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Database: UniProt
Entry: A0A0G0HIY5_9BACT
LinkDB: A0A0G0HIY5_9BACT
Original site: A0A0G0HIY5_9BACT 
ID   A0A0G0HIY5_9BACT        Unreviewed;       669 AA.
AC   A0A0G0HIY5;
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=US24_C0006G0007 {ECO:0000313|EMBL:KKQ12034.1};
OS   candidate division WS6 bacterium GW2011_GWC2_36_7.
OC   Bacteria; Candidatus Dojkabacteria.
OX   NCBI_TaxID=1619091 {ECO:0000313|EMBL:KKQ12034.1, ECO:0000313|Proteomes:UP000034075};
RN   [1] {ECO:0000313|EMBL:KKQ12034.1, ECO:0000313|Proteomes:UP000034075}
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:KKQ12034.1}.
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DR   EMBL; LBSF01000006; KKQ12034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0HIY5; -.
DR   PATRIC; fig|1619091.4.peg.102; -.
DR   Proteomes; UP000034075; 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   Gene3D; 1.10.10.160; -; 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; 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; 1.
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          8..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..585
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   669 AA;  76178 MW;  BADFF420207FA341 CRC64;
     MNLDIILGGL NPEQKKAVEC TEGPLLVFAG AGSGKTRVIT SRIAYLISEK KVQPQNILAV
     TFTKKAAGEM QERIKSILKD IGASIEDLPA VGTFHSIGAL FLRQNAKAVG LTNNFSIYDS
     DDSENLIKEL MIERQIDIKQ IKPQSISYLI SAAKNEMVTP ENFGSHYGGY LEDIAAEIYP
     AYQKQLKTQN SVDFGDLLYL AVKMLEENEE VRKHYQDKFE YLLIDEYQDT NNAQYKFARL
     LSEKHQNICV VGDDDQGIYA WRGADIKNIQ SFEEDFTKVT VIKLEQNYRS TKNVISAAVA
     VIQQNNKRVD KKLWTDNNDG ENISVYQARD QEDESEYVTE KIRHMRDMHI PLSNVAILYR
     TNYQSRAIEE ALLKTGVPYK LVGGFRFYER KEIKDVISYL RFLYNIKDEL SLGRIINVPS
     RKIGPKTVAA LHDLARQADC SIGELLVSAY ALGHPESQAI IDLGGGLLNR VNEVSGELAK
     FASLISTFGY LYVEARKKNL LDIIDIILEK TNYIQWFDDG TDQAQMKKEN VTELKNVAYQ
     YVKKYPEKSL EMFLNEINLI EQEQDKNQDG SGSYVNLMTL HSSKGLEFDY VFVIGMEEGL
     LPHSRAFTDE SELEEERRLC YVGITRAKQK LTLTFAETRL TREGFTSQIP SRFLGEIPQD
     ICEYYSWNA
//
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