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Database: UniProt
Entry: A0A0G1DE78_9BACT
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ID   A0A0G1DE78_9BACT        Unreviewed;       968 AA.
AC   A0A0G1DE78;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UV71_C0001G0059 {ECO:0000313|EMBL:KKS96185.1};
OS   Microgenomates group bacterium GW2011_GWC1_43_13.
OC   Bacteria.
OX   NCBI_TaxID=1618521 {ECO:0000313|EMBL:KKS96185.1, ECO:0000313|Proteomes:UP000034809};
RN   [1] {ECO:0000313|EMBL:KKS96185.1, ECO:0000313|Proteomes:UP000034809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:KKS96185.1}.
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DR   EMBL; LCFN01000001; KKS96185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1DE78; -.
DR   PATRIC; fig|1618521.3.peg.63; -.
DR   Proteomes; UP000034809; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          8..305
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          306..595
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   968 AA;  111106 MW;  EA808DE6E0E0B7E0 CRC64;
     MAKDILALKL NREQQAAVKF GTGPLLIIAG AGTGKTTVIT ERIKYLILSK KIKPSEILAL
     TFTEKAAREM EERVDVAMPY GYTQMWIMTF HSFCDRILRR EALHIGLTPR YKLMTEAEAV
     QLLRNNLFKL DLNYFRPLGN PTKFLSGILQ HFSRLQDEDV SPNDYAEWVK KQKTKKNKER
     TEIEKWEELS KAYKAYDEIK VKEGLMDFGD LIVKTLKLFR TRPNILKEYQ KQFKYLLVDE
     FQDTNYAQNE LAKLLAGKNG NINVVGDDDQ SIYRFRGAAV SNIVQFRKNF PKTKAVVLTK
     NYRSTQEILD RSYDLIQFNN PDRLEVVEKI DKKLKSQVAK DGAEIGFIHS DRVENESDRI
     AKEIKRLNEE EKYSWRDFAI LVRANNHSDP IMRALSRHGI PYQFLGPGRL FKQPEIVDLI
     SYLKVLRDFT DSVAFYRLLA LDYFNISGRD LAALGNYARK YNTSLFESAE KIDDIFVTVK
     TKETIKKILG IINKHLDIAK KETAGQLLYY FLEETGLLLK LLSPESVEAE NRAKNISKFF
     DKLKTYEIDH EDATIPAVTD WLDLSMELGE SPLATNEDWS EINAVNILTA HSAKGLEFPV
     VFIVNLVGQR FPTSERREQI AIPEELIKEI LPVGDYHLEE ERRLFYVGMT RAKEKLILTA
     ADYYGEAKRE KKLSPFIFES LGDSALSAEQ SKIKADQLSF LDYQIKAKPT EAPVKAGEDL
     HIDYLSYSQI ETFQTCPLHY KLRYIYKVPT PPNASASFGT TIHATLKSFY EEVSSGQKPV
     EKLLLKLLED NWVREGYTSK KHEVEFIQKG KDYLIGFLKY GFSPKKMPIA LEQPFTVHVG
     KDLKIGGRID RVDDLGNGQI EVVDYKTGAT IPTQKEVDKN LQLSFYALAA TKIPTVPFGK
     APEKIKLSLY YLDLQEKIST VRTAEQLEGA VSEILKIRDR IEKSDFKCSD HVFCQKGCEY
     ALFCRSDR
//
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