ID K9TIK1_9CYAN Unreviewed; 960 AA.
AC K9TIK1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=Oscil6304_2205 {ECO:0000313|EMBL:AFY81839.1};
OS Oscillatoria acuminata PCC 6304.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY81839.1, ECO:0000313|Proteomes:UP000010367};
RN [1] {ECO:0000313|EMBL:AFY81839.1, ECO:0000313|Proteomes:UP000010367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY81839.1,
RC ECO:0000313|Proteomes:UP000010367};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
RL Submitted (JUN-2012) 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; CP003607; AFY81839.1; -; Genomic_DNA.
DR RefSeq; WP_015148482.1; NC_019693.1.
DR AlphaFoldDB; K9TIK1; -.
DR STRING; 56110.Oscil6304_2205; -.
DR REBASE; 57902; Oac6304ORF2198P.
DR KEGG; oac:Oscil6304_2205; -.
DR PATRIC; fig|56110.3.peg.2607; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_3; -.
DR InParanoid; K9TIK1; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000010367; 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; 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:UP000010367};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 250..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 960 AA; 112458 MW; 4F648F4611C930EC CRC64;
MTQSEAQLEQ DLIERLAGLG YEPVTIRNAV ELTANLKTQL EKHNDITLSD QEFKSILNHL
DKGNVFDRAK RLRDKMELSR DDGTTFYLEF ISTEHWCENQ YQVTNQVTNQ GSYKNRYDVT
LLINGLPLVQ IELKRRGLEL KEAFNQINRY QRHSYGADNG LFQYVQIFVI SNGVNTRYYA
NNRKQEYKQT FYWADEGNNL LTNLDDFADR FLEKCHLSKM ICKYIVLHES NKVLMVLRPY
QYYAVETIIE RVKNTDKNGY IWHTTGSGKT LTSFKAAQIL TKLPTVHKVL FVVDRADLDY
QTSREFNYFS PDCVDTTDNT QQLVKQMSGD SPLIVTTIQK LNRAITSSRH EADMAPLQNQ
RIIFIFDECH RSQFGETHRK ITRFFHNAQL FGFTGTPIFA EKNVYVKDGL KLSTASLFTE
CLHRYVITNA IADENVLKFS VEYWGKLKRK DGTIIPEPKG DREFFENPDR ISLIVDWIIE
NHHRKTHRKK FSAMFCVSSV NTLITYYETF KAKKQQGLHD LRVVTIFTPI DNEDDDEANG
LIGEPDFDIT TDTSRRHHSR DKLDEFISDY NQMYKTQHSA KNSQAFYAYY KDISKRMKDR
DREDAQDVDR ADILLVVNMF LTGFDVKKIN TLYLDKNLKY HGLIQAYSRT NRILGELKSQ
GNIVCFRNLK ENTDDAVLLF SDENAKEEIF IQPYEYHVEQ FNEEVQALRA IASIPNDVNQ
LIDEEDQVEF VKAFRNLIRF LNVSKSFTEF SFSDLNLDEQ TFEDYKSKYL DIYDRTRSKP
DEEKESLVEE VDFELELIQR DEINVSYILK LLGRLQRDRQ TDVTSEEYQS QKASILELIG
KEAQLRSKRD LLEKFIEERL PTLDPKEKIE SVFQHFWTQE RIAAIEQFCQ AENLKIEVVN
RMIADYQFSG KEPLRETVLS ACNQTPKLLE RKKVFTRVVS KLLAIINRFD DAIGLLDEEE
//
