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Database: UniProt
Entry: A0A0G1WAJ9_9BACT
LinkDB: A0A0G1WAJ9_9BACT
Original site: A0A0G1WAJ9_9BACT 
ID   A0A0G1WAJ9_9BACT        Unreviewed;       649 AA.
AC   A0A0G1WAJ9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UY54_C0003G0007 {ECO:0000313|EMBL:KKW15831.1};
OS   Parcubacteria group bacterium GW2011_GWA2_50_10b.
OC   Bacteria.
OX   NCBI_TaxID=1618854 {ECO:0000313|EMBL:KKW15831.1, ECO:0000313|Proteomes:UP000034043};
RN   [1] {ECO:0000313|EMBL:KKW15831.1, ECO:0000313|Proteomes:UP000034043}
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:KKW15831.1}.
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DR   EMBL; LCQJ01000003; KKW15831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WAJ9; -.
DR   PATRIC; fig|1618854.3.peg.56; -.
DR   Proteomes; UP000034043; 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          4..292
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          293..549
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         25..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   649 AA;  73428 MW;  C02232D75B585874 CRC64;
     MTSERLNSEQ KRAVLAVDGP VLILAGAGAG KTKTIAERIR HLVRSGVSPS SILAITFTNK
     ASREMRERVE RGLSEDPAIN RPVSMAERPF VSTFHALGVH ILREQSLKAG IKRHFAIFDR
     DDSKRAVKEA LVTLGFDPKT HEPGAVLSVI SKLKGRGINV EEWSEAEQGG YFLDVVAQVW
     PEYERALKRE DALDFDDLLL KTSNLLREDP AVRGYYQSVW RYIHIDEYQD TNRVQYDISK
     MLVGVGENIC VVGDIDQNIY SWRGADIKNI LDFEKDYPKA QVITLEENYR STKTILEAAN
     AVIEKNKIRR KKNLFTSNAA GEKITAIGLI DEATEAAFIA SKAREFIKNG IPPDEMAVLY
     RANFQSRVLE EAFMSAEVPY QILGTRFFER KEVKDIISYL RAAKNPESLS DLKRIINTPA
     RGIGKTTILK IFGGTAESLP LAMKTKIAVF RKLLSKIAEI SAEKRVSETI SFIIKESGLE
     EEWKEGGEDG AARLENTYEL VNFASRYDAM PPEEGILSFL SETALQSDQD ELKEERKAVR
     LMTVHAAKGL EFDVVFISGL EDGLFPHQRM NQSNITAEEA EEERRLFYVA LTRARKKIFL
     SYAQVRTVFG RQQVNMPSEF IFDIPENLVE QEIIEESMGR RRPLLEIEF
//
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