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Database: UniProt
Entry: A0A0G0UKN4_9BACT
LinkDB: A0A0G0UKN4_9BACT
Original site: A0A0G0UKN4_9BACT 
ID   A0A0G0UKN4_9BACT        Unreviewed;       960 AA.
AC   A0A0G0UKN4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UT84_C0006G0009 {ECO:0000313|EMBL:KKR50807.1};
OS   Candidatus Curtissbacteria bacterium GW2011_GWA1_40_16.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1618405 {ECO:0000313|EMBL:KKR50807.1, ECO:0000313|Proteomes:UP000034531};
RN   [1] {ECO:0000313|EMBL:KKR50807.1, ECO:0000313|Proteomes:UP000034531}
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   -!- 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:KKR50807.1}.
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DR   EMBL; LBYI01000006; KKR50807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0UKN4; -.
DR   PATRIC; fig|1618405.3.peg.401; -.
DR   Proteomes; UP000034531; 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:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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:SF48; ATP-DEPENDENT HELICASE/NUCLEASE SUBUNIT A; 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}; Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          1..282
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          283..584
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         4..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   960 AA;  110056 MW;  AFD339328954CCA9 CRC64;
     MIIAGAGTGK TTVIARRIAY IIEKKLAKPA EILALTFTDK AAGEMEERVD QLVPYGFTDT
     WISTFHAFGD RILRDNAFDL GISPDFKVLS KPQQVLFFQQ NIFKFNLDYY RPLANPTKFI
     SAVLSFFSRL KDENVSPEEF VQKIKNQKSK IKSKEDIEEI KKLQELANAY TTYEDLKTKA
     GLLDFGDQVT KTIGLFKKRP KILKGYQNHF KYIMVDEYQD TNFAQNELVK LLSSNHKNIC
     VVGDDDQSIY KFRGAAISNI MRFKKDYKNA KQVVLTQNYR STQAILDCSY RLIRHNDPDR
     LEVQNKIDKK LKSTKKEYGQ TPKEIYADTL SQEADLVAAE IEKLTKKTQN SKLKTQNLLY
     RDIAILVRAN SSADPFLRAL NMRGIPHKFV GSSGLYQQEE VAVLISFLTA ISNFEDSLNL
     YNLLVSDIYE MPPVDAIKLT SWANRKNKSL YYLLKNLDKI TNDDLELSKD SEAVTKRVIE
     DLDEEINLSK KQNAGRVLFD FLKRTNYLKK LEKENTIEAQ IKIQNIAKFF DKVREFTDIA
     SAETVNQFIN YLDALRGAGD DPATVEFDPD TDAVNVMTVH SAKGLEFPVV FLVNLISDKF
     PSRSRPEAIE VPKELIKEDL PQGDWHREEE RRLFYVGATR AKDLLYFSWA RDTGSFRIKK
     ISPFVLEALD KVKAGGELVK LSPLEKIAQF EQSAPKTHTQ TAFFDVDVLK LTQGSIDDYL
     TCAYKYRYIH ILKIPILRHH AIVYGSALHA AVAEFLRAKK RGKIISQNQL FEIFENAWDS
     EGFLTVEHEE KRKEQGKLAL SAFWKRESKT KDLPSLIESK FKFSLEGITV VGRYDRVDVK
     PGSKIEIIDY KSSENIDEER AKSQAKESTQ LAIYALSYWR AYRILPEKLT LHFLETGIEG
     SYAPIQKDIE KTEKLITDTA QKINRDIKSN HFTANPKYFG REPACVYCAY KSICPFSLAK
//
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