ID A0A1F6WC05_9BACT Unreviewed; 993 AA.
AC A0A1F6WC05;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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};
DE Flags: Fragment;
GN ORFNames=A3F19_01320 {ECO:0000313|EMBL:OGI79438.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_12_FULL_37_29.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801759 {ECO:0000313|EMBL:OGI79438.1, ECO:0000313|Proteomes:UP000177052};
RN [1] {ECO:0000313|EMBL:OGI79438.1, ECO:0000313|Proteomes:UP000177052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGI79438.1}.
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DR EMBL; MFUJ01000010; OGI79438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6WC05; -.
DR Proteomes; UP000177052; Unassembled WGS sequence.
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; -; 2.
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: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}.
FT DOMAIN 1..316
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 317..605
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGI79438.1"
SQ SEQUENCE 993 AA; 115244 MW; 84B9C45C0089503A CRC64;
AQREAVDTID GPVMVVAGPG TGKTQILALR IGNILLKTDT SADGVLCLTF TNSAVSAMRE
RLRKYIGREA SKVKVATFHS FGMEILGKYF SILGLYAKPE LMDEKDIIAL CDEVLHKNDW
KYIRPRSETS RYFRDLKSFI SFLKRERITP EHFKNEIEKE IKNIERDPLS ISTRGERKGE
MKKDVERKME GLHRTLEAVK FYSLYEIEKK EKNLFDFDDI LGALVLIVEE SIEAKNYIRE
NFLYVLIDEH QDSSGVQNEF LEKVWKEEDK PNIFVVGDDR QLIYGFGGAS LEYFENFKDT
FGKAKLISLE ENYRSTQKIL DSAHDLLRSS ITKNRLKSNR KENHALRLVE AYYPRDEIIF
IALEIKDKIK KRGSGEHGRT SIDPNDIAIL VPKNRQVKST ITILKDMGVP VAGVAMMDFF
DVPESSAFLR VLKIIANPGD GALLATSFFD KFSLISPFKA HEFIKGNKMR EFSLLDVQEE
TPTLFSTQGR SALGENKQND VNIWIQKLKL WLSYSTLPLY AFIQKVGTEF LLDNAKNHEE
LMIRIEVLRT MLHLVLFETE KHSKMSLKVF LDFLERIENY RENISLAVFS PNDGVKVLTL
HGSKGLEFDH VYIAHMDEKS FSGSKREGFI LPEYIKEKVE KRDEIVLKRE LYVAMTRAKR
FCTISYALQS HTGGDQELAH IVSDLSENFE KQKAHETEKI ILKNDERAYV EKKSNEERNI
NLEDLIKLVA KDYEDRKVSV SLLNNFFECS WKWYFRNLLQ LPEPKQESLE FGNIVHGSID
AVLKLEKKLN EKDLKNMVLH QVRKSGFGDE RKEKELFKLA FNILSKWVNE RLDKINNKRE
SEQSVSVKDN RFPNLNIYGK IDLIEILDKD NVRVTDFKTG SVRKKGDIEK IDKEGRMSSY
LRQLVMYSYL IKQSSKLKIN VNESCLEFLE AKNEKETFYN RVITSKEIDL LIKDIKDYDQ
LIKNGKWVNR PCNYNSYGKN TECEYCKLAE IYK
//
