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Database: UniProt
Entry: A0A1F6AP24_9BACT
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ID   A0A1F6AP24_9BACT        Unreviewed;       617 AA.
AC   A0A1F6AP24;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=A2960_04720 {ECO:0000313|EMBL:OGG26252.1};
OS   Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_39_12b.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1798388 {ECO:0000313|EMBL:OGG26252.1, ECO:0000313|Proteomes:UP000176609};
RN   [1] {ECO:0000313|EMBL:OGG26252.1, ECO:0000313|Proteomes:UP000176609}
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:OGG26252.1}.
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DR   EMBL; MFJR01000012; OGG26252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6AP24; -.
DR   Proteomes; UP000176609; 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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 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; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          7..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..529
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   617 AA;  71536 MW;  8A6244F1D8978D55 CRC64;
     MESNLLKTLN PIQQQAVITT EGPILVLAGA GSGKTKVLTY KATYLILVKM IEPDNILMLT
     FTNKAANEMK ERISKLLITH NSQPTTNLPF AGTFHWLCAK ILRKEGSFIG IPPNYIIYDQ
     QDQKEALKQV ITELNLDKKK FNPSLAAALI SEAKNELITA QEYPQYAHGY FQQEIAKIFL
     AYQKVLRENN ALDFDDLILM TVNLFQKVDE VARIYQNKFR YVLVDEYQDT NRAQFILTKL
     LAKLWRNLCV VGDASQSIYG WRGADYRNIF NFNKDYSDVK VFHLEQNYRS TQNILDAAYA
     VISKNNSHPI LKLWTNQTSG EPIVVYQASS EHDEAEYIIN QIIEIKYRFP EFQYSDFAVL
     YRTNAQSRVL EETLILRGIP YILVGGVRFY ERKEIKDVLA YLRLLVNPKD KISYKRIEKI
     GKKRLEKFVV FESRYKEKIE SNNLTTLALL DEVILETEYL ELYDKDNEED LSRLENIKEL
     RSVASEFTDL NLFLENVALV EQEHLPDHPL IGKKIKAAVT LMTLHAAKGL EFKIVFLVGM
     EEGLFPHSRS LLEPLELEEE RRLCYVGITR AMKRLYLTFA QRRLFFGLRS SNAVSRFITE
     IPEDLTQIHQ TYKFTTT
//
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