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Protein

Crossover junction endodeoxyribonuclease RusA

Gene

rusA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Corrects the defects in genetic recombination and DNA repair associated with inactivation of ruvAB or ruvC.

Catalytic activityi

Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).

Cofactori

Mg2+CuratedNote: Binds 1 Mg2+ ion per subunit.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi70MagnesiumCurated1
Metal bindingi72MagnesiumCurated1
Metal bindingi91MagnesiumCurated1

GO - Molecular functioni

  • crossover junction endodeoxyribonuclease activity Source: EcoCyc
  • magnesium ion binding Source: InterPro
  • recombination hotspot binding Source: EcoCyc

GO - Biological processi

  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6306-MONOMER.
ECOL316407:JW0538-MONOMER.
BRENDAi3.1.22.4. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Crossover junction endodeoxyribonuclease RusA (EC:3.1.22.4)
Alternative name(s):
Holliday junction nuclease RusA
Holliday junction resolvase
Gene namesi
Name:rusA
Synonyms:rus, ybcP
Ordered Locus Names:b0550, JW0538
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG20283. rusA.

Subcellular locationi

GO - Cellular componenti

  • Holliday junction resolvase complex Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16R → Q: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi17Y → L: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi19R → Q: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi58R → Q: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi68R → Q: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi69R → Q or A: Loss of ability to promote DNA repair. Great loss of Holliday junction resolvase activity. No effect on DNA binding. 1 Publication1
Mutagenesisi70D → N: Reduces junction resolution 80-fold. No effect on DNA binding. 2 Publications1
Mutagenesisi72D → N: Loss of ability to resolve junctions. No effect on DNA binding. 1 Publication1
Mutagenesisi73N → A: Slight reduction in ability to promote DNA repair. Great reduction in Holliday junction resolution activity. 1 Publication1
Mutagenesisi76K → Q: Loss of ability to promote DNA repair. Loss of Holliday junction resolvase activity. No effect on DNA binding. 1 Publication1
Mutagenesisi76K → R: Loss of ability to promote DNA repair. Less than 2% activity of Holliday junction resolvase. No effect on DNA binding. 1 Publication1
Mutagenesisi80D → N: Slight reduction in ability to resolve junctions. No effect on DNA binding. 1 Publication1
Mutagenesisi87F → Y or V: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi90D → N: Slight reduction in ability to resolve junctions. No effect on DNA binding. 1 Publication1
Mutagenesisi91D → N: Loss of ability to resolve junctions. No effect on DNA binding. 1 Publication1
Mutagenesisi101K → Q: No effect on ability to promote DNA repair. 1 Publication1
Mutagenesisi111E → Q: No effect on resolvase activity or DNA binding. 1 Publication1
Mutagenesisi116E → Q: No effect on resolvase activity or DNA binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001920041 – 120Crossover junction endodeoxyribonuclease RusAAdd BLAST120

Proteomic databases

PaxDbiP0AG74.
PRIDEiP0AG74.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi4261529. 59 interactors.
849560. 4 interactors.
DIPiDIP-16988N.
IntActiP0AG74. 1 interactor.
STRINGi511145.b0550.

Structurei

Secondary structure

1120
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi14 – 17Combined sources4
Beta strandi18 – 23Combined sources6
Beta strandi25 – 27Combined sources3
Helixi29 – 44Combined sources16
Beta strandi55 – 62Combined sources8
Beta strandi64 – 67Combined sources4
Helixi72 – 84Combined sources13
Beta strandi87 – 89Combined sources3
Helixi91 – 93Combined sources3
Beta strandi94 – 102Combined sources9
Beta strandi109 – 116Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q8RX-ray1.90A/B1-120[»]
2H8CX-ray3.10A/B/C/D1-120[»]
2H8EX-ray1.20A1-120[»]
ProteinModelPortaliP0AG74.
SMRiP0AG74.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG74.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 16DNA binding4
Regioni66 – 73DNA binding8

Sequence similaritiesi

Belongs to the RusA family.Curated

Phylogenomic databases

eggNOGiENOG4106CZA. Bacteria.
COG4570. LUCA.
HOGENOMiHOG000119986.
InParanoidiP0AG74.
KOiK01160.
OMAiIHYISDW.

