Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P77766 (RNAAM_ECOLI)

Entry version 127 (02 Dec 2020)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
Add a publicationFeedback
Protein

5'-3' exoribonuclease

Gene

yciV

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

Efficiently catalyzes the hydrolysis of the 3'-phosphate from 3',5'-bis-phosphonucleotides as well as the successive hydrolysis of 5'-phosphomononucleotides from the 5'-end of short pieces of RNA and DNA, with no specificity toward the identity of the nucleotide base. Is more efficient at hydrolyzing RNA oligonucleotides than DNA oligonucleotides. This enzyme can also hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency approximately 10-fold lower than that of the corresponding single-stranded oligonucleotides.1 Publication

Miscellaneous

Since E.coli possesses another enzyme, CysQ, which has been demonstrated to catalyze the hydrolysis of 3',5'-pAp to 5'-AMP and phosphate during sulfur assimilation, it seems therefore unlikely that the hydrolysis of 3',5'-bis-phosphonucleotides will be the primary physiological function of YciV.1 Publication

<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

Mn2+1 PublicationNote: Binds 1 Mn2+ ion per subunit (PubMed:25871919). However, the sequence similarity to CV_1693 from C.violaceum tends to indicate a trinuclear metal center.Curated1 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

kcat is 9.9 sec(-1) with pAp as substrate. kcat is 5.6 sec(-1) with 2'-deoxy-pAp as substrate. kcat is 6.0 sec(-1) with pCp (2'5'/3'5' mixture) as substrate. kcat is 1.9 sec(-1) with 2'-deoxy-pCp as substrate. kcat is 5.5 sec(-1) with pGp (2'5'/3'5' mixture) as substrate. kcat is 1.7 sec(-1) with 2'-deoxy-pGp as substrate. kcat is 4.7 sec(-1) with pUp as substrate. kcat is 2.1 sec(-1) with 2'-deoxy-pUp as substrate. kcat is 1.6 sec(-1) with 2'-deoxy-pTp as substrate. kcat is 3.3 sec(-1) with 2'-deoxy-pIp as substrate. kcat is 0.22 sec(-1) with 3'-AMP as substrate. kcat is 0.60 sec(-1) with p(Gp)G as substrate. kcat is 14 sec(-1) with p(Ap)A as substrate. kcat is 3.8 sec(-1) with p(Ap)2A as substrate. kcat is 3.6 sec(-1) with p(Ap)3A as substrate. kcat is 2.7 sec(-1) with p(Ap)4A as substrate. kcat is 2.5 sec(-1) with p(dAp)dA as substrate. kcat is 0.72 sec(-1) with p(dAp)2dA as substrate. kcat is 1.20 sec(-1) with p(dAp)3dA as substrate. kcat is 0.79 sec(-1) with p(dAp)4dA as substrate.1 Publication
  1. KM=56 µM for pAp1 Publication
  2. KM=53 µM for 2'-deoxy-pAp1 Publication
  3. KM=86 µM for pCp (2'5'/3'5' mixture)1 Publication
  4. KM=114 µM for 2'-deoxy-pCp1 Publication
  5. KM=45 µM for pGp (2'5'/3'5' mixture)1 Publication
  6. KM=30 µM for 2'-deoxy-pGp1 Publication
  7. KM=59 µM for pUp (2'5'/3'5' mixture)1 Publication
  8. KM=110 µM for 2'-deoxy-pUp1 Publication
  9. KM=32 µM for 2'-deoxy-pTp1 Publication
  10. KM=48 µM for 2'-deoxy-pIp1 Publication
  11. KM=420 µM for 3'-AMP1 Publication
  12. KM=14.0 µM for p(Gp)G1 Publication
  13. KM=160 µM for p(Ap)A1 Publication
  14. KM=55 µM for p(Ap)2A1 Publication
  15. KM=45 µM for p(Ap)3A1 Publication
  16. KM=59 µM for p(Ap)4A1 Publication
  17. KM=149 µM for p(dAp)dA1 Publication
  18. KM=67 µM for p(dAp)2dA1 Publication
  19. KM=180 µM for p(dAp)3dA1 Publication
  20. KM=280 µM for p(dAp)4dA1 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 bindingi13Manganese 1; via tele nitrogenBy similarity1
    Metal bindingi15Manganese 1; via tele nitrogenBy similarity1
    Metal bindingi20Manganese 2By similarity1
    Metal bindingi45Manganese 2; via tele nitrogenBy similarity1
    Metal bindingi72Manganese 1By similarity1
    Metal bindingi72Manganese 3By similarity1
    Metal bindingi83Manganese 3; via pros nitrogenBy similarity1
    Metal bindingi198Manganese 3; via tele nitrogenBy similarity1
    Metal bindingi255Manganese 1By similarity1
    Metal bindingi257Manganese 2; via tele nitrogenBy similarity1

    <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 ...

