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Protein

Holliday junction ATP-dependent DNA helicase RuvA

Gene

ruvA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.UniRule annotation

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, SOS response

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-305-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Holliday junction ATP-dependent DNA helicase RuvAUniRule annotation (EC:3.6.4.12UniRule annotation)
Gene namesi
Name:ruvAUniRule annotation
Ordered Locus Names:TTHA0291
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Holliday junction ATP-dependent DNA helicase RuvAPRO_0000094701Add
BLAST

Interactioni

Subunit structurei

Forms a complex with RuvB.

Binary interactionsi

WithEntry#Exp.IntActNotes
ruvBQ5SL871EBI-1034659,EBI-1034647

Protein-protein interaction databases

IntActiQ9F1Q3. 1 interaction.
MINTiMINT-88028.
STRINGi300852.TTHA0291.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Beta strandi14 – 207Combined sources
Beta strandi22 – 298Combined sources
Helixi32 – 376Combined sources
Beta strandi42 – 487Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 7511Combined sources
Beta strandi76 – 783Combined sources
Helixi82 – 9110Combined sources
Helixi94 – 1029Combined sources
Helixi106 – 1094Combined sources
Helixi117 – 12711Combined sources
Turni128 – 1303Combined sources
Helixi144 – 15512Combined sources
Helixi160 – 17314Combined sources
Helixi179 – 1879Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IXRX-ray3.30A/B1-191[»]
1IXSX-ray3.20A130-191[»]
ProteinModelPortaliQ9F1Q3.
SMRiQ9F1Q3. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F1Q3.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105KA4. Bacteria.
COG0632. LUCA.
HOGENOMiHOG000057115.
KOiK03550.
OMAiRNQETIF.
OrthoDBiEOG679THG.
PhylomeDBiQ9F1Q3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00031. DNA_helic_RuvA.
InterProiIPR011114. DNA_helicas_Holl-junc_RuvA_C.
IPR013849. DNA_helicase_Holl-junc_RuvA_I.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR000085. RuvA.
IPR010994. RuvA_2-like.
[Graphical view]
PfamiPF07499. RuvA_C. 1 hit.
PF01330. RuvA_N. 1 hit.
[Graphical view]
SMARTiSM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF46929. SSF46929. 1 hit.
SSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00084. ruvA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9F1Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRYLRGLVL KKEAGGFVLL AGGVGFFLQA PTPFLQALEE GKEVGVHTHL
60 70 80 90 100
LLKEEGLSLY GFPDEENLAL FELLLSVSGV GPKVALALLS ALPPRLLARA
110 120 130 140 150
LLEGDARLLT SASGVGRRLA ERIALELKGK VPPHLLAGEK VESEAAEEAV
160 170 180 190
MALAALGFKE AQARAVVLDL LAQNPKARAQ DLIKEALKRL R
Length:191
Mass (Da):20,414
Last modified:March 1, 2001 - v1
Checksum:i1DA0CADFDD5EBC3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048605 Genomic DNA. Translation: BAB18786.1.
AP008226 Genomic DNA. Translation: BAD70114.1.
RefSeqiWP_011174059.1. NC_006461.1.
YP_143557.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70114; BAD70114; BAD70114.
GeneIDi3168157.
KEGGittj:TTHA0291.
PATRICi23955537. VBITheThe93045_0291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048605 Genomic DNA. Translation: BAB18786.1.
AP008226 Genomic DNA. Translation: BAD70114.1.
RefSeqiWP_011174059.1. NC_006461.1.
YP_143557.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IXRX-ray3.30A/B1-191[»]
1IXSX-ray3.20A130-191[»]
ProteinModelPortaliQ9F1Q3.
SMRiQ9F1Q3. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9F1Q3. 1 interaction.
MINTiMINT-88028.
STRINGi300852.TTHA0291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70114; BAD70114; BAD70114.
GeneIDi3168157.
KEGGittj:TTHA0291.
PATRICi23955537. VBITheThe93045_0291.

Phylogenomic databases

eggNOGiENOG4105KA4. Bacteria.
COG0632. LUCA.
HOGENOMiHOG000057115.
KOiK03550.
OMAiRNQETIF.
OrthoDBiEOG679THG.
PhylomeDBiQ9F1Q3.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-305-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9F1Q3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00031. DNA_helic_RuvA.
InterProiIPR011114. DNA_helicas_Holl-junc_RuvA_C.
IPR013849. DNA_helicase_Holl-junc_RuvA_I.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR000085. RuvA.
IPR010994. RuvA_2-like.
[Graphical view]
PfamiPF07499. RuvA_C. 1 hit.
PF01330. RuvA_N. 1 hit.
[Graphical view]
SMARTiSM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF46929. SSF46929. 1 hit.
SSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00084. ruvA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of Thermus thermophilus HB8 RuvA protein, the subunit of the RuvAB protein complex that promotes branch migration of Holliday junctions."
    Ohnishi T., Iwasaki H., Ishino Y., Kuramitsu S., Nakata A., Shinagawa H.
    Genes Genet. Syst. 75:233-243(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiRUVA_THET8
AccessioniPrimary (citable) accession number: Q9F1Q3
Secondary accession number(s): Q5SLK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2001
Last modified: November 11, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.