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Database: UniProt
Entry: A0A0G1LLM9_9BACT
LinkDB: A0A0G1LLM9_9BACT
Original site: A0A0G1LLM9_9BACT 
ID   A0A0G1LLM9_9BACT        Unreviewed;       818 AA.
AC   A0A0G1LLM9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UW97_C0001G0014 {ECO:0000313|EMBL:KKT96861.1};
OS   Parcubacteria group bacterium GW2011_GWA2_45_15.
OC   Bacteria.
OX   NCBI_TaxID=1618833 {ECO:0000313|EMBL:KKT96861.1, ECO:0000313|Proteomes:UP000034700};
RN   [1] {ECO:0000313|EMBL:KKT96861.1, ECO:0000313|Proteomes:UP000034700}
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   -!- 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:KKT96861.1}.
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DR   EMBL; LCKK01000001; KKT96861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1LLM9; -.
DR   PATRIC; fig|1618833.3.peg.14; -.
DR   Proteomes; UP000034700; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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   GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.91.30; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF63; DNA HELICASE IV; 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   Pfam; PF01396; zf-C4_Topoisom; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 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          133..597
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   818 AA;  94675 MW;  E46F7ED58F47DE22 CRC64;
     MIILVIVVTI SLAFIAYKSQ EASRDKHSLD QLLSLKKDES SFKDAILDFQ NLLQGSWYIS
     DRQYQLWKTK YKHLAGMLNP AFGKVKTQDP FKQLILDFTG YWHEGRKIVD GFNEQFVKQE
     SPVIKHILSE KEIQSNSDQI TAIASDEDNT LLVAGAGTGK TTTILGKLAY LVERVGVKPE
     EILLLSFTGR VVDELNERIG KKFPTNNIKA LTFHSFGLSV VGEVLRQKPD LAFSTTQARL
     KFLNEQFDVL LKNRAYLDRV VEYFAYYFKP VVLEPGFKSL DDYYKYVRTE QNLTLRKEYV
     KSQQEVMIAN FLYINGINYE YEAPYKHKTS DNKYRQYKPD FYLPDYDIYL EHFGVNRKGE
     VHFSQNETQN ALQTKKYQAE MVWKRNLHKQ QQTKLVETFS YEFTERNWTD QLTNKLNTHN
     VQFSRRNIGE IFSSLKANGT VKQMVELFAT FLDLTKSNGY TLANLQSKIV ARNSPRELAF
     FDVFSPIYQA YEDYLKQTNA IDFHDMLIKA ASFINAGRYK ANFRYIIIDE FQDFSMSKCV
     LVKALCDQNP DTKLFCVGDD WQSVFRFTGS DISLMTNFEE SYGFTRKSQL VVTNRFNHNL
     ATISNQFILK NPLQIKKEVR SEKDIFGEAV EIHYKKKTDD DWVLKEVLGS LNTGAHNEKR
     KSTVFLLGRY KHNKPEHLSK YQHELGNLTI DFLTVHSSKG SEADYVVVLD VISGKYGFPS
     EITDDPLLEI VLSKGDLYPH AEERRLMYVA MTRARHKVYI ITDENRPSVF VLELDKSKTP
     DTAIVCQSCG GELVQKKGPY GIFYSCTNFP RCNYKVTK
//
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