQINR YQRHSFWSNH GLFQYVQLFV ISNGVNTKYL
ANNALQSVKQ TFYWADENNK NIKELPDFTN AFLSPDHLGK MIAKYIVRNE THKILMVLRP
YQYYAVEKLV AQVENTTENA YIWHTTGSGK TLTSFKASQI IMDLPSVDKV LFVVDRKDLD
YQTMKEFNSF KKDSVDVTNN TSSLVKQLAD ESKLVLTTIQ KLNNAISKSH YENQLSSLKN
RRVVLIFDEC HRSQFGETHQ KITDYFTNSQ LFGFTGTPIF ADNASKNDLG KRTTKDLFGE
CLHKYVITDA IDDENVLKFG IEYIGRYKQK GRTLLDIEVE DIDKAAVFKD ERRLRKIADY
IIAYHSAKTF DKEYSALFAV SDIKTLIKYY EIFQEKKRAG AHNLRIATIF SYGANEANED
AQDYLPDNET LTAAESEIDY TSTSHSREKL DAFIADYNNM YNTSFSTKDS VQFENYFKDI
SKRLKDREKK TFNDAKDRLD IVIVVNMMLT GFDAKKVNTL YVDKNLKHHG LIQAYSRTNR
ILGEKKSQGN ILCFRNLKKA TDEAITLFSN KNASESIFVP PFENIAEKFD EALENLLKIT
PTYQSVDDLV GEDQELAFVQ AFRRLLRAKN VLESYVDFDW ENLGIDEQTF ANYQSEYWDL
HDKVKSNNQT NKVSILDDID FELELIHRDQ INVVYILQLL SKLKTADKNE VAKQKKAIID
LLGGDVKLRS KRELIEKFIE ENLPNISDAD SITDEFEKYW QEQKVKALTK ICTEENLDQA
QFNSLIQSYT YNGQEPIRQD IFKCLDNRPS ILKAREIGDR ILSKMKKFID IFINGMSA
//