    <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
    LigandManganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:G6634-MONOMER
    MetaCyc:G6634-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:
    5'-3' exoribonuclease1 Publication (EC:3.1.13.-1 Publication)
    Alternative name(s):
    3',5'-nucleotide bisphosphate phosphatase1 Publication (EC:3.1.3.971 Publication)
    RNase AM1 Publication
    <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:yciV
    Synonyms:trpHBy similarity
    Ordered Locus Names:b1266Imported, JW1258Imported
    <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 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_00000656381 – 2935'-3' exoribonucleaseAdd BLAST293

    Proteomic databases

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

    More...    PaxDbi    		P77766

    PRoteomics IDEntifications database

    More...    PRIDEi    		P77766

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260125, 43 interactors
    850224, 1 interactor

    Protein interaction database and analysis system

    More...    IntActi    		P77766, 9 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1266

    <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

    3D structure databases

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

    More...    SMRi    		P77766

    Database of comparative protein structure models

    More...    ModBasei    		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

    <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 PHP family. TrpH/YciV subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0613, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_067347_0_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P77766

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P77766

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR004013, PHP_dom
    IPR003141, Pol/His_phosphatase_N
    IPR016195, Pol/histidinol_Pase-like

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02811, PHP, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00481, POLIIIAc, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF89550, SSF89550, 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.

    P77766-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSDTNYAVIY DLHSHTTASD GCLTPEALVH RAVEMRVGTL AITDHDTTAA 
            60         70         80         90        100
    IAPAREEISR SGLALNLIPG VEISTVWENH EIHIVGLNID ITHPLMCEFL 
           110        120        130        140        150
    AQQTERRNQR AQLIAERLEK AQIPGALEGA QRLAQGGAVT RGHFARFLVE 
           160        170        180        190        200
    CGKASSMADV FKKYLARGKT GYVPPQWCTI EQAIDVIHHS GGKAVLAHPG 
           210        220        230        240        250
    RYNLSAKWLK RLVAHFAEHH GDAMEVAQCQ QSPNERTQLA ALARQHHLWA 
           260        270        280        290 
    SQGSDFHQPC PWIELGRKLW LPAGVEGVWQ LWEQPQNTTE REL
    Length:293
    Mass (Da):32,580
    Last modified:February 1, 1997 - 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:i0A045925C472A15F
    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
    		U00096 Genomic DNA Translation: AAC74348.1
    AP009048 Genomic DNA Translation: BAA14800.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		E64874

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415782.1, NC_000913.3
    WP_001285661.1, NZ_STEB01000005.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74348; AAC74348; b1266
    BAA14800; BAA14800; BAA14800

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		945857

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW1258
    eco:b1266

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|511145.12.peg.1315

    <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: AAC74348.1
    AP009048 Genomic DNA Translation: BAA14800.1
    PIRiE64874
    RefSeqiNP_415782.1, NC_000913.3
    WP_001285661.1, NZ_STEB01000005.1

    3D structure databases

    SMRiP77766
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi4260125, 43 interactors
    850224, 1 interactor
    IntActiP77766, 9 interactors
    STRINGi511145.b1266

    Proteomic databases

    PaxDbiP77766
    PRIDEiP77766

    Genome annotation databases

    EnsemblBacteriaiAAC74348; AAC74348; b1266
    BAA14800; BAA14800; BAA14800
    GeneIDi945857
    KEGGiecj:JW1258
    eco:b1266
    PATRICifig|511145.12.peg.1315

    Organism-specific databases

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

    More...    EchoBASEi    		EB4005

    Phylogenomic databases

    eggNOGiCOG0613, Bacteria
    HOGENOMiCLU_067347_0_0_6
    InParanoidiP77766
    PhylomeDBiP77766

    Enzyme and pathway databases

    BioCyciEcoCyc:G6634-MONOMER
    MetaCyc:G6634-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P77766

    Family and domain databases

    InterProiView protein in InterPro
    IPR004013, PHP_dom
    IPR003141, Pol/His_phosphatase_N
    IPR016195, Pol/histidinol_Pase-like
    PfamiView protein in Pfam
    PF02811, PHP, 1 hit
    SMARTiView protein in SMART
    SM00481, POLIIIAc, 1 hit
    SUPFAMiSSF89550, SSF89550, 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 nameiRNAAM_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: P77766
    <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: July 15, 1998
    Last sequence update: February 1, 1997
    Last modified: December 2, 2020
    This is version 127 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

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again