RUVA_ALKMQ
ID RUVA_ALKMQ Reviewed; 194 AA.
AC A6TQM4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031};
GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; OrderedLocusNames=Amet_2338;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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. RuvA stimulates,
CC in the presence of DNA, the weak ATPase activity of RuvB.
CC {ECO:0000255|HAMAP-Rule:MF_00031}.
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_00031};
CC -!- SUBUNIT: Forms a complex with RuvB. {ECO:0000255|HAMAP-Rule:MF_00031}.
CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP-
CC Rule:MF_00031}.
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DR EMBL; CP000724; ABR48492.1; -; Genomic_DNA.
DR AlphaFoldDB; A6TQM4; -.
DR SMR; A6TQM4; -.
DR STRING; 293826.Amet_2338; -.
DR EnsemblBacteria; ABR48492; ABR48492; Amet_2338.
DR KEGG; amt:Amet_2338; -.
DR eggNOG; COG0632; Bacteria.
DR HOGENOM; CLU_087936_3_0_9; -.
DR OMA; VGMAVQC; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 CDD; cd14332; UBA_RuvA_C; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00031; DNA_helic_RuvA; 1.
DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000085; RuvA.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR011114; RuvA_C.
DR InterPro; IPR036267; RuvA_C_sf.
DR Pfam; PF07499; RuvA_C; 1.
DR Pfam; PF01330; RuvA_N; 1.
DR SUPFAM; SSF46929; SSF46929; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00084; ruvA; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..194
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_1000057232"
SQ SEQUENCE 194 AA; 21650 MW; E65CEB6A97AF571B CRC64;
MFEYMKGMIV EAQIDKIIVE VNGIGYRINS SINSASQVKI GQVSTLFTHF VLREDEAHLY
GFVDKEELAM FKKLISVSKI GPKVAAGILS TYTPQRLGAY IVSNDAQAIA KSPGVGKKTA
ERMILELKDK IDDSQVEYDQ NFFNHENKNN NEVVDALMAL GYTKHEGEQA ASAVRDTSLS
TEEMIRKALN WLAR