Family and domain databases

Gene3Di3.30.1330.70. 1 hit.
InterProiIPR016281. Endonuclease_RusA.
IPR008822. Endonuclease_RusA-like.
[Graphical view]
PfamiPF05866. RusA. 1 hit.
[Graphical view]
PIRSFiPIRSF001007. RusA. 1 hit.
SUPFAMiSSF103084. SSF103084. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AG74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTYSITLPW PPSNNRYYRH NRGRTHVSAE GQAYRDNVAR IIKNAMLDIG
60 70 80 90 100
LAMPVKIRIE CHMPDRRRRD LDNLQKAAFD ALTKAGFWLD DAQVVDYRVV
110 120
KMPVTKGGRL ELTITEMGNE
Length:120
Mass (Da):13,846
Last modified:December 20, 2005 - v1
Checksum:i38401669E8819EA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92587 Genomic DNA. Translation: CAA63321.1.
U82598 Genomic DNA. Translation: AAB40746.1.
U00096 Genomic DNA. Translation: AAC73651.1.
AP009048 Genomic DNA. Translation: BAE76325.1.
PIRiS66590.
RefSeqiNP_415082.1. NC_000913.3.
WP_001099712.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73651; AAC73651; b0550.
BAE76325; BAE76325; BAE76325.
GeneIDi945174.
KEGGiecj:JW0538.
eco:b0550.
PATRICi32116262. VBIEscCol129921_0571.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92587 Genomic DNA. Translation: CAA63321.1.
U82598 Genomic DNA. Translation: AAB40746.1.
U00096 Genomic DNA. Translation: AAC73651.1.
AP009048 Genomic DNA. Translation: BAE76325.1.
PIRiS66590.
RefSeqiNP_415082.1. NC_000913.3.
WP_001099712.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q8RX-ray1.90A/B1-120[»]
2H8CX-ray3.10A/B/C/D1-120[»]
2H8EX-ray1.20A1-120[»]
ProteinModelPortaliP0AG74.
SMRiP0AG74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261529. 59 interactors.
849560. 4 interactors.
DIPiDIP-16988N.
IntActiP0AG74. 1 interactor.
STRINGi511145.b0550.

Proteomic databases

PaxDbiP0AG74.
PRIDEiP0AG74.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73651; AAC73651; b0550.
BAE76325; BAE76325; BAE76325.
GeneIDi945174.
KEGGiecj:JW0538.
eco:b0550.
PATRICi32116262. VBIEscCol129921_0571.

Organism-specific databases

EchoBASEiEB4170.
EcoGeneiEG20283. rusA.

Phylogenomic databases

eggNOGiENOG4106CZA. Bacteria.
COG4570. LUCA.
HOGENOMiHOG000119986.
InParanoidiP0AG74.
KOiK01160.
OMAiIHYISDW.

Enzyme and pathway databases

BioCyciEcoCyc:G6306-MONOMER.
ECOL316407:JW0538-MONOMER.
BRENDAi3.1.22.4. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AG74.
PROiP0AG74.

Family and domain databases

Gene3Di3.30.1330.70. 1 hit.
InterProiIPR016281. Endonuclease_RusA.
IPR008822. Endonuclease_RusA-like.
[Graphical view]
PfamiPF05866. RusA. 1 hit.
[Graphical view]
PIRSFiPIRSF001007. RusA. 1 hit.
SUPFAMiSSF103084. SSF103084. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRUSA_ECOLI
AccessioniPrimary (citable) accession number: P0AG74
Secondary accession number(s): P40116, Q2MBN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Encoded by the cryptic lambdoid prophage DLP12. Normally not expressed. Complete suppression of ruv mutations by RusA is dependent on the activity of RecG.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.