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Database: UniProt
Entry: A0A1F3EBA9_9BACT
LinkDB: A0A1F3EBA9_9BACT
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ID   A0A1F3EBA9_9BACT        Unreviewed;       774 AA.
AC   A0A1F3EBA9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=A2X13_06690 {ECO:0000313|EMBL:OFX52470.1};
OS   Bacteroidetes bacterium GWC2_33_15.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797324 {ECO:0000313|EMBL:OFX52470.1, ECO:0000313|Proteomes:UP000177978};
RN   [1] {ECO:0000313|EMBL:OFX52470.1, ECO:0000313|Proteomes:UP000177978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OFX52470.1}.
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DR   EMBL; MENN01000003; OFX52470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3EBA9; -.
DR   Proteomes; UP000177978; 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; 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; PF21196; PcrA_UvrD_tudor; 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          6..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..573
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   774 AA;  88483 MW;  8ACDACB48430D291 CRC64;
     MYEFLNELNE AQREAVVNYS GASLVIAGAG SGKTRVLTYR IAYLLAKEIP ARQILALTFT
     NKAAAEMKSR IAKMAGNDVA RFLWMGTFHS IFARILRNES GKLGYSSNYT IYDPIDTKSL
     IKKIIKELNL DDKIYKSNEV YGRISSAKNN LITAKAYSSN NQIIIQDQKN NRSRITDIYT
     IYSNRCKKAD AMDFDDLLLN TNILFRDFPE VLEKYQNMFK YILVDEYQDT NFAQYLIVNK
     LSSKNKNICV VGDDAQSIYS FRGAKIENIL NFKNDYPGYK LFKLEQNYRS TQTIVNAANS
     LIKKNKEQIP KKVFSANSVG EKIKVVEAET DKDEAYKIAR IIQDVIEEKN YDNKDFAILY
     RTNAQSRSFE EAFRRFNIPY KVYGSISFYQ RKEIKDILAY FRLSINHNDE EALTRVINYP
     ARGIGQTTLE RIEETAKNEN LTTWDILTQI QKNGLGLNSG TQSKLNSFKE LIEKFSEGIK
     QNDAYDAAIL IAKESGIIDE FKNPESHEEQ TRLENLEELL NGIKEFVDEQ NDTDLLPTLD
     KYMENVALLT NQDNEKDDDF NKVTIMTIHS AKGLEFKHVF LVGLEEDLFP SSMSSGTQKE
     LEEERRLCYV ALTRAEETAV ISFAKERYKW GVPSSCRPSR FIKEIDEQFL ELPDSFLETP
     FPLITKNDLP GFSSKPKFIK NDKPGINGNL QSVNKRLVKI SSNQNNHTNQ ESEIIPDDPG
     LIAEGMVVRH SKFGLGEVLQ IEGVAPNSKA TVYFEVVGEK QLLLKFAKLQ IVKK
//
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