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UniProtKB - P33919 (RADD_ECOLI)

Entry version 144 (07 Apr 2021)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

Putative DNA repair helicase RadD

Gene

radD

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

RadD contains helicase motifs, suggesting it may be a helicase, although that activity has not been observed (Probable). In combination with RadA is important in repair of double-strand DNA breaks (DSB) (PubMed:25425430, PubMed:25484163). Has DNA-independent ATPase activity that is stimulated by single-stranded DNA-binding protein SSB. ATPase is stimulated by a peptide with the last 10 residues of SSB, but not when the peptide's last Phe residue is missing. Binds ssDNA; binding is slightly better in the presence of nucleotides (PubMed:27519413). May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds to DNA structures with 3 branches that resemble replication forks (PubMed:31665437).3 Publications4 Publications

<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

<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

Zn2+Combined sources1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

ATPase activity in the presence of KCl in the absence of any nucleic acid substrate.1 Publication
  1. KM=0.85 µM for ATP1 Publication
  2. KM=0.63 µM for ATP in the presence of SSB1 Publication
  3. KM=0.40 µM for ATP in the presence of last 10 residues of SSB1 Publication

    pH dependencei

    Optimum pH is >7.5.1 Publication

    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 bindingi384ZincCombined sources1 Publication1
    Metal bindingi387ZincCombined sources1 Publication1
    Metal bindingi411ZincCombined sources1 Publication1
    Metal bindingi425ZincCombined sources1 Publication1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionDNA-binding, Helicase, Hydrolase
    Biological processDNA damage, DNA repair
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG12045-MONOMER
    MetaCyc:EG12045-MONOMER

    <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:
    Putative DNA repair helicase RadD1 Publication (EC:3.6.4.122 Publications)
    <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:radD1 Publication
    Synonyms:yejH, yejI, yejJ
    Ordered Locus Names:b2184, JW2172
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    100- to 10000-fold decrease in survival after IR (PubMed:25049088, PubMed:25425430). Double radA-radD deletions have nearly 106-fold lower survival upon IR, and the double mutant is more severely affected by UV radiation than either of the single mutants alone (up to 100 J/m2). The single mutation is more sensitive to dsDNA breaks induced by CFX, the double radA-radD mutant is inviable upon CFX treatment; the SOS response is slightly induced in the single and more induced in the double mutant. No effect on RecA-mediated conjugational DNA recombination (PubMed:25425430). In another study double radA-radD deletions are sensitive to CFX but not to UV (up to 40 J/m2) or azidothymidine (AZT) (PubMed:25484163). Deletion of radD leads to an increase in DNA crossing over, DNA repeat deletion and DNA repeat expansion; double uup-radD deletion increases the phenotypes. Single radD deletion has no effect on cell growth or filamentation, double uup-radD deletions are filamentous and lack defined nucleoids. Single deletion is more sensitive to CFX (PubMed:31665437).4 Publications

    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>Mutagenesisi37K → R: Partially complements a radD deletion mutant for survival of ionizing radiation (possible loss of ATPase activity), increases sensitivity to UV of a double radA-radD deletion. Has a dominant negative effect on survival of UV in the presence of wild-type enzyme or ciprofloxacin survival. Has no ATPase activity, does not bind ssDNA. 2 Publications1
    Mutagenesisi356 – 586Missing : Does not complement sensitivity of a double radA-radD deletion to dsDNA breaks. 1 PublicationAdd BLAST231
    Mutagenesisi437C → A: Does not complement sensitivity of a double radA-radD deletion to dsDNA breaks. 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_00001691641 – 586Putative DNA repair helicase RadDAdd BLAST586

    Proteomic databases

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

    More...    PaxDbi    		P33919

    PRoteomics IDEntifications database

    More...    PRIDEi    		P33919

    <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

    Monomer (PubMed:31035307, PubMed:27519413).

    Interacts with single-stranded DNA-binding protein SSB (PubMed:27519413).

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4259416, 278 interactors
    849903, 1 interactor

    Protein interaction database and analysis system

    More...    IntActi    		P33919, 5 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b2184

    <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

    1586
    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    		P33919

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 171Helicase ATP-binding1 PublicationPROSITE-ProRule annotationAdd BLAST154
    Domaini241 – 386Helicase C-terminal1 PublicationPROSITE-ProRule annotationAdd BLAST146

    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>Regioni376 – 425Zinc finger domain1 PublicationAdd BLAST50
    Regioni429 – 574C-terminal domain1 PublicationAdd BLAST146

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The C-terminal domain (residues 356-586) is required to alleviate the deleterious effects of UV or ciprofloxacin (CFX) treatment in a double radA-radD mutant; its effect on ionising irradiation (IR) survival in the single radD mutant were not reported (PubMed:25425430). Crystals have 4 domains; helicase ATP-binding (residues 7-185), helicase C-terminal (residues 187-365), a zinc finger domain (residues 376-425) and the C-terminal domain (429-574) (PubMed:31035307).2 Publications

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1061, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_014765_1_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P33919

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P33919

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR006935, Helicase/UvrB_N
    IPR014001, Helicase_ATP-bd
    IPR001650, Helicase_C
    IPR027417, P-loop_NTPase
    IPR011332, Ribosomal_zn-bd

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00271, Helicase_C, 1 hit
    PF04851, ResIII, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00487, DEXDc, 1 hit
    SM00490, HELICc, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52540, SSF52540, 1 hit
    SSF57829, SSF57829, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS51192, HELICASE_ATP_BIND_1, 1 hit
    PS51194, HELICASE_CTER, 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.

