ID A0A0G0FZD8_9BACT Unreviewed; 971 AA.
AC A0A0G0FZD8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=US40_C0017G0004 {ECO:0000313|EMBL:KKQ24308.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_37_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618486 {ECO:0000313|EMBL:KKQ24308.1, ECO:0000313|Proteomes:UP000034917};
RN [1] {ECO:0000313|EMBL:KKQ24308.1, ECO:0000313|Proteomes:UP000034917}
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:KKQ24308.1}.
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DR EMBL; LBSV01000017; KKQ24308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0FZD8; -.
DR PATRIC; fig|1618486.3.peg.985; -.
DR Proteomes; UP000034917; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IPR011335; Restrct_endonuc-II-like.
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 SUPFAM; SSF52980; Restriction endonuclease-like; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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 1..296
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 297..605
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 971 AA; 112417 MW; 462564F0D0BA842B CRC64;
MLNDEQKKAS EYNKGPLLIV AGAGTGKTTV IVEKIKYLLK KKLAKPEEIL ALTFTEKAAN
EMEERVDKEI PYGYFQMWIS TFHSFADQVL KENATEIGLS PSYRLMTEAE TVIFLRKNIF
LFNLKYFRPL GNPNKFLQSL LQHFSRLRDE NIDPQEYVDF AKKTKTEDII EKEKALELAD
AYKTYQALKL KENFFDYADL IFYLDKLFRT RKNILEIYQK KFKYVLVDEF QDTNIAQYDL
IRLICPPSSN PLLTVVGDDS QAIYKFRGAS VSNILNFMKD YQNAKQISLL KNYRSNQIIL
DIAYRLIKNN DPDTLEAKLG ISKKLVADNN SNKSDKNAVA FNFSESAEDE ADFVAKEITK
LNKKFKYSDI AILTRANNHA QPFINALLRH GIPFQFLGPS TLYKQPEVKD LIAYLKVLNN
PEDSVSLYRI LNMDIFNIEI KDLTFLNTFA KKTNLPLFQA IETCLGLSEK NLYQEEFENY
RRLIPYMKKE TKEKLLIIYQ MIKKHFAKVK KDTAGQILFY FLEDSKLLPH LANFKTEKDE
EIALNISKFF NRLKAYESDH EDASINAVVD FIDMSVELGE SPIASKTDIG QFNAVNIITA
HSAKGLEFEV VFLANLTKGR FPTNERNEII PIPDELIKEI LPTGDYHIEE ERRLFYVSIT
RAKEKLYMTA SRFYGAGKRE QKISPFVIES LGEENIKKTV TIKKEEQAQL SIFDFKKPTS
PIIKQSYFPN TFSYTQLDTY IRCPLHYKYQ YVLKIPTPVT SPLAFGDTIH RTLQNFYNEF
LKDKNIDENR LLQIYKKNWL PAGYSSAAYE ETRKKSGENT LLDYKNKFHK KNLNLIAIEK
PFKIKITPDI YIVGKIDRVD NIGDDKIEII DYKTGRMPKE SDLKKSLQLS IYAMAAIDYG
LYNKKLPQVL LTFFYLEEGK KISFQKSTED LEETKSKIIE IVGKIRNNEF PVTTGPGLAF
CSFPMICEAC Q
//
