ID A0A0G1NY00_9BACT Unreviewed; 1044 AA.
AC A0A0G1NY00;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=UX00_C0007G0202 {ECO:0000313|EMBL:KKT97942.1};
OS Microgenomates group bacterium GW2011_GWB1_45_17.
OC Bacteria.
OX NCBI_TaxID=1618506 {ECO:0000313|EMBL:KKT97942.1, ECO:0000313|Proteomes:UP000034461};
RN [1] {ECO:0000313|EMBL:KKT97942.1, ECO:0000313|Proteomes:UP000034461}
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:KKT97942.1}.
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DR EMBL; LCKN01000007; KKT97942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NY00; -.
DR PATRIC; fig|1618506.3.peg.676; -.
DR Proteomes; UP000034461; 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; 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; 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 23..334
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 353..634
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1044 AA; 120106 MW; 0D20A3998E85B6B8 CRC64;
MPSQSPLKKP QEKSNAVFSS LYSKLNPEQK KAVDAVEGPV MVFAGPGTGK TQVLAMRAAN
ILRKTDVGPH NILALTFTES AAKAMRDRLI SIIGEDAYYV NIATFHSFCS DVIQSNPEFF
PFSRDAEPLT DLERFTIVEN IIREQAFEAI KPINSPIFYV RDCIKAMQDL KRENVEPDDF
RKLIEYDVLQ LKKAESLPKT EQKQREKNIA KQRELLQVYV LYQQKLREMG RYDYEDMISF
AVHAFEQDEI LLRSYQERLQ YILVDEYQDT NAAQNKVLEL LASYWGKQAN VFVVGDSDQS
LYRFQGASLE NSVAFVKKYP TALFITLTKN YRSTQTILDA ATELIAKNNF THATLLEKFQ
KISAKKSTRT SVPLSATVSY PAQPVYVAAF SSDLAETAYI AEEISTLIKK GTNPSEIAVL
YRTNNDSAAI EDALVKWEIP YEIDSGVDIL DSPVVMQLLT LFRVIYDLRT TREAIDLFTV
LNYEWVGLDA LDLLKLSRHA AEKKQSLFDI VQGNEIKALQ LKKAKETIAF VQKLIQWSKD
DAQKTFPLWF ETVLNDSGFL SWVLKRNDAA EAINKIQSLF REVKIQTSVD KSTKLETFLR
TIERMREHRI AVNEEVLQLQ RKAVKLATAH SAKGREWEYV FIIRAIDGKW GNTRSKDLIP
LPEGVLRYTN IEEKEKNEDD RRVFYVALTR AKKRVTVTYA KTSVSGNRTK ENTQTLFIEE
IPEKLKKEVD TTSFEQSANA VLAKLLHAPV NQTQTIEENE WLSGLLENFV LTPTTLNTYL
ECAYKFKLNT LVKVPRAKED YLAFGTAIHK ALEMLFRSFI EKNKIPSKEF VIGEFEKSLH
REIMTQDEEK ARLNQGRKVL SAYYDEYTSQ FAKPVFLEKF LGYGWPRIYL DDIRIGGRID
KIEWADDAHK TVTVVDYKTG QPKTRGEIEG KTKTSNGDYK RQLLFYKLLT DLDRSFGHKV
EKGMFDFIEK DKQTGKFRRE EFFLPKEEVD GLRKIIKDVM GEVRALYFPR TTHYSVCKEC
EFAQHCWPDG IPEQKAEQMK LISS
//
