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Entry version 111 (02 Dec 2020)
Sequence version 1 (20 Dec 2005)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction). EC:3.1.22.4

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi70MagnesiumCurated1
Metal bindingi72MagnesiumCurated1
Metal bindingi91MagnesiumCurated1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA recombination, DNA repair
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6306-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.22.4, 2026

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Crossover junction endodeoxyribonuclease RusA (EC:3.1.22.4)
Alternative name(s):
Holliday junction nuclease RusA
Holliday junction resolvase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rusA
Synonyms:rus, ybcP
Ordered Locus Names:b0550, JW0538
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001920041 – 120Crossover junction endodeoxyribonuclease RusAAdd BLAST120

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0AG74

PRoteomics IDEntifications database

More...
PRIDEi
P0AG74

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261529, 59 interactors
849560, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-16988N

Protein interaction database and analysis system

More...
IntActi
P0AG74, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b0550

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1120
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0AG74

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AG74

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni13 – 16DNA binding4
Regioni66 – 73DNA binding8

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RusA family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG4570, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_139466_0_2_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AG74

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1330.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016281, Endonuclease_RusA
IPR008822, Endonuclease_RusA-like
IPR036614, RusA-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05866, RusA, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001007, RusA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF103084, SSF103084, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i38401669E8819EA6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S66590

NCBI Reference Sequences

More...
RefSeqi
NP_415082.1, NC_000913.3
WP_001099712.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73651; AAC73651; b0550
BAE76325; BAE76325; BAE76325

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
49585103
945174

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0538
eco:b0550

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1727

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q8RX-ray1.90A/B1-120[»]
2H8CX-ray3.10A/B/C/D1-120[»]
2H8EX-ray1.20A1-120[»]
SMRiP0AG74
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261529, 59 interactors
849560, 4 interactors
DIPiDIP-16988N
IntActiP0AG74, 1 interactor
STRINGi511145.b0550

Proteomic databases

PaxDbiP0AG74
PRIDEiP0AG74

Genome annotation databases

EnsemblBacteriaiAAC73651; AAC73651; b0550
BAE76325; BAE76325; BAE76325
GeneIDi49585103
945174
KEGGiecj:JW0538
eco:b0550
PATRICifig|1411691.4.peg.1727

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB4170

Phylogenomic databases

eggNOGiCOG4570, Bacteria
HOGENOMiCLU_139466_0_2_6
InParanoidiP0AG74

Enzyme and pathway databases

BioCyciEcoCyc:G6306-MONOMER
BRENDAi3.1.22.4, 2026

Miscellaneous databases

EvolutionaryTraceiP0AG74

Protein Ontology

More...
PROi
PR:P0AG74

Family and domain databases

Gene3Di3.30.1330.70, 1 hit
InterProiView protein in InterPro
IPR016281, Endonuclease_RusA
IPR008822, Endonuclease_RusA-like
IPR036614, RusA-like_sf
PfamiView protein in Pfam
PF05866, RusA, 1 hit
PIRSFiPIRSF001007, RusA, 1 hit
SUPFAMiSSF103084, SSF103084, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRUSA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AG74
Secondary accession number(s): P40116, Q2MBN1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: December 2, 2020
This is version 111 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

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