ID A0A0T5ZUR1_9BACT Unreviewed; 718 AA.
AC A0A0T5ZUR1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=XU11_C0007G0041 {ECO:0000313|EMBL:KRT66557.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT66557.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT66557.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT66557.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT66557.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDXN01000007; KRT66557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZUR1; -.
DR STRING; 1640508.XU11_C0007G0041; -.
DR PATRIC; fig|1640508.3.peg.574; -.
DR Proteomes; UP000051780; 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 7..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 285..555
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 718 AA; 82772 MW; F9FA9398C83447E3 CRC64;
MESDILNDVN PFQREAVTHP EGPVLALAGA GSGKTRIITY RIAYLIKEKG VSPTNILAVT
FTNKAANEMK ERVHRLVAKD AHELWIGTFH SVCLRILKKE IDKLDGFRRD FIIYDEVDQI
KLIRECMNKL GFSERISDPR SVRSQIDCAK NKGQSPWDFG ASIYDERISR VYHIYEQELR
RANALDFGDL LDFTATLFEK RPDVLDKYQN QFHHILVDEY QDTNHIQYKI VKLLSEKHRN
VFVVGDDNQS IYGWRGADIT NILNFESDFP DAKVVKLEQN YRSTKNILRA ANAVILRNRY
RRDKRLWTEN TEGSAVVYYE AHDERDEARY VASQIEYERT TNGRLYGDFA VFYRTNNQSR
VIEEEFVHQG IPYNIVGGVG FYERAEIKDI MAYLRVIANP LDEISLRRII NVPSRGIGKG
TIGTLEKIAQ ERDISLFDAT ELAIKNELLS KKALASLEKF YNLINELIKL SQRLSIGRLL
DKILEKTNYL ELLEHDEERR DNLGEILTLA AEFKKEEANN SIHDFLDWIT LSSDVDRFNE
KADKVTLMTL HCAKGLEFSI VFIVGMEESL FPHIKSLGNG RLIEEERRLC YVGITRSKEK
IYLTSTSKRR LFGVEHRSIP SRFVIEIPRK LLQWESYQTN FGEVTFKKHD NDQIRVDGNG
FPKNGDGYVI GENVIHPSFG QGVVKRVEGL GDEAKVVISF HDHGEKKIMA SFLGLKKI
//