ID U5N5M6_9BURK Unreviewed; 1001 AA.
AC U5N5M6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=Cenrod_0709 {ECO:0000313|EMBL:AGX86816.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX86816.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX86816.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX86816.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(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}.
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DR EMBL; CP004885; AGX86816.1; -; Genomic_DNA.
DR AlphaFoldDB; U5N5M6; -.
DR STRING; 946483.Cenrod_0709; -.
DR REBASE; 71923; CbaCRORF709P.
DR KEGG; cbx:Cenrod_0709; -.
DR PATRIC; fig|946483.4.peg.709; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000017184; Chromosome.
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:UP000017184};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 259..440
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1001 AA; 113578 MW; 1FD25E349625BB4C CRC64;
MIEQQIEQGF IDKLTGLKYE YRSDITDRAA LEQNFREKFE ALNRVRLTEA EFARLLDEIV
TPDVFTAAKT LRSINAFTRD DGTPLNYSLV NLKDWCKNHF EVINQLRINT DNSHHRYDVI
LLINGVPCVQ IELKTLGVNP RRAMEQIVEY KHDPGNGYTK TLLCFMQLFI VSNRDRTYYF
ANNNARHFAF NADERFLPIY EFADEDNRKI IQLDAFAERF MKKCDLGRTI SRYMVLLAGE
QKLMIMRPYQ VYAVQHMVKC IDEDNGNGYI WHTTGSGKTL TSFKASTLLK ENDHIHKCVF
VVDRKDLDRQ TREEFNKFQE GCVEENTNTA ALVRRLLSED YADKVIVTTI QKLGLALDEN
SKRNKQRSKN GQATYKEQLE ALKDHRIVFI FDECHRSQFG ENHKAIKAFF PKAQLFGFTG
TPIFDANASQ QKIEDTQASM RTTADLFQKQ LHAYTITHAI EDGNVLRFHV DYFKPKGKKL
PKPGEPLAKK AVIEAILSKH DAATGGRRFN AILATASIND AIEYHAQFKA MQAEKQAADP
DFKPLNIACV FSPPAEGDPD VKQIQEDLPQ EQADNEEDPE GKKAALKAIL ADYNARYGTN
HRLGEFDLYY QDVQKRIKDQ QWPNADYPSA QKIDITIVVD MLLTGFDSKF LNTLYVDKNL
KHHGLIQAFS RTNRVLNGSK PYGNILDFRQ QQDSVDAAIA LFSGEKTGEQ AREIWLVDKA
PVVIQKLETA MQKLDSFMKS QGLDCTPSAV ANLKGDEART AFITHFKEVQ RLKTQLDQYT
DLTQENKASI EQVLPEENLR GFKGQYLETA KKLRDQQGKS GNKPGTDSPV DQLDFEFVLF
ASAVIDYDYI MGLIAKFSEK GPGKSKMTRE ELIGLISADA KFMNERDDIA EYIGTLKAGE
GLSESAIREG YTRFKVEKNA KELAAIAQKH GLATAALQAF VDGILDRMIF DGEQLGDLMA
PLDLGWKART QAELALMEDL LPLLTKRAGG RDISGLSAYE P
//
