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Database: UniProt
Entry: A0A0U3PUM0_9ACTN
LinkDB: A0A0U3PUM0_9ACTN
Original site: A0A0U3PUM0_9ACTN 
ID   A0A0U3PUM0_9ACTN        Unreviewed;       988 AA.
AC   A0A0U3PUM0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=AS200_27720 {ECO:0000313|EMBL:ALV35413.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV35413.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV35413.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV35413.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP013743; ALV35413.1; -; Genomic_DNA.
DR   RefSeq; WP_058925023.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3PUM0; -.
DR   STRING; 1725411.AS200_27720; -.
DR   KEGG; scx:AS200_27720; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000068029; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT   DOMAIN          11..301
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          302..577
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          675..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   988 AA;  109328 MW;  BCB692810B167C6E CRC64;
     MNVDVEQALG GWLTPEQYGA AVAPEDEVLA LAGAGSGKSR TLAGRVAYKI ANGASPESVV
     AFTFTEKAGE QIKTRVAQAL KVCGVDPLLV GGMYIGTIHA WCRRVLGDMD ARYRQFDVLD
     EMQFLVYLIS RYPKLNINPL RDAHPTAKGN RRGYFETLKE LSRAWHMMND ELLDPAQIAA
     EDPALGEALE RLRDQMEQDN FIDFSLMQRL VVEALEAQEP GAVQALALLR HVLVDEYQDV
     NVVQERLIGL MHQNSETLFV VGDDDQAIYG WRGADVTNIL EFNRRYPTAA VHKLLTNFRS
     TSAIVEAAGD FAAQELGPSR LPKQLHAAAN HDPREFAVLN FPVRAVEAEF VAERIDELLG
     TAYEESDGTV RGLTPADFAI LMRSTGQPES DGTKRHTAYI QALDARNIPY DLNAGGQLFD
     RAQPAAVRSA FELLRDAMPD RTQVEDLFHS QLKKAFPQAD LSRVIRVFAD WGRRIHAPIA
     PGLPRQRLFP QQLLHDLLEA LDVANSGFDD GVMADLGTFS RILQDIETVY LSIDGKPRFG
     ELLNFLQNVA GDGYETDNQM MARPDAVTVS TVHKAKGLEF PVVFVVDVEN GRFPGRRRSY
     DGWIPETLIQ QAIDNGSYQT GPHDQARLFY TAITRAERFL YVTGSALLPG GKRLTKTSPY
     AVRLNHPEIR RDLLDPAAPP RVVPPVEAQR RRGDESVLPT TYSQIHTFMR CPHAYKLSVV
     NGFSPPIPEL FGFGRAVHAA VGKLHQAYKD KAPTSDEARA IAENMFHLKH VAPSSDPVDR
     PGAYERAKQK SSDIVSDYVD KYGTDFELKR QVELPFEIPV EGAVISGAID LLLSVDDADT
     IHDAKVIDFK TMAGGPEPTN NPDLNWEDLS LQVQLYGRGA EQVHGMNART GAVHLLKDGQ
     RVQVPVDADA VDAAVANVEW AVSRITDGDF PQRGSRTKCG DCDFAQICSK KLQPFKTEEE
     PPDLHLPDGT NGKRFLKVSA FSRTGPNE
//
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