ID A0A0G0UYE2_9BACT Unreviewed; 990 AA.
AC A0A0G0UYE2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=UT91_C0002G0023 {ECO:0000313|EMBL:KKR55362.1};
OS Parcubacteria group bacterium GW2011_GWA2_40_23.
OC Bacteria.
OX NCBI_TaxID=1618816 {ECO:0000313|EMBL:KKR55362.1, ECO:0000313|Proteomes:UP000034534};
RN [1] {ECO:0000313|EMBL:KKR55362.1, ECO:0000313|Proteomes:UP000034534}
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:KKR55362.1}.
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DR EMBL; LBYP01000002; KKR55362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0UYE2; -.
DR STRING; 1618816.UT91_C0002G0023; -.
DR PATRIC; fig|1618816.3.peg.174; -.
DR Proteomes; UP000034534; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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 SUPFAM; SSF52980; Restriction endonuclease-like; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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 5..326
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 327..616
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 990 AA; 115365 MW; 0FBD8693D9A3BBC6 CRC64;
MSLLESSNKE QLSAIMHEAG PQLIVAGAGT GKTRVITARI AYLITEKNIN VDEILALTFT
DKAAEEMEER VDKMLPYGYV DLWISTFHSF CDKLLKRHAL DIGLSNNYKL INETEAWLLI
KKNLARFDLD YYRPLGNPTK FIHALLKHFS RCKDEGISAE EYLEFADGLK LDLDVTDYVK
KLDLPEDFAE LKKEEKQALL KQEIIRINEI AKAYHTYQQI LIENDCLDFG DLHNYAIKLF
KDRPLILDKY RRQFKYILVD EFQDTNFVQY ELIKLLAAPK NNLTVVGDDD QSIYKFRGAS
ISNIMQFKED YPNAQEVVLT ENYRSAQEIL DLSYNFIKQN DPNRLEAKLN INKKLKSNKT
EQGVIDHKHF ETIDAEAQFV ISQIREIQKV TQCEWKQFAI LVRANESANI FISYLDSANI
PYQFLALRGL YTKPVIVDLL NYLKLLDDYH EGASVYRLLN FPCFKLKTDQ IIKIVHYAKQ
KSFSLYDTLK KIVIIPGIEM ETITQVGKIY AQVEADTALA QKKRPTEVLL NFLYTSGYLE
HVKNLDEKIA KENLDYIQQF FQKVKEIETT YEDARIKDIV EVFDLELQSG EAGRLAFDVE
TGPDMVKVMT VHGSKGLEFD YVFLPNLVDR KFPTDERKEA IEIPAALIEE KLPEGNFHLE
EERRLFYVAM TRARRGLFFT SAEDYGGVRK KRLSRFLIEM GYKKDYDIQS TETILIKPSK
SSAVDKFVYE LPKRFSFSQI ATYEKCPLQY KYGNILKIPA FGSHYFTFGT IIHSTLQKFL
EESYQVNNNV QEDLFSNIKK TIKKGTLPLD RLYQVYDDVW FDDWFQDPKQ KEEYYKKGKA
LLKSFHADFN SELPEVRNLE ISFKLPVGPY FFSGRIDRVD NLESGLVQII DYKTGQAKDD
KLTTDDKRQL LFYQIAAEEA LKLKVEKMTY HYLEENKKIS FMGKEKDKEE LKKRFIEDIE
LIKAQKFEAT PSPYVCGSCD YRNICEHKKL
//
