ID A0A0G1KDE5_9BACT Unreviewed; 1070 AA.
AC A0A0G1KDE5;
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=UW78_C0006G0116 {ECO:0000313|EMBL:KKT81751.1};
OS Candidatus Azambacteria bacterium GW2011_GWA1_44_9.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618610 {ECO:0000313|EMBL:KKT81751.1, ECO:0000313|Proteomes:UP000034595};
RN [1] {ECO:0000313|EMBL:KKT81751.1, ECO:0000313|Proteomes:UP000034595}
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:KKT81751.1}.
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DR EMBL; LCJQ01000006; KKT81751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KDE5; -.
DR Proteomes; UP000034595; 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..392
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 393..683
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 1070 AA; 122367 MW; A820497AB696CA75 CRC64;
MALSFEERYA KLNDAQKRAV DTTEGPVLVV AGPGSGKTEL LSLRVGNILR QGQVSPHNIL
CLTFTDNGAM NMRERLVALI GQDAYRVGIF TFHAFCNHII ARYPEYFWKA THFTQANDIA
RAEILTELFS SLPHNHPLGS FHPEKGFVFL RDVADRIKHI KSFGLTALEY LGVIQELPKE
YDAINTILTE WPDRMSIKKL DEIERIITNL EALKGTTSIY LVKTLKQALT EAEALGKTEP
LAVWKKDHTE KGDGARILKD AHNQEKIFAV AELYQRYSNA MYERALYDYD DMIIEVAHAL
RDNPILRNTL EEQYQYIMID EFQDTNEAQM SLVKEITQSP LHERRPNVCV VGDDDQAIYK
FQGAEISHLI NFRDTTYADV QTIVLDKNYR STAPILTLAR TLITQGKGRL ENKYEDISKL
LSSENKTLPE GTITIHQTES DVQEYAGVAR AVRATIDNGT EPNDIAILAR GHRELQAILP
YLDRENIPYE YIKKANVFDE PHVKILIDVC AYISSVMRHE ATADYVLPRL LAHPCFQIDR
LGLFKLAVES KEKHTSWTET IMTVDEPHIK KIGTLLAELA IEGETTPLEH ILEAFMEKSG
FKEFYFSRES IKKSPTTYVS FLASLKTFIE ALREWKEGEI LLTSDVQPFV QMHIEHKIPL
ISESPFMKNE HSVQLMSAHA SKGLEFGTVF IISAHDDLWT RSPRTNIAPL PSPLLPLMQP
AGDTEDDFIR LLYVAITRAK HTLHISSHDT QVRYLSDVSN GDTALHTTAF QPLSETSIEA
HENALALYKA PYQEDEWALL KRLVKDYRMP VTHLNNFTNI TKGGPLLFIE QNLLRFPQPM
NSSGVYGTAM HKAIEEHIMY PKYHEGEQAS LAHLVAVFQK EIKRGRLPRT EELRQIERGE
KTLAQFYRST KDYFLPDDKI EVDMKNEGII IDDAHLTGKL DFLRLRNGAY EIIDFKTGKP
FSSWDEAKSD DDKIKLHKYR QQLIVYKILL GNSIHFKDYP AEKSALWFVE EEPITELVLN
TSDEEIERTK KLISAVYKKI VTLDFPDITP YGTTYKGLLQ FEEDLIEQKI
//
