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Database: UniProt
Entry: A0A1F4ZAT9_9BACT
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ID   A0A1F4ZAT9_9BACT        Unreviewed;       945 AA.
AC   A0A1F4ZAT9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=A2989_00820 {ECO:0000313|EMBL:OGD03358.1};
OS   Candidatus Amesbacteria bacterium RIFCSPLOWO2_01_FULL_48_25.
OC   Bacteria; Candidatus Amesbacteria.
OX   NCBI_TaxID=1797259 {ECO:0000313|EMBL:OGD03358.1, ECO:0000313|Proteomes:UP000177080};
RN   [1] {ECO:0000313|EMBL:OGD03358.1, ECO:0000313|Proteomes:UP000177080}
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   -!- 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:OGD03358.1}.
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DR   EMBL; MEXN01000007; OGD03358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4ZAT9; -.
DR   STRING; 1797259.A2989_00820; -.
DR   Proteomes; UP000177080; 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: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   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          5..292
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          293..575
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   945 AA;  107351 MW;  E9BEB924F5E9C2F7 CRC64;
     MSEEKTLNKQ QLEAVTHSSG PLLIIAGAGT GKTTVVTERV KWLIAQGLAQ PSEILCLTFT
     EKAAGQMQER IDVALPYGYT QMWVSTFHSF CDRILREEGL HLGLDTNYKL LTAPDAVSLL
     KNHLFDFDLN YYRPLGNPAK FLTAALQHFN RLQDEDVSPS QYLAWSKKKD SNYQELAGLY
     SDYSDLKVKE GVLDFSDLIS YSLKLFRDRP SVLKLYQQKF KYILVDEFQD TNYAQNQLIN
     LLASRNRNLT VVADDDQAIY RWRGAAISNV IQFRKNYSDA KLITLVQNYR STQGILDKAH
     TLIQNNNPDR LEVKEKIDKK LTSVRKIKGE KIELLHFDRV ESEADAVAKK IKEILTNDSK
     LTAKDFAILV RANAHAEPFV RALSHHGIPH QFLGPGRLFH QPEIKDLIAY LKVLYNFEDN
     VSFYRVLAME FFSIPARDLA VITNLARKQN LSLFAASEQS DLPSVKLLVD LIDRHLHLVP
     KETAGQILYD FLEKSGLLKA ILDYRTPIDE IKAQNIMKFF NKLKSFETQN SDASVHTIVD
     WLNLSSDMGE SPQAAEVDWG QNDAVNILTV HSAKGLEFPV VFLVNLVVDR FPSRSRSEPI
     PIPDALIKEI LPEGDSHLQE ERRLFYVGLT RAKDLLFLTA ADFYGEGKRI KKLSPFIAET
     LGPIQSSAHP AIQPSLLDWQ PARIATQSVA GGKPIPITYL SYSQIQTFLD CPLHYKAKYI
     LKIPTPTSAA SSFGNTIHAT LKEFFTNKGQ TDVLDLLKKN WSSEGYTSKK HEQAYFDRGQ
     KYLTEYLEKN FDPKHLPIKL EEPFIVPLPA GRQVFLKIGG KIDRVDLLPN GKIEIIDYKT
     SVTLPTQKDA DKDLQLSFYA LVATLLREPP FNRKPEDVLL SLYFFDQQKK ISTTRTSTQL
     EEAKQQIMSY ADQISRSDFH CSGSQLCRIC DYKILCDYAQ VDNAQ
//
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