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RUVA_RHOJR
ID   RUVA_RHOJR              Reviewed;         200 AA.
AC   Q0S1C7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 109.
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};
GN   OrderedLocusNames=RHA1_ro06893;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG98659.1; -; Genomic_DNA.
DR   RefSeq; WP_009480136.1; NC_008268.1.
DR   AlphaFoldDB; Q0S1C7; -.
DR   SMR; Q0S1C7; -.
DR   STRING; 101510.RHA1_ro06893; -.
DR   EnsemblBacteria; ABG98659; ABG98659; RHA1_ro06893.
DR   KEGG; rha:RHA1_ro06893; -.
DR   eggNOG; COG0632; Bacteria.
DR   HOGENOM; CLU_087936_2_1_11; -.
DR   OMA; VGMAVQC; -.
DR   Proteomes; UP000008710; 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..200
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT                   /id="PRO_1000002534"
SQ   SEQUENCE   200 AA;  20451 MW;  27E1058637C4B8D9 CRC64;
     MIASVRGEVL EIALDHAVIE SAGVGYRVNA TPATLGGLQR GSEARLVTAM IVREDSMTLY
     GFPDSESKEL FGLLQTVSGV GPRLAMATLA VLEPDALRAA LAEGNVTALT RVPGIGKRGA
     ERMVVELRDK VDAVASTSGA VPLGAGGGGS VRDQIVEALV GLGFPAKQAE QAADSVLAEA
     PESTTSTALR SALSLLGKTR
 
 
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