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Entry version 107 (26 Feb 2020)
Sequence version 2 (10 Apr 2019)
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Protein

Polyprotein nsP1234

Gene
N/A
Organism
Ross river virus (strain T48) (RRV)
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>
-Protein inferred from homologyi <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

Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.By similarity
The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarity). As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins (By similarity).By similarity
The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).Curated
Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of FXR family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-FXR complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of FXR family members to self-assemble and bind DNA (Probable).By similarityCurated
Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (By similarity). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (By similarity). Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (By similarity). The nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA (By similarity).By similarity
RNA dependent RNA polymerase (By similarity). Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarity). The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs (By similarity).By similarity

Miscellaneous

Viral replication produces dsRNA in the late phase of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A (By similarity). This inactivates completely cellular translation initiation, resulting shutoff of host proteins synthesis (By similarity). However, phosphorylation of EIF2A is probably not the only mechanism responsible for the host translation shutoff (By similarity). The viral translation can still occur normally because it relies on a hairpin structure in the coding region of sgRNA and is EIF2A-, EIF2D-, EIF4G- EIF4A-independent (By similarity).By similarity
The genome codes for P123, but readthrough of a terminator codon UGA occurs between the codons for Phe-531 and Leu-533 giving rise to P1234 (Probable). P1234 is cleaved quickly by nsP2 into P123' and nsP4 (By similarity). Further processing of p123' gives nsP1, nsP2 and nsP3' which is 6 amino acids longer than nsP3 since the cleavage site is after the readthrough (By similarity). This unusual molecular mechanism ensures that few nsP4 are produced compared to other non-structural proteins (By similarity). Mutant viruses with no alternative termination site grow significantly slower than wild-type virus (By similarity). The opal termination codon is frequently mutated to a sense codon on passage in cell culture (By similarity). The presence of the opal codon may be a requirement for viral maintenance in both vertebrate and invertebrate hosts and a selective advantage may be conferred in cell culture for the sense codon (By similarity).By similarityCurated

<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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei10ADP-riboseBy similarity1
Binding sitei24ADP-riboseBy similarity1
Binding sitei32ADP-riboseBy similarity1
Binding sitei112ADP-riboseBy similarity1
Binding sitei113ADP-riboseBy similarity1
Binding sitei114ADP-riboseBy similarity1
<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 bindingi262ZincBy similarity1
Metal bindingi264ZincBy similarity1
Metal bindingi287ZincBy similarity1
Metal bindingi305ZincBy 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

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 functionHydrolase, Nucleotidyltransferase, RNA-binding, RNA-directed RNA polymerase, Transferase
Biological processViral RNA replication
LigandMetal-binding, Nucleotide-binding, Zinc

<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:
Polyprotein nsP1234
Short name:
P1234
Alternative name(s):
Non-structural polyprotein
Cleaved into the following 5 chains:
Polyprotein P123'
Short name:
P123'
Polyprotein P123
Short name:
P123
Non-structural protein 3' (EC:3.1.3.84Curated)
Short name:
nsP3'
Non-structural protein 3 (EC:3.1.3.84By similarity)
Short name:
nsP3
RNA-directed RNA polymerase nsP4 (EC:2.7.7.19By similarity, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 4
Short name:
nsP4
<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>OrganismiRoss river virus (strain T48) (RRV)
<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 identifieri11032 [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 lineageiVirusesRiboviriaTogaviridaeAlphavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 hostiAedes [TaxID: 7158]
Culex annulirostris (Common banded mosquito) [TaxID: 162997]
Homo sapiens (Human) [TaxID: 9606]
Macropus sp. (kangaroo) [TaxID: 9322]

<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

  • Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated
  • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3' is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
  • Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated
  • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasmic vesicle, Host membrane, Membrane

<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_0000308401‹1 – ›1149Polyprotein nsP1234Add BLAST›1149
ChainiPRO_0000446654‹1 – 538Polyprotein P123'Add BLAST›538
ChainiPRO_0000446655‹1 – 531Polyprotein P123Add BLAST›531
ChainiPRO_00000412221 – 538Non-structural protein 3'Add BLAST538
ChainiPRO_00004466561 – 531Non-structural protein 3Add BLAST531
ChainiPRO_0000041223539 – 1149RNA-directed RNA polymerase nsP4Add BLAST611

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 residuei344Phosphothreonine; by hostBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form the early replication complex (By similarity). At the same time, P1234 is also cut at the nsP1/nsP2 site early in infection but with lower efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and P1234 and allowing the formation of the late replication complex (By similarity). NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than nsP4 (By similarity).By similarity
Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P123 is cleaved at the nsP1/nsP2 site with low efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123 and allowing the formation of the late replication complex (By similarity).By similarity
Phosphorylated by host on serines and threonines.By similarity
Phosphorylated by host on serines and threonines.By similarity
ubiquitinated; targets the protein for rapid degradation via the ubiquitin system (By similarity). Nsp4 is present in extremely low quantities due to low frequency of translation through the amber stop-codon and the degradation by the ubiquitin pathway (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei538 – 539Cleavage; by protease nsP2By similarity2

Keywords - PTMi

Phosphoprotein, Ubl conjugation

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with mRNA-capping enzyme nsP1 (By similarity).

Interacts with host DDX1 (By similarity). RNA-directed

Interacts with host DDX3 (By similarity).

Interacts (via C-terminus) with host G3BP1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).

Interacts (via C-terminus) with host G3BP2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).

By similarity

Interacts with itself.

