ID A0A0G0JPV1_9BACT Unreviewed; 1062 AA.
AC A0A0G0JPV1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=US90_C0015G0026 {ECO:0000313|EMBL:KKQ69583.1};
OS Candidatus Shapirobacteria bacterium GW2011_GWE2_38_30.
OC Bacteria; Candidatus Shapirobacteria.
OX NCBI_TaxID=1618490 {ECO:0000313|EMBL:KKQ69583.1, ECO:0000313|Proteomes:UP000034406};
RN [1] {ECO:0000313|EMBL:KKQ69583.1, ECO:0000313|Proteomes:UP000034406}
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:KKQ69583.1}.
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DR EMBL; LBUT01000015; KKQ69583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JPV1; -.
DR STRING; 1618490.US90_C0015G0026; -.
DR PATRIC; fig|1618490.4.peg.590; -.
DR Proteomes; UP000034406; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
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; PF12705; PDDEXK_1; 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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 10..385
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 386..676
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1062 AA; 123532 MW; 82F72E3AEE16A5EF CRC64;
MSDIFSTEYK NLNPEQKLAV DTIEGPVMVI AGAGTGKTQT IALRIANIIK NTQTPASSIL
CLTFTDTATI TMRKRLVSII GSQAYSVKIN TFHAFCNDII QDNPEYFIFA PNLKSLDNLS
RLQIVQNLIN QLQNGSPLKP WGDHFHYQRE IISSIQTLKR ENITPSSFKK LIEDVLYFID
NSKDIHSKLK TLRTSKTLES ELLSLYNDLS LIPNLSTPIH SFLNYHFQLF KSGFYLSGPA
KNPNINFKNA LLKLIDNFSS DIPKQNELFQ LYQNYQKTLN DQGFYDFDDM ILFVLQAFSD
HTELLLRYQE TYQYILVDEY QDTNSAQNKI IENLGSYFDN PNLFVVGDDD QSIFRFQGAA
IENIYRFYQK YSPKLIILRN NYRSHQLILD SSLSVINHNQ SRIANYISHL DKSLKSVSTL
DADPINLFSA SNNLEENYYI AHTIENLIKT GTKPNQIAIL YRQHTDITDI AEMLTNFDIN
FYLASDRDIL KDPLFIQINK LFQFIDDPTK SDLLYHILSA PFIKINSQDL LKLFRFSKKL
HAPLWQLISD PKLLSQITPA LNSHTLIKLK NFNLRLAKSR HWLEIYPIDR FFNLTIRKFK
ILSYILSRKD FEILNKLKTF YSEIKRLSQD IPNFTLTDFL SRLQLLSDNN LPFPVPPGRL
QSEDSVQLMT VHSAKGLEFE HVFLVKVVDK HWGNNRNHQI LRLPPGILQT EISSDLYDQN
EDERRLFYVA LTRAKSQIYI SYSSQNDNSR PQIPSLFISE INPKLVQNID PPDNIYQQAL
TTSFPLKLKK PNISGKYKEY LLDYLSNNYQ FNVTHLNSYL KCPFCFYHQT ILRIPAAKNK
YSSFGTAFHD TLSFILDKLN HQQPIPSDKI IFNFFKESLL KENLSSQDFE ESIHRAENSL
LEYVHHYAKH FPSHNQTEYN FASEHLMFEN IPVTGKIDLV SYKSNNSVEL VDFKTGNPDT
KSKELSPDGE YFRQLVFYYL LVSLSSRLKV KIDKGVIDFV QKSKIKNTFI RRDFEIDPHH
IDKLKLEIKD TYKKILNLDF FTIGSDCKDH MKIHYLLEKS KF
//
