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Entry version 169 (08 May 2019)
Sequence version 3 (01 Nov 1997)
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Protein

Exoribonuclease 2

Gene

rnb

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

Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction (PubMed:11948193). RNases 2 and R (rnr) contribute to rRNA degradation during starvation, while RNase R and PNPase (pnp) are the major contributors to quality control of rRNA during steady state growth (PubMed:21135037). This RNase is required to decrease expression of RNase PH (rnp) at 42 degrees Celsius during starvation, which in turn represses rRNA degradation (PubMed:28625967).3 Publications

Miscellaneous

In K12 strains that are derived from W1485 (including MG1655 and W3110) the rph gene has a frameshift that leads to loss of its ribonuclease PH activity. In strain K12 / MG1655(Seq)* the wild-type Rph protein has been restored (PubMed:28625967).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. EC:3.1.13.1

<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+1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Stimulated by the presence of a monovalent cation (PubMed:11948193). Acetylation leads to decreased substrate binding and decreased catalytic activity (PubMed:26847092).2 Publications

<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

    1. Vmax=109800 nmol/min/mg enzyme with Poly(A) as substrate1 Publication
    2. Vmax=160 nmol/min/mg enzyme with 23S rRNA as substrate1 Publication
    3. Vmax=30 nmol/min/mg enzyme with 16S rRNA as substrate1 Publication
    4. Vmax=20 nmol/min/mg enzyme with 5S rRNA as substrate1 Publication

    pH dependencei

    Optimum pH is 7.5-9.5.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    <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 functionExonuclease, Hydrolase, Nuclease, RNA-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11620-MONOMER
    ECOL316407:JW1279-MONOMER
    MetaCyc:EG11620-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.13.1 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_and_taxonomy_section">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:
    Exoribonuclease 2 (EC:3.1.13.1)
    Alternative name(s):
    Exoribonuclease II
    Short name:
    RNase II
    Short name:
    Ribonuclease II
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:rnb
    Ordered Locus Names:b1286, JW1279
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG11620 rnb

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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

    In the presence of wild-type RNase PH (rph) 80-90% reduction in viability in stationary phase (96 hours of growth) at 31 and 42 degrees Celsius or when cells are rapidly starved at 42 degrees Celsius; if rph is also absent there is no visible phenotype under these 3 growth conditions (PubMed:28625967). Its absence leads to extensive degradation of rRNA (PubMed:28625967).1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi501K → Q or R: Strong decrease in acetylation. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001663801 – 644Exoribonuclease 2Add BLAST644

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei501N6-acetyllysine; by PatZ1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Acetylated at Lys-501 by PatZ. Deacetylated by CobB.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P30850

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

    More...
    PaxDbi
    P30850

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P30850

    <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_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263341, 45 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10724N

    Protein interaction database and analysis system

    More...
    IntActi
    P30850, 10 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1286

    <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

    1644
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    2ID0X-ray2.35A/B/C/D1-644[»]
    2IX0X-ray2.44A6-644[»]
    2IX1X-ray2.74A6-644[»]

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

    More...
    SMRi
    P30850

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P30850

    <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_and_domains_section">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>Domaini561 – 643S1 motifAdd BLAST83

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108IEC Bacteria
    COG4776 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000271427

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P30850

    KEGG Orthology (KO)

    More...
    KOi
    K01147

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P30850

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01036 RNase_II, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011129 CSD
    IPR040476 CSD2
    IPR012340 NA-bd_OB-fold
    IPR013223 RNase_B_OB_dom
    IPR011804 RNase_II
    IPR001900 RNase_II/R
    IPR022966 RNase_II/R_CS
    IPR004476 RNase_II/RNase_R
    IPR003029 S1_domain

