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UniProtKB - Q9RUV0 (PPDE_DEIRA)

Entry version 110 (02 Dec 2020)
Sequence version 1 (01 May 2000)
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Protein

Phosphatase/phosphodiesterase DR_1281

Gene

DR_1281

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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

Has a dual activity phosphatase/phosphodiesterase in vitro, with a preference to phosphoenolpyruvate (PEP) and 2',3'-cAMP, respectively. Can also use 2',3'-cGMP, 2',3'-cCMP and various model substrates such as p-nitrophenyl phosphate (pNPP), bis-p-nitrophenyl phosphate (bis-pNPP) and p-nitrophenyl thymidine monophosphate (pNP-TMP).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 Publication, Co2+1 Publication, Fe2+1 PublicationNote: Mn2+ is the preferable metal for phosphatase activity. Phosphodiesterase activity is observed in the presence of Co2+, Mn2+ or Fe2+.1 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 0.18 sec(-1) with PEP as substrate. kcat is 0.38 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.32 sec(-1) with 2',3'-cCMP as substrate. kcat is 0.42 sec(-1) with 2',3'-cGMP as substrate. kcat is 0.20 sec(-1) with pNPP as substrate. kcat is 6.97 sec(-1) with bis-pNPP as substrate. kcat is 1.41 sec(-1) with pNP-TMP as substrate.1 Publication
  1. KM=0.36 mM for PEP (at pH 6.5)1 Publication
  2. KM=0.55 mM for 2',3'-cAMP (at pH 6.5)1 Publication
  3. KM=0.87 mM for 2',3'-cCMP (at pH 6.5)1 Publication
  4. KM=1.28 mM for 2',3'-cGMP (at pH 6.5)1 Publication
  5. KM=0.08 mM for pNPP (at pH 8.5)1 Publication
  6. KM=0.22 mM for bis-pNPP (at pH 8.5)1 Publication
  7. KM=0.05 mM for pNP-TMP (at pH 8.5)1 Publication
  1. Vmax=0.38 µmol/min/mg enzyme with PEP as substrate (at pH 6.5)1 Publication
  2. Vmax=0.83 µmol/min/mg enzyme with 2',3'-cAMP as substrate (at pH 6.5)1 Publication
  3. Vmax=0.68 µmol/min/mg enzyme with 2',3'-cCMP as substrate (at pH 6.5)1 Publication
  4. Vmax=0.91 µmol/min/mg enzyme with 2',3'-cGMP as substrate (at pH 6.5)1 Publication
  5. Vmax=0.44 µmol/min/mg enzyme with pNPP as substrate (at pH 8.5)1 Publication
  6. Vmax=13.8 µmol/min/mg enzyme with bis-pNPP as substrate (at pH 8.5)1 Publication
  7. Vmax=2.79 µmol/min/mg enzyme with pNP-TMP as substrate (at pH 8.5)1 Publication

pH dependencei

Optimum pH is 6.0-7.0.1 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 bindingi8Divalent metal cation 1By similarity1
Metal bindingi37Divalent metal cation 1By similarity1
Metal bindingi37Divalent metal cation 2By similarity1
Metal bindingi38Divalent metal cation 1By similarity1
Metal bindingi65Divalent metal cation 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei66Proton donorBy similarity1
Metal bindingi148Divalent metal cation 2; via tele nitrogenBy similarity1
Metal bindingi173Divalent metal cation 2; via pros nitrogenBy similarity1
Metal bindingi175Divalent metal cation 1; 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 functionHydrolase
LigandCobalt, Iron, Manganese, Metal-binding

<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:
Phosphatase/phosphodiesterase DR_1281Curated
Alternative name(s):
2',3'-cyclic-nucleotide 2'-phosphodiesteraseCurated (EC:3.1.4.161 Publication)
Calcineurin-like phosphoesterase1 Publication
Phosphoenolpyruvate phosphataseCurated (EC:3.1.3.601 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
Ordered Locus Names:DR_1281Imported
<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>OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
<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 identifieri243230 [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 › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›
<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
  • UP000002524 <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 I

<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_00004396401 – 255Phosphatase/phosphodiesterase DR_1281Add BLAST255

<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

STRING: functional protein association networks

More...STRINGi		243230.DR_1281

<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

1255
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		Q9RUV0

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		Q9RUV0

<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 YmdB-like family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1692, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_068238_0_0_0

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9RUV0

Identification of Orthologs from Complete Genome Data

More...OMAi		NHIWDKK

Database of Orthologous Groups

More...OrthoDBi		1127353at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029052, Metallo-depent_PP-like
IPR005235, YmdB-like

The PANTHER Classification System

More...PANTHERi		PTHR36303, PTHR36303, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13277, YmdB, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF004789, DR1281, 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.

Q9RUV0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVLFIGDVF GQPGRRVLQN HLPTIRPQFD FVIVNMENSA GGFGMHRDAA 
        60         70         80         90        100
RGALEAGAGC LTLGNHAWHH KDIYPMLSED TYPIVRPLNY ADPGTPGVGW 
       110        120        130        140        150
RTFDVNGEKL TVVNLLGRVF MEAVDNPFRT MDALLERDDL GTVFVDFHAE 
       160        170        180        190        200
ATSEKEAMGW HLAGRVAAVI GTHTHVPTAD TRILKGGTAY QTDAGFTGPH 
       210        220        230        240        250
DSIIGSAIEG PLQRFLTERP HRYGVAEGRA ELNGVALHFE GGKATAAERY 

RFIED
Length:255
Mass (Da):27,936
Last modified:May 1, 2000 - 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:i82F9DB08AD169D46
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
AE000513 Genomic DNA Translation: AAF10852.1

Protein sequence database of the Protein Information Resource

More...PIRi		D75415

NCBI Reference Sequences

More...RefSeqi		NP_295005.1, NC_001263.1
WP_010887924.1, NZ_CP015081.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAF10852; AAF10852; DR_1281

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dra:DR_1281

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|243230.17.peg.1477

<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
AE000513 Genomic DNA Translation: AAF10852.1
PIRiD75415
RefSeqiNP_295005.1, NC_001263.1
WP_010887924.1, NZ_CP015081.1

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
1T70X-ray2.30A/B/C/D/E/F/G/H1-255[»]
SMRiQ9RUV0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_1281

Genome annotation databases

EnsemblBacteriaiAAF10852; AAF10852; DR_1281
KEGGidra:DR_1281
PATRICifig|243230.17.peg.1477

Phylogenomic databases

eggNOGiCOG1692, Bacteria
HOGENOMiCLU_068238_0_0_0
InParanoidiQ9RUV0
OMAiNHIWDKK
OrthoDBi1127353at2

Miscellaneous databases

EvolutionaryTraceiQ9RUV0

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR029052, Metallo-depent_PP-like
IPR005235, YmdB-like
PANTHERiPTHR36303, PTHR36303, 1 hit
PfamiView protein in Pfam
PF13277, YmdB, 1 hit
PIRSFiPIRSF004789, DR1281, 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 nameiPPDE_DEIRA
<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: Q9RUV0
<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: April 12, 2017
Last sequence update: May 1, 2000
Last modified: December 2, 2020
This is version 110 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, 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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