RUVA_IDILO
ID RUVA_IDILO Reviewed; 205 AA.
AC Q5QYU4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=IL1086;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV81926.1; -; Genomic_DNA.
DR RefSeq; WP_011234337.1; NC_006512.1.
DR AlphaFoldDB; Q5QYU4; -.
DR SMR; Q5QYU4; -.
DR STRING; 283942.IL1086; -.
DR EnsemblBacteria; AAV81926; AAV81926; IL1086.
DR KEGG; ilo:IL1086; -.
DR eggNOG; COG0632; Bacteria.
DR HOGENOM; CLU_087936_0_0_6; -.
DR OMA; VGMAVQC; -.
DR OrthoDB; 1370858at2; -.
DR Proteomes; UP000001171; 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; 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; Reference proteome; SOS response.
FT CHAIN 1..205
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_0000224873"
FT REGION 136..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 22729 MW; FD2D1432086CCFDE CRC64;
MIGHIQGVLT SKQPPEVVLD VQGIGYEIQL PMTCFYQLPP VGETIKLITH FVVREDAQLL
YGFISASERS LFRLLLKTQG VGPKLALAIL SGMSADEFVM AVNQNDVTRL VKLPGVGKKT
AERLVIEMRD RLKDWQPSTP FTDRAPLDSQ GMDAREHPAD ARTDAISALQ SLGYKENQAE
KALQKVYSAE HNSETLIRLA LKQLS