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF17876 CSD2, 1 hit
    PF08206 OB_RNB, 1 hit
    PF00773 RNB, 1 hit
    PF00575 S1, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00357 CSP, 1 hit
    SM00955 RNB, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50249 SSF50249, 4 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00358 3_prime_RNase, 1 hit
    TIGR02062 RNase_B, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01175 RIBONUCLEASE_II, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P30850-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ
    60 70 80 90 100
    MKKVMHGDRI IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV
    110 120 130 140 150
    PDHPLLKDAI PCRAARGLNH EFKEGDWAVA EMRRHPLKGD RSFYAELTQY
    160 170 180 190 200
    ITFGDDHFVP WWVTLARHNL EKEAPDGVAT EMLDEGLVRE DLTALDFVTI
    210 220 230 240 250
    DSASTEDMDD ALFAKALPDD KLQLIVAIAD PTAWIAEGSK LDKAAKIRAF
    260 270 280 290 300
    TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTLSA DGTIEDNIEF
    310 320 330 340 350
    FAATIESKAK LVYDQVSDWL ENTGDWQPES EAIAEQVRLL AQICQRRGEW
    360 370 380 390 400
    RHNHALVFKD RPDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA
    410 420 430 440 450
    ARVLRDKLGF GIYNVHMGFD PANADALAAL LKTHGLHVDA EEVLTLDGFC
    460 470 480 490 500
    KLRRELDAQP TGFLDSRIRR FQSFAEISTE PGPHFGLGLE AYATWTSPIR
    510 520 530 540 550
    KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM AERDVGDWLY
    560 570 580 590 600
    ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAVRDE
    610 620 630 640
    LVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPVA
    Length:644
    Mass (Da):72,491
    Last modified:November 1, 1997 - v3
    <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:i36B16712CDF14394
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti384I → N in CAA48112 (PubMed:8497196).Curated1
    Sequence conflicti399C → G in CAA48112 (PubMed:8497196).Curated1
    Sequence conflicti513A → R in CAA48112 (PubMed:8497196).Curated1

    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
    X67913 Genomic DNA Translation: CAA48112.1
    U00096 Genomic DNA Translation: AAC74368.1
    AP009048 Genomic DNA Translation: BAA14840.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A64877

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415802.1, NC_000913.3
    WP_000484984.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74368; AAC74368; b1286
    BAA14840; BAA14840; BAA14840

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945864

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1279
    eco:b1286

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.993

    <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
    X67913 Genomic DNA Translation: CAA48112.1
    U00096 Genomic DNA Translation: AAC74368.1
    AP009048 Genomic DNA Translation: BAA14840.1
    PIRiA64877
    RefSeqiNP_415802.1, NC_000913.3
    WP_000484984.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2ID0X-ray2.35A/B/C/D1-644[»]
    2IX0X-ray2.44A6-644[»]
    2IX1X-ray2.74A6-644[»]
    SMRiP30850
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263341, 45 interactors
    DIPiDIP-10724N
    IntActiP30850, 10 interactors
    STRINGi511145.b1286

    Proteomic databases

    jPOSTiP30850
    PaxDbiP30850
    PRIDEiP30850

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74368; AAC74368; b1286
    BAA14840; BAA14840; BAA14840
    GeneIDi945864
    KEGGiecj:JW1279
    eco:b1286
    PATRICifig|1411691.4.peg.993

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1577
    EcoGeneiEG11620 rnb

    Phylogenomic databases

    eggNOGiENOG4108IEC Bacteria
    COG4776 LUCA
    HOGENOMiHOG000271427
    InParanoidiP30850
    KOiK01147
    PhylomeDBiP30850

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11620-MONOMER
    ECOL316407:JW1279-MONOMER
    MetaCyc:EG11620-MONOMER
    BRENDAi3.1.13.1 2026

    Miscellaneous databases

    EvolutionaryTraceiP30850

    Protein Ontology

    More...
    PROi
    PR:P30850

    Family and domain databases

    HAMAPiMF_01036 RNase_II, 1 hit
    InterProiView protein in InterPro
    IPR011129 CSD
    IPR040476 CSD2
    IPR012340 NA-bd_OB-fold
    IPR013223 RNase_B_OB_dom
    IPR011804 RNase_II
    IPR001900 RNase_II/R
    IPR022966 RNase_II/R_CS
    IPR004476 RNase_II/RNase_R
    IPR003029 S1_domain
    PfamiView protein in Pfam
    PF17876 CSD2, 1 hit
    PF08206 OB_RNB, 1 hit
    PF00773 RNB, 1 hit
    PF00575 S1, 1 hit
    SMARTiView protein in SMART
    SM00357 CSP, 1 hit
    SM00955 RNB, 1 hit
    SUPFAMiSSF50249 SSF50249, 4 hits
    TIGRFAMsiTIGR00358 3_prime_RNase, 1 hit
    TIGR02062 RNase_B, 1 hit
    PROSITEiView protein in PROSITE
    PS01175 RIBONUCLEASE_II, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiRNB_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: P30850
    Secondary accession number(s): P78280
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 1, 1997
    Last modified: May 8, 2019
    This is version 169 of the entry and version 3 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, 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
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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