RUVB_MARMS
ID RUVB_MARMS Reviewed; 337 AA.
AC A6VXD3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; OrderedLocusNames=Mmwyl1_2190;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_00016};
CC -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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DR EMBL; CP000749; ABR71112.1; -; Genomic_DNA.
DR RefSeq; WP_012069891.1; NC_009654.1.
DR AlphaFoldDB; A6VXD3; -.
DR SMR; A6VXD3; -.
DR STRING; 400668.Mmwyl1_2190; -.
DR EnsemblBacteria; ABR71112; ABR71112; Mmwyl1_2190.
DR KEGG; mmw:Mmwyl1_2190; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_6; -.
DR OMA; IHRMSRP; -.
DR OrthoDB; 874197at2; -.
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: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; DNA damage; DNA recombination; DNA repair; Helicase;
KW Hydrolase; Nucleotide-binding; SOS response.
FT CHAIN 1..337
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_1000074088"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ SEQUENCE 337 AA; 37492 MW; 125DE416D6AE1CB5 CRC64;
MIEQDRIISA ELKGNDRQVD RAIRPQALAE YIGQPVVREQ MEIFIQAARQ RGEPLDHTLI
FGPPGLGKTT LANIIGNEMG AEVRTTSGPV LERAGDLAAL LTNLNEGDIL FIDEIHRLSP
AIEEVLYPAM EDYQLDIMIG EGPAARSIKI ELPPFTLVGA TTRAGLLTSP LRDRFGIVQR
LEFYDVESLT TIVARSAGKM GVELDQSGCF EVARRSRGTP RIANRLLRRV RDVAQVSGEV
LVGQKVAQRA LDMLSVDSQG FDHLDRRMLL TMIEKFDGRP VGLDSVSAAL GEDKDTIEDV
IEPFLIQQGF IIRTPRGRQV TKRAYEHFNY QLPSDFK