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Database: UniProt
Entry: A0A1F5H523_9BACT
LinkDB: A0A1F5H523_9BACT
Original site: A0A1F5H523_9BACT 
ID   A0A1F5H523_9BACT        Unreviewed;       289 AA.
AC   A0A1F5H523;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=A3B54_04020 {ECO:0000313|EMBL:OGD99266.1};
OS   Candidatus Curtissbacteria bacterium RIFCSPLOWO2_01_FULL_42_50.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1797730 {ECO:0000313|EMBL:OGD99266.1, ECO:0000313|Proteomes:UP000177039};
RN   [1] {ECO:0000313|EMBL:OGD99266.1, ECO:0000313|Proteomes:UP000177039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- SIMILARITY: Belongs to the HsdR family.
CC       {ECO:0000256|ARBA:ARBA00008598}.
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:OGD99266.1}.
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DR   EMBL; MFBT01000020; OGD99266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5H523; -.
DR   Proteomes; UP000177039; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   Gene3D; 3.90.1570.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF04851; ResIII; 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};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          159..289
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   289 AA;  33285 MW;  854D5064B1D2E3F1 CRC64;
     MNKLHKETDA RIIIDRLLRE AGWDIEDKQQ VSTEEAAADG RADYLLKDQN GIPLAVIEAK
     RFSTEPTLAQ QQARDYAESI NAPFVFLSNG EIIYFWDYKN NSARLVDSFY SQEDLHRRNM
     LSKRVKSLKE IPFPTKFFYL NEELIVRPYQ TSAIEAVDKE IEQGKRRILI EMATGTGKTL
     TIAMIMKRLF EAGLIQRVLF LVDRKQLAEQ AKDVFAEYLK DTPSKVWYGG KPKELGQIVI
     GTLPTIASQL ERFGPGHFDL VVTDECHRSI YNIYRDLLNH FDALHISSH
//
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