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Entry version 80 (18 Sep 2019)
Sequence version 2 (15 Feb 2017)
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Protein

RNA-directed RNA polymerase subunit beta

Gene
N/A
Organism
Escherichia phage Qbeta (Bacteriophage Q-beta)
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

This is the catalytic subunit of the viral RNA-dependent RNA polymerase complex. This complex is involved in viral RNA replication that produces (+)-stranded genomes via a complementary, (-)-stranded intermediate. Binds RNA cooperatively with the host ribosomal protein S1.9 Publications

Miscellaneous

In order to produce high amounts of RNA polymerase catalytic core, a fusion protein consisting of tsf-tufB-replicase with a cleavable linker between tufB and the viral replicase subunit is frequently used.5 Publications

<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

<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+3 PublicationsNote: Binds 2 Mg2+ per subunit, Ca2+ is used in crystallization to prevent RNA polymerase activity.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi274Magnesium 13 Publications1
Metal bindingi274Magnesium 23 Publications1
Metal bindingi359Magnesium 13 Publications1
Metal bindingi359Magnesium 23 Publications1
Metal bindingi360Magnesium 13 Publications1
Metal bindingi360Magnesium 23 Publications1

<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 functionNucleotidyltransferase, RNA-binding, RNA-directed RNA polymerase, Transferase
Biological processViral RNA replication
LigandMagnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.48 727

<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:
RNA-directed RNA polymerase subunit beta (EC:2.7.7.481 Publication)
Alternative name(s):
RNA replicase beta chain
RNA-directed RNA polymerase subunit II1 Publication
<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 phage Qbeta (Bacteriophage Q-beta)
<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 identifieri39803 [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 lineageiVirusesRiboviriaLeviviridaeAllolevivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiEscherichia coli [TaxID: 562]
<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
  • UP000305125 <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: Genome
  • UP000306921 Componenti: Genome
  • UP000185268 Componenti: Genome

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_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>Mutagenesisi78K → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi132R → M: Complete loss of infectivity; when associated with M-133. 1 Publication1
Mutagenesisi133R → M: Complete loss of infectivity; when associated with M-132. 1 Publication1
Mutagenesisi134K → A: Complete loss of infectivity. 1 Publication1
Mutagenesisi137K → M: Complete loss of infectivity. 1 Publication1
Mutagenesisi153R → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi164R → A: 80% loss of RNA polymerase activity. 1 Publication1
Mutagenesisi168H → A: 80% loss of RNA polymerase activity. 1 Publication1
Mutagenesisi214K → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi220R → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi241R → A: Decreased initiation of RNA polymerase activity. 1 Publication1
Mutagenesisi274D → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi279S → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi329F → A: Decreased initiation of RNA polymerase activity. 1 Publication1
Mutagenesisi345E → A: Almost complete loss of infectivity. 1 Publication1
Mutagenesisi348D → A: 80% loss of infectivity. 1 Publication1
Mutagenesisi350D → A: 95% loss of infectivity. 1 Publication1
Mutagenesisi357Y → A: Decreased initiation of RNA polymerase activity. 2 Publications1
Mutagenesisi359D → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi360D → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi395E → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi411Y → A: 60% loss of RNA polymerase activity. 1 Publication1
Mutagenesisi413R → A: Loss of RNA polymerase activity. 1 Publication1
Mutagenesisi511Y → A: 50% loss of RNA polymerase activity. 1 Publication1
Mutagenesisi549N → A: 25% loss of RNA polymerase activity. 1 Publication1
Mutagenesisi549N → G: 50% loss of RNA polymerase activity. 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_00001648551 – 589RNA-directed RNA polymerase subunit betaAdd BLAST589

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P14647

<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">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; the replicase complex can dimerize. Part of the viral RNA-dependent RNA polymerase complex, the other subunits are the host ribosomal protein S1, EF-Tu and EF-Ts. S1 is needed for the initiation of genomic RNA (+)-strand replication.

9 Publications

<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

Database of interacting proteins

More...
DIPi
DIP-59375N

Protein interaction database and analysis system

More...
IntActi
P14647, 2 interactors

<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

1589
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
P14647

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_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>Domaini259 – 391RdRp catalyticPROSITE-ProRule annotationAdd BLAST133

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007096 RNA-dir_Rpol_phage_catalytic
IPR005093 RNArep_beta

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03431 RNA_replicase_B, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50522 RDRP_PHAGE, 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>. 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_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.

