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Database: UniProt
Entry: A0A0G0RVG0_9BACT
LinkDB: A0A0G0RVG0_9BACT
Original site: A0A0G0RVG0_9BACT 
ID   A0A0G0RVG0_9BACT        Unreviewed;       644 AA.
AC   A0A0G0RVG0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UT58_C0011G0004 {ECO:0000313|EMBL:KKR26505.1};
OS   Microgenomates group bacterium GW2011_GWC1_39_7b.
OC   Bacteria.
OX   NCBI_TaxID=1618516 {ECO:0000313|EMBL:KKR26505.1, ECO:0000313|Proteomes:UP000034178};
RN   [1] {ECO:0000313|EMBL:KKR26505.1, ECO:0000313|Proteomes:UP000034178}
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:KKR26505.1}.
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DR   EMBL; LBXI01000011; KKR26505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0RVG0; -.
DR   PATRIC; fig|1618516.3.peg.302; -.
DR   Proteomes; UP000034178; 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; 3.
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   InterPro; IPR027785; UvrD-like_helicase_C.
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   Pfam; PF13538; UvrD_C_2; 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          9..293
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          294..521
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   644 AA;  73064 MW;  70742A7E579A964F CRC64;
     MNDVDKLTND LNKDQFAAVI YTAGPLLVLA GAGSGKTKVL THRVAYFIQQ GLIKPENALL
     LTFTNKAATE MRQRINDLLG QSSANSKQST VFSGTFHSFC AKVLRIDGKH IGIPINFIIY
     DDQDQKDAVK QILESINIST DQFAPASILN GIGEAKNQML TPAEYKNFVR GEWQEVVAKV
     YEQYEKMLKD IGALDFDDLM IKTVQLFKEV PEILTKWQTT LTHIFVDEWQ DTNKIQYTLT
     KLLVGKNRNI TAVGDASQSI YSWRGADYRN ITLLTRDYPD IKIVNLEQNY RSTQNILDAA
     NLVISKNTNH PILKLWTDKH AGSKIKLYSA RNGFDEADFV VSEIQSRDSK YGDFAILYRT
     NAQSRVLEEA FLHAGIPYSL VGGTRFYDRK EVKDIISYLK YLVNPKDSVS RKRIEKIGIR
     RFEKLEEFRN SQNSLNSLTT LEMLDAVIQK TDYLSLFQKE SEENLARLEN IKELRSVATE
     FPAISDFLEN VALVESTQKP ANSASIAKDS VTLMTLHAAK GLEFPIVFIV GMEEGLFPHS
     RSLMDGNQLE EERRLAYVGI TRAKDVLYLT YASSRLYFGE RISNPPSRFI MDIPEDLIEN
     IDANIWKDDL SSKALASEDL KLDSVEDIKG TFDDIIEKYL PHDD
//
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