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Database: UniProt
Entry: A0A0G0VXW7_9BACT
LinkDB: A0A0G0VXW7_9BACT
Original site: A0A0G0VXW7_9BACT 
ID   A0A0G0VXW7_9BACT        Unreviewed;       747 AA.
AC   A0A0G0VXW7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UU58_C0005G0011 {ECO:0000313|EMBL:KKS04562.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWA2_41_25.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618736 {ECO:0000313|EMBL:KKS04562.1, ECO:0000313|Proteomes:UP000034236};
RN   [1] {ECO:0000313|EMBL:KKS04562.1, ECO:0000313|Proteomes:UP000034236}
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:KKS04562.1}.
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DR   EMBL; LCBE01000005; KKS04562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0VXW7; -.
DR   PATRIC; fig|1618736.3.peg.245; -.
DR   Proteomes; UP000034236; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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; 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; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          9..324
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          325..654
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          88..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   747 AA;  83964 MW;  1C221E57F73AB973 CRC64;
     MITDTEHLKG LNKEQKEAAL HIKGPLLIVA GAGAGKTKTI THRIVNLIKN GVAPEKILAV
     TFTNKAAKEM RDRIQTAIFS FDSRRGGENF PMRGVSQADG PRGSAPRARG DSDPAEEESS
     TPFVSTFHSL GVHIIKENAR LLGLTRYFTI LDEGDAASLI KEIMKEIGID PKQYDPKKIK
     NIISREKGKF THLSTYAESV NNTIGKIVAQ VWNLYEKRKM KENALDFDDL LLKAVKLLKD
     NVEIRKVYQE KWEYIHVDEY QDTNEVQYLM SKLLSENNHN ICVVGDADQN IYSWRGANLK
     NILSFEKDYP SAKIILLEQN YRSTKNILEA ANVIIKKNIY RPDKNLFTDN KIGEKIGLYE
     ALDENDEADF VAIKILELLD GSVGSSFSQV LGNNPQTIRK STPGYAKENK AGVSLRGVSQ
     ADGPRGSAPS ADGDSDPAET APARLSEVAI LYRANFQSRA LEEAMLRYNI PYQVLGVKFF
     ERKEIKDTLA YLRAALNPNS LSDIKRIINF PARGIGKVTL AKIFAGNTES LPIKVKIKVY
     NFYKVLEEIR EKIKTEKASR IIKFVVQHSG IENELSSGTE EDMERLENIK ELATLALKYD
     NLANGLGVER LLEDAALASD QDSLMINTPH PDPLLGKERE NNAVKLMTVH ASKGLEFKYV
     FVTGLEDGLF PHERQNEMQN GEDREEERRL FYVALTRAKE KLFLSFANFR TIFGSRNINT
     PSEFIADIPP NLLQKEKEDS GIKTIYI
//
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