    P33919-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIFTLRPYQQ EAVDATLNHF RRHKTPAVIV LPTGAGKSLV IAELARLARG 
            60         70         80         90        100
    RVLVLAHVKE LVAQNHAKYQ ALGLEADIFA AGLKRKESHG KVVFGSVQSV 
           110        120        130        140        150
    ARNLDAFQGE FSLLIVDECH RIGDDEESQY QQILTHLTKV NPHLRLLGLT 
           160        170        180        190        200
    ATPFRLGKGW IYQFHYHGMV RGDEKALFRD CIYELPLRYM IKHGYLTPPE 
           210        220        230        240        250
    RLDMPVVQYD FSRLQAQSNG LFSEADLNRE LKKQQRITPH IISQIMEFAA 
           260        270        280        290        300
    TRKGVMIFAA TVEHAKEIVG LLPAEDAALI TGDTPGAERD VLIENFKAQR 
           310        320        330        340        350
    FRYLVNVAVL TTGFDAPHVD LIAILRPTES VSLYQQIVGR GLRLAPGKTD 
           360        370        380        390        400
    CLILDYAGNP HDLYAPEVGT PKGKSDNVPV QVFCPACGFA NTFWGKTTAD 
           410        420        430        440        450
    GTLIEHFGRR CQGWFEDDDG HREQCDFRFR FKNCPQCNAE NDIAARRCRE 
           460        470        480        490        500
    CDTVLVDPDD MLKAALRLKD ALVLRCSGMS LQHGHDEKGE WLKITYYDED 
           510        520        530        540        550
    GADVSERFRL QTPAQRTAFE QLFIRPHTRT PGIPLRWITA ADILAQQALL 
           560        570        580 
    RHPDFVVARM KGQYWQVREK VFDYEGRFRL AHELRG
    Length:586
    Mass (Da):66,413
    Last modified:November 1, 1997 - v2
    <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:i2D173250F83333DF
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA16381 differs from that shown. Reason: Frameshift.Curated

    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
    		U00096 Genomic DNA Translation: AAC75245.1
    AP009048 Genomic DNA Translation: BAE76649.1
    U00008 Genomic DNA Translation: AAA16381.1 Frameshift.

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		G64987

    NCBI Reference Sequences

    More...    RefSeqi    		NP_416689.1, NC_000913.3
    WP_000578061.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC75245; AAC75245; b2184
    BAE76649; BAE76649; BAE76649

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		945529

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW2172
    eco:b2184

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.52

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <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
    		U00096 Genomic DNA Translation: AAC75245.1
    AP009048 Genomic DNA Translation: BAE76649.1
    U00008 Genomic DNA Translation: AAA16381.1 Frameshift.
    PIRiG64987
    RefSeqiNP_416689.1, NC_000913.3
    WP_000578061.1, 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
    6JDEX-ray2.80A/B1-586[»]
    SMRiP33919
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4259416, 278 interactors
    849903, 1 interactor
    IntActiP33919, 5 interactors
    STRINGi511145.b2184

    Proteomic databases

    PaxDbiP33919
    PRIDEiP33919

    Genome annotation databases

    EnsemblBacteriaiAAC75245; AAC75245; b2184
    BAE76649; BAE76649; BAE76649
    GeneIDi945529
    KEGGiecj:JW2172
    eco:b2184
    PATRICifig|1411691.4.peg.52

    Organism-specific databases

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

    More...    EchoBASEi    		EB1979

    Phylogenomic databases

    eggNOGiCOG1061, Bacteria
    HOGENOMiCLU_014765_1_0_6
    InParanoidiP33919
    PhylomeDBiP33919

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12045-MONOMER
    MetaCyc:EG12045-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P33919

    Family and domain databases

    InterProiView protein in InterPro
    IPR006935, Helicase/UvrB_N
    IPR014001, Helicase_ATP-bd
    IPR001650, Helicase_C
    IPR027417, P-loop_NTPase
    IPR011332, Ribosomal_zn-bd
    PfamiView protein in Pfam
    PF00271, Helicase_C, 1 hit
    PF04851, ResIII, 1 hit
    SMARTiView protein in SMART
    SM00487, DEXDc, 1 hit
    SM00490, HELICc, 1 hit
    SUPFAMiSSF52540, SSF52540, 1 hit
    SSF57829, SSF57829, 1 hit
    PROSITEiView protein in PROSITE
    PS51192, HELICASE_ATP_BIND_1, 1 hit
    PS51194, HELICASE_CTER, 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 nameiRADD_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: P33919
    Secondary accession number(s): P36926
    , P36927, P76449, Q2MAQ7
    <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: February 1, 1994
    Last sequence update: November 1, 1997
    Last modified: April 7, 2021
    This is version 144 of the entry and version 2 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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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