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Database: UniProt
Entry: A0A0F9Z5M9_9BACT
LinkDB: A0A0F9Z5M9_9BACT
Original site: A0A0F9Z5M9_9BACT 
ID   A0A0F9Z5M9_9BACT        Unreviewed;       571 AA.
AC   A0A0F9Z5M9;
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=UR30_C0013G0018 {ECO:0000313|EMBL:KKP38994.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP38994.1, ECO:0000313|Proteomes:UP000034765};
RN   [1] {ECO:0000313|EMBL:KKP38994.1, ECO:0000313|Proteomes:UP000034765}
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:KKP38994.1}.
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DR   EMBL; LBOR01000013; KKP38994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9Z5M9; -.
DR   STRING; 1619061.UR30_C0013G0018; -.
DR   PATRIC; fig|1619061.3.peg.1082; -.
DR   Proteomes; UP000034765; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 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; 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; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          1..257
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          258..516
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         21..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   571 AA;  67370 MW;  C4B401EBC859D2EC CRC64;
     MINSNQEKAV KTTDGPVRII AGPGTGKTFT LISRVEYLIR EHKVMPWKIL VISFTNKAAN
     ELSFRLSEKE INNVNVTTFH SLAAQMLRKF LNSDFKIIDA ETQKEILKNI LTEDEFKEVN
     DILRKLQDSK ESLANIEENR LAEIKKSYQK NLDKNNFLDF YQLLKTFHFL LKNDEIVRSK
     CRELFDYIMV DEYQDVNQIQ MDIVNILSEI HQNICIVGDP DQTIYSWRGS DVANMSNFLI
     KYNNAKTIFL SENYRTPKLI LEGASNLIKN NKNRLNTNIN AVKEDEHKIN IWNSLYENQL
     YEILSTVLEN TFGSHSNMQE ADVLDHNCKE LFCFKDMAIL FRTGHQATRV ASFLSRKGYP
     YQIAKDDNFR AKKEIMDFVK ILEYLLDFEK FSADNFEIWL HKKIDDYNSK NKFSEEKRKN
     VLNLLSFGFQ FRDFPPKEGL INFLDSIKNM QDSDNIIEAD KINLLTLHAS KGLEFPIVIL
     WGLEENNLPL KKHIDDSYFL EEERRLMYVG MTRTKQYLHI FSNKRYGDKI FKKSRFINEI
     GDMCFEERIL EQKRENKIRK KEMEKAQMKM F
//
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