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RUVA_FRATW
ID   RUVA_FRATW              Reviewed;         216 AA.
AC   A4IY85;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=FTW_1070;
OS   Francisella tularensis subsp. tularensis (strain WY96-3418).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=418136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WY96-3418;
RX   PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA   Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA   Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA   Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA   Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT   "Complete genomic characterization of a pathogenic A.II strain of
RT   Francisella tularensis subspecies tularensis.";
RL   PLoS ONE 2:E947-E947(2007).
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; CP000608; ABO46886.1; -; Genomic_DNA.
DR   RefSeq; WP_003026241.1; NC_009257.1.
DR   AlphaFoldDB; A4IY85; -.
DR   SMR; A4IY85; -.
DR   KEGG; ftw:FTW_1070; -.
DR   HOGENOM; CLU_087936_0_0_6; -.
DR   OMA; KAPAVMA; -.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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   SMART; SM00278; HhH1; 2.
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; SOS response.
FT   CHAIN           1..216
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT                   /id="PRO_1000002453"
SQ   SEQUENCE   216 AA;  23563 MW;  7934CA4C1791B74E CRC64;
     MISFIKGVLI EKDPTALLID VNGIGYEVFV PMTTFYTLGD IDSQVSLYTH FIVREDAQQL
     YGFKSKVDKK VFQELIKVNG IGARTAIAIL SGMDSKTLLH CIENKDYALL ATVPGIGKKT
     AERLVVEIYD KLLKMANEIY AQTSGTTTTS QDSQAQQAPT SVVLANSIFN ESVDALLALG
     YKQKDAEKMA RSAMGDATTA AEVIRKALQG SIKSKR
 
 
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