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Database: UniProt
Entry: A0A0G1R923_9BACT
LinkDB: A0A0G1R923_9BACT
Original site: A0A0G1R923_9BACT 
ID   A0A0G1R923_9BACT        Unreviewed;       659 AA.
AC   A0A0G1R923;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UX39_C0008G0021 {ECO:0000313|EMBL:KKU26558.1};
OS   Candidatus Magasanikbacteria bacterium GW2011_GWA2_46_17.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1619042 {ECO:0000313|EMBL:KKU26558.1, ECO:0000313|Proteomes:UP000034175};
RN   [1] {ECO:0000313|EMBL:KKU26558.1, ECO:0000313|Proteomes:UP000034175}
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:KKU26558.1}.
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DR   EMBL; LCMA01000008; KKU26558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1R923; -.
DR   PATRIC; fig|1619042.3.peg.328; -.
DR   Proteomes; UP000034175; 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; 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; 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; 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};
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          5..304
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          305..563
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   659 AA;  74980 MW;  B914F4F994C3AF4B CRC64;
     MEHLIGLNEQ QKQAVLQKDG PVLIIAGAGA GKTKTITHRI LHLIKGGADP RSILAVTFTN
     KAAKEMRERV HTLLASDKSL NFPTSDFSPV TSYMSHVTCS PFISTFHALG VHILKENARL
     LNIPRHFTIL DKSDSSKLIK DAMDQEEIDR KNFDPALIQN LISREKGDAV TCAEFEAKAS
     TEYIPQIVAK VWTRYEASLV KEKALDFDDL LLKTARLLKE NAGVREHYQN IWRHIHIDEY
     QDTNRVQHLI AKYLAEKHKN ICVVGDPDQL IYEWRGAHMK NIMGFEKDYP NAKIIFLEEN
     YRSTQTILTA ANRVIAKNKM RKEKNLFTKN GEGERIGLME AYDENDEARF VAQKCKELID
     ERAVSASEIA VLYRANFQSR ALEEAMLQNE VPYQVLGIRF FERKEVKDII AYLKAALNPE
     GLSDLKRIIN VPPRGLGKVT VLKVFAGQES TLPAATRKKV ADFKNVLVEI KNTAFKEKPS
     QTIKYILRAS GMEEGFRKGG NEEAERLENI KELVTFATKY DIYANPEEGT ERFLEDAALA
     SDQDELMKNK SAVKLMTVHA AKGLEFEYVF ITGLEDDLFP HKKLNSGGFD ERQSEEERRL
     FYVALTRAKK KLYLSYASVR TIFGSKQVNV PSEFIFDVDD ELVEKEERFE GGGKIIYLD
//
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