Interacts with mRNA-capping enzyme nsP1.

Interacts with protease nsP2.

Interacts with itself.

By similarity

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini‹1 – 160MacroPROSITE-ProRule annotationAdd BLAST›160
Domaini903 – 1018RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi512 – 515FGDF; binding to host G3BP1By similarity4
Motifi523 – 526FGDF; binding to host G3BP1By similarity4

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

In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3/G3BP1 complex (By similarity).By similarity
In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3'/G3BP1 complex (By similarity).By similarity

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002589 Macro_dom
IPR007094 RNA-dir_pol_PSvirus
IPR001788 Tymovirus_RNA-dep_RNA_pol

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01661 Macro, 1 hit
PF00978 RdRP_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00506 A1pp, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51154 MACRO, 1 hit
PS50507 RDRP_SSRNA_POS, 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: Fragment.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P13888-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
APSYRVRRTD ISGHAEEAVV NAANAKGTVG DGVCRAVARK WPDSFKGAAT
60 70 80 90 100
PVGTAKLVQA NGMNVIHAVG PNFSTVTEAE GDRELAAAYR AVAGIINASN
110 120 130 140 150
IKSVAIPLLS TGVFSGGKDR VMQSLNHLFT AMDTTDADVV IYCRDKAWEK
160 170 180 190 200
KIQEAIDRRT AVELVSEDIS LESDLIRVHP DSCLVGRKGY SITDGKLHSY
210 220 230 240 250
LEGTRFHQTA VDMAEISTLW PKLQDANEQI CLYALGESMD SIRTKCPVED
260 270 280 290 300
ADSSTPPKTV PCLCRYAMTA ERVARLRMNN TKAIIVCSSF PLPKYRIEGV
310 320 330 340 350
QKVKCDRVLI FDQTVPSLVS PRKYIPAAAS THADTVSLDS TVSTGSAWSF
360 370 380 390 400
PSEATYETME VVAEVHHSEP PVPPPRRRRA QVTMHHQELL EVSDMHTPIA
410 420 430 440 450
ARVEIPVYDT AVVVERVAIP CTSEYAKPIP APRAARVVPV PAPRIQRAST
460 470 480 490 500
YRVSPTPTPR VLRASVCSVT TSAGVEFPWA PEDLEVLTEP VHCKMREPVE
510 520 530 540 550
LPWEPEDVDI QFGDFETSDK IQFGDIDFDQ FXLGRAGAYI FSSDTGPGHL
560 570 580 590 600
QQKSVRQHAL PCEMLYVHEE ERTYPPALDE AREKLLQAKM QMAPTEANKS
610 620 630 640 650
RYQSRKVENM KAVIIDRLKD GARTYLTEQS EKIPTYVSKY PRPVYSPSVE
660 670 680 690 700
DSLQNPEVAV AACNAFLEAN YPTVASYQIT DEYDAYLDMV DGSESCLDRA
710 720 730 740 750
TFCPAKLRCY PKHHAYHQPQ VRSAVPSPFQ NTLQNVLAAA TKRNCNVTQM
760 770 780 790 800
RELPTLDSAV LNVECFKKFA CNGEYWQEFK DNPIRITTEN ITTYVTRLKG
810 820 830 840 850
PKAAALFAKT HNLVPLQEVP MDRFVVDMKR DVKVTPGTKH TEERPKVQVI
860 870 880 890 900
QAAEPLATAY LCGIHRELVR RLKAVLAPNI HTLFDMSAED FDAIIAAHFQ
910 920 930 940 950
PGDAVLETDI ASFDKSQDDS LALTALMLLE DLGVDQELLD LIEAAFGEIT
960 970 980 990 1000
SVHLPTGTRF KFGAMMKSGM FLTLFVNTLL NIVIACRVLR EKLTNSVCAA
1010 1020 1030 1040 1050
FIGDDNIVHG VRSDPLMAER CASWVNMEVK IIDATMCEKP PYFCGGFILY
1060 1070 1080 1090 1100
DKVTGSACRV ADPLKRLFKL GKPLPAGDTQ DEDRRRALKD ETDRWARVGL
1110 1120 1130 1140
KSELEIALSS RYEVNGTGNI VRAMATLAKS LKNFKKLRGP IVHLYGGPK
Length:1,149
Mass (Da):127,267
Last modified:April 10, 2019 - 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:i5AB143F6AA775DCB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11
Non-terminal residuei11491

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
M20539 Genomic RNA Translation: AAA47407.1
K00046 Genomic RNA Translation: AAA47403.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...
PIRi
A28614

<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
M20539 Genomic RNA Translation: AAA47407.1
K00046 Genomic RNA Translation: AAA47403.1 Sequence problems.
PIRiA28614

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

Family and domain databases

InterProiView protein in InterPro
IPR002589 Macro_dom
IPR007094 RNA-dir_pol_PSvirus
IPR001788 Tymovirus_RNA-dep_RNA_pol
PfamiView protein in Pfam
PF01661 Macro, 1 hit
PF00978 RdRP_2, 1 hit
SMARTiView protein in SMART
SM00506 A1pp, 1 hit
PROSITEiView protein in PROSITE
PS51154 MACRO, 1 hit
PS50507 RDRP_SSRNA_POS, 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 nameiPOLN_RRVT
<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: P13888
<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: January 1, 1990
Last sequence update: April 10, 2019
Last modified: February 26, 2020
This is version 107 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
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Main funding by: National Institutes of Health

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