ID S9QKX4_9RHOB Unreviewed; 956 AA.
AC S9QKX4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=thalar_01598 {ECO:0000313|EMBL:EPX80258.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX80258.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
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:EPX80258.1}.
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DR EMBL; AONI01000009; EPX80258.1; -; Genomic_DNA.
DR RefSeq; WP_021100164.1; NZ_KE557306.1.
DR AlphaFoldDB; S9QKX4; -.
DR STRING; 1123360.thalar_01598; -.
DR REBASE; 79334; Tar19593ORF1596P.
DR PATRIC; fig|1123360.3.peg.1584; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_5; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000015351; 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; 2.
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:UP000015351};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 252..417
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 956 AA; 109289 MW; 6FA91098EA996BB0 CRC64;
MAEYQSEAQL EDGLVKRLTS LGYAPVTLLD MDAMRANLRA QLGKHNGVTL SDAEFAKVLN
HLDKGNVFEK AKTLRGRMQL TRDDGTPLYL QFLNTQEWCQ NQYQVTTQVT VTGHHKTRFD
VTLLINGLPL VQIELKRRGV ELKEAFNQIN RYQRHSYWSE SGLFQYVQLF VISNGVNTKY
YANNRNQDFK QTFFWAKEDN ELVTQLDAFA DAFLEKCHVS KMISKYIVLH ESDKILMALR
PYQYYAVEAI DARVKNGRKN GYIWHTTGSG KTLTSFKAAQ VLIENPKVHK VVFVVDRADL
DYQTTKEFNF FSDGSVDGTD NTKALVGQLG GDTKLIVTTI QKLNTAISRD RYEGPLQAVK
DQRVVFIFDE CHRSQFGDTH KRIVQFFSKA QMFGFTGTPI FADNAVGKRT TKDLFAECLH
KYVITDAIAD ENVLRFSVEY WGKLKRKDGS LIDEDVPAIN VREFFDSPER IDGVVDWIIQ
NHDRKTHNKQ FSAMLCVSSV DALIAYYEAF RRKKGAGEHH LRVATIFTYG PNEADPDADG
LIGDPDLNVA DMPVDVHKRD RLESFVADYN AMYQTKETVK DSAGFYTYYN HLSKRLKDRD
RKDALDKDRL DILLVVNMFL TGFDAKKLNT LYVDKNLKYH GLIQAFSRTN RILGQVKSQG
NIVCFRNLKP NTDQAITLFS NKDAIETILM APYGDYLDQF NEAIEVLRKI APDPDSVNDL
KSEEDQLAFV QAFRDLIRLR NVLTSFAEYD ADDLDLEAQI FEDYKSKYLD IHDKTKADKP
DSDAVSIIDE VDFELELIQR DEINVAYILA LLAEAFADQD SLDPKVRDAS KAKRKMVYDL
LGSERHLRSK RELIEKFIEE HMPNMPKGQT VEDAFSGFWD EEKSNAIAEI CEAENLDPSA
FKAMIEQYHF SGKKPLQGAI VEALSEKPKI LERKSVVERI AAKLLRLVTT FDEGLG
//