P14647-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKTASSRNS LSAQLRRAAN TRIEVEGNLA LSIANDLLLA YGQSPFNSEA
60 70 80 90 100
ECISFSPRFD GTPDDFRINY LKAEIMSKYD DFSLGIDTEA VAWEKFLAAE
110 120 130 140 150
AECALTNARL YRPDYSEDFN FSLGESCIHM ARRKIAKLIG DVPSVEGMLR
160 170 180 190 200
HCRFSGGATT TNNRSYGHPS FKFALPQACT PRALKYVLAL RASTHFDIRI
210 220 230 240 250
SDISPFNKAV TVPKNSKTDR CIAIEPGWNM FFQLGIGGIL RDRLRCWGID
260 270 280 290 300
LNDQTINQRR AHEGSVTNNL ATVDLSAASD SISLALCELL LPPGWFEVLM
310 320 330 340 350
DLRSPKGRLP DGSVVTYEKI SSMGNGYTFE LESLIFASLA RSVCEILDLD
360 370 380 390 400
SSEVTVYGDD IILPSCAVPA LREVFKYVGF TTNTKKTFSE GPFRESCGKH
410 420 430 440 450
YYSGVDVTPF YIRHRIVSPA DLILVLNNLY RWATIDGVWD PRAHSVYLKY
460 470 480 490 500
RKLLPKQLQR NTIPDGYGDG ALVGSVLINP FAKNRGWIRY VPVITDHTRD
510 520 530 540 550
RERAELGSYL YDLFSRCLSE SNDGLPLRGP SGCDSADLFA IDQLICRSNP
560 570 580
TKISRSTGKF DIQYIACSSR VLAPYGVFQG TKVASLHEA
Length:589
Mass (Da):65,531
Last modified:February 15, 2017 - 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:i8C02DB50F7202DEF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti71L → F in strain:QB_1. 1 Publication1
Natural varianti130M → I in strain: QB_ancestral, QB_1, QB_2, Qbeta_1_FR and Qbeta_2_FR. 2 Publications1
Natural varianti198I → T2 Publications1
Natural varianti251L → R in strain:QB_1 and Qbeta_2_FR. 2 Publications1
Natural varianti418S → G in strain:QB_1 and Qbeta_2_FR. 1 Publication1
Natural varianti500D → G in strain:QB_2 and Qbeta_2_FR. 2 Publications1

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
X14764 mRNA Translation: CAA32872.1
AY099114 Genomic RNA Translation: AAM33128.1
GQ153928 Genomic RNA Translation: ACY07225.1
GQ153929 Genomic RNA Translation: ACY07229.1
AB971354 Genomic RNA Translation: BAP18765.1
JF719735 Genomic RNA Translation: AEQ25543.1
JF719736 Genomic RNA Translation: AEQ25547.1
GQ153931 Genomic RNA Translation: ACY07237.1
M24876 Genomic RNA Translation: AAA50307.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S03340 RRBPBQ

<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
X14764 mRNA Translation: CAA32872.1
AY099114 Genomic RNA Translation: AAM33128.1
GQ153928 Genomic RNA Translation: ACY07225.1
GQ153929 Genomic RNA Translation: ACY07229.1
AB971354 Genomic RNA Translation: BAP18765.1
JF719735 Genomic RNA Translation: AEQ25543.1
JF719736 Genomic RNA Translation: AEQ25547.1
GQ153931 Genomic RNA Translation: ACY07237.1
M24876 Genomic RNA Translation: AAA50307.1
PIRiS03340 RRBPBQ

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
3AGPX-ray2.80A1-589[»]
3AGQX-ray3.22A1-589[»]
3AVTX-ray2.61A1-589[»]
3AVUX-ray2.91A1-589[»]
3AVVX-ray3.12A1-589[»]
3AVWX-ray2.60A1-589[»]
3AVXX-ray2.41A1-589[»]
3AVYX-ray2.62A1-589[»]
3MMPX-ray2.50F/G1-589[»]
3VNUX-ray3.20A1-589[»]
3VNVX-ray2.60A1-589[»]
4FWTX-ray3.20A1-589[»]
4Q7JX-ray2.90C/G2-589[»]
4R71X-ray3.21B/D1-589[»]
SMRiP14647
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59375N
IntActiP14647, 2 interactors

Proteomic databases

PRIDEiP14647

Enzyme and pathway databases

BRENDAi2.7.7.48 727

Family and domain databases

InterProiView protein in InterPro
IPR007096 RNA-dir_Rpol_phage_catalytic
IPR005093 RNArep_beta
PfamiView protein in Pfam
PF03431 RNA_replicase_B, 1 hit
PROSITEiView protein in PROSITE
PS50522 RDRP_PHAGE, 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 nameiRDRP_BPQBE
<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: P14647
Secondary accession number(s): D0U1F4
, D0U1F8, D0U1G6, G4WZR0, G4WZR4, Q8LTE0
<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: April 1, 1990
Last sequence update: February 15, 2017
Last modified: September 18, 2019
This is version 80 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 programViral 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
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