RUVA_THET8
ID RUVA_THET8 Reviewed; 191 AA.
AC Q9F1Q3; Q5SLK2;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 133.
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=TTHA0291;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11245216; DOI=10.1266/ggs.75.233;
RA Ohnishi T., Iwasaki H., Ishino Y., Kuramitsu S., Nakata A., Shinagawa H.;
RT "Identification and characterization of Thermus thermophilus HB8 RuvA
RT protein, the subunit of the RuvAB protein complex that promotes branch
RT migration of Holliday junctions.";
RL Genes Genet. Syst. 75:233-243(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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. 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.
CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP-
CC Rule:MF_00031}.
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DR EMBL; AB048605; BAB18786.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70114.1; -; Genomic_DNA.
DR RefSeq; WP_011174059.1; NC_006461.1.
DR RefSeq; YP_143557.1; NC_006461.1.
DR PDB; 1IXR; X-ray; 3.30 A; A/B=1-191.
DR PDB; 1IXS; X-ray; 3.20 A; A=130-191.
DR PDBsum; 1IXR; -.
DR PDBsum; 1IXS; -.
DR AlphaFoldDB; Q9F1Q3; -.
DR SMR; Q9F1Q3; -.
DR IntAct; Q9F1Q3; 1.
DR STRING; 300852.55771673; -.
DR EnsemblBacteria; BAD70114; BAD70114; BAD70114.
DR GeneID; 3168157; -.
DR KEGG; ttj:TTHA0291; -.
DR PATRIC; fig|300852.9.peg.291; -.
DR eggNOG; COG0632; Bacteria.
DR HOGENOM; CLU_087936_3_0_0; -.
DR OMA; VGMAVQC; -.
DR PhylomeDB; Q9F1Q3; -.
DR EvolutionaryTrace; Q9F1Q3; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..191
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_0000094701"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1IXR"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1IXR"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:1IXR"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1IXR"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1IXR"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1IXR"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:1IXS"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:1IXS"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1IXS"
SQ SEQUENCE 191 AA; 20414 MW; 1DA0CADFDD5EBC3B CRC64;
MIRYLRGLVL KKEAGGFVLL AGGVGFFLQA PTPFLQALEE GKEVGVHTHL LLKEEGLSLY
GFPDEENLAL FELLLSVSGV GPKVALALLS ALPPRLLARA LLEGDARLLT SASGVGRRLA
ERIALELKGK VPPHLLAGEK VESEAAEEAV MALAALGFKE AQARAVVLDL LAQNPKARAQ
DLIKEALKRL R
