ID A0A520H3P3_9BURK Unreviewed; 351 AA. AC A0A520H3P3; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 29-SEP-2021, entry version 10. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000256|HAMAP-Rule:MF_00016}; DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_00016}; GN Name=ruvB {ECO:0000256|HAMAP-Rule:MF_00016, GN ECO:0000313|EMBL:RZM01076.1}; GN ORFNames=EOP73_14265 {ECO:0000313|EMBL:RZM01076.1}; OS Variovorax sp. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=1871043 {ECO:0000313|EMBL:RZM01076.1, ECO:0000313|Proteomes:UP000317610}; RN [1] {ECO:0000313|EMBL:RZM01076.1, ECO:0000313|Proteomes:UP000317610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PMG_050 {ECO:0000313|EMBL:RZM01076.1}; RX PubMed=30498029; DOI=.1073/pnas.1812668115; RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J., RA Murphy G.P., McGenity T.J., Murrell J.C.; RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018). CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures CC cruciform structure in supercoiled DNA with palindromic sequence, CC indicating that it may promote strand exchange reactions in homologous CC recombination. RuvAB is a helicase that mediates the Holliday junction CC migration by localized denaturation and reannealing. CC {ECO:0000256|HAMAP-Rule:MF_00016}. 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=3.6.4.12; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00016}; CC -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000256|HAMAP-Rule:MF_00016}. CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|HAMAP- CC Rule:MF_00016}. 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:RZM01076.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SEGK01000263; RZM01076.1; -; Genomic_DNA. DR Proteomes; UP000317610; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140603; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00016; DNA_helic_RuvB; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041445; AAA_lid_4. DR InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008824; RuvB-like_N. DR InterPro; IPR008823; RuvB_C. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR42848; PTHR42848; 1. DR Pfam; PF17864; AAA_lid_4; 1. DR Pfam; PF05491; RuvB_C; 1. DR Pfam; PF05496; RuvB_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00635; ruvB; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00016}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00016}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP- KW Rule:MF_00016}. FT DOMAIN 63..191 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 71..78 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 351 AA; 38675 MW; 08F72C4DA38D7B82 CRC64; MTIQTDDFAP APPRMVSAAP ASPNEEAIER ALRPRLLDEY VGQAKVREQL EIFIGAAKKR SEALDHVLLF GPPGLGKTTL SHIIAAELGV NLRQTSGPVL EKPKDLAALL TNLERNDVLF IDEIHRLSPV VEEILYPALE DYQIDIMIGE GPAARSIKLD LQPFTLVGAT TRAGMLTNPL RDRFGIVSRL EFYTPEELAR IVTRSARLLD VPTDAEGGFE IARRSRGTPR IANRLLRRVR DYAQVKGEGR ITQEIANRAL AMLDVDPQGF DLMDRKMLEA VIHRFDGGPV GLDNIAASIG EEPGTIEDVI EPYLIQQGYL QRTPRGRIAT LAAYRHLGVA PPQRAEGGLF G //