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
//