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UniProtKB - P21530 (POLG_CSFVB)

Entry version 155 (02 Dec 2020)
Sequence version 1 (01 May 1991)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Classical swine fever virus (strain Brescia) (CSFV) (Hog cholera virus)
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

Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.By similarity
Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Plays also a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.By similarity
Plays a role in viral entry. Interacts with host RPSA that acts as a cellular attachment receptor for the virus. Possesses also intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferon and assist in the development of persistent infections.By similarity
Plays a role in cell attachment and subsequent fusion of viral and cellular membranes. Therefore, mediates together with envelope glycoprotein E2 the viral entry.By similarity
Plays a role in cell attachment and subsequent fusion of viral and cellular membranes. Therefore, mediates together with envelope glycoprotein E1 the viral entry.By similarity
Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules.By similarity
Autoprotease that associates with the host chaperone JIV and cleaves the NS2-3 protein between NS2 and NS3. Plays also a role in the formation of infectious particles.By similarity
Plays a role in the regulation of viral RNA replication.By similarity
Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Plays a role in the inhibition of host NF-kappa-B activation by interacting with and inhibiting host TRAF6. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.By similarity
Acts as a cofactor for the NS3 protease activity.By similarity
Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). Antagonizes host cell apoptosis by interacting with host ferritin heavy chain. The ORF4 protein physically binds host FTH1/FHC, resulting in the reduction of FTH1 protein levels in host cells. Reduction of FTH1 concentration further inhibits the accumulation of reactive oxygen in host cells, leading to reduced apoptosis.By similarity
Replicates the viral (+) and (-) genome.PROSITE-ProRule annotation

<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

  • Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites. EC:3.4.21.113

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei49For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei69For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei1447For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1461For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1512For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1658Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1695Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1752Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1

<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 ...

GO - Biological processi

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 functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel
Biological processActivation of host autophagy by virus, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host RLR pathway by virus, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

Protein family/group databases

MEROPS protease database

More...MEROPSi		S31.001

<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:
Genome polyprotein
Cleaved into the following 13 chains:
N-terminal protease (EC:3.4.22.-)
Short name:
N-pro
Alternative name(s):
Autoprotease p20
Capsid protein C
E(rns) glycoprotein
Alternative name(s):
gp44/48
Envelope glycoprotein E1
Alternative name(s):
gp33
Envelope glycoprotein E2
Alternative name(s):
gp55
Viroporin p7By similarity
Non-structural protein 2-3
Short name:
NS2-3
Cysteine protease NS2 (EC:3.4.22.-)
Alternative name(s):
Non-structural protein 2
Serine protease NS3 (EC:3.4.21.113, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Non-structural protein 3
Non-structural protein 4A
Short name:
NS4A
Non-structural protein 4B
Short name:
NS4B
Non-structural protein 5A
Short name:
NS5A
RNA-directed RNA polymerase (EC:2.7.7.48)
Alternative name(s):
NS5B
<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>OrganismiClassical swine fever virus (strain Brescia) (CSFV) (Hog cholera virus)
<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 identifieri11098 [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 lineageiViruses › Riboviria › Orthornavirae › Kitrinoviricota › Flasuviricetes › Amarillovirales › Flaviviridae › Pestivirus ›
<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 hostiSus scrofa (Pig) [TaxID: 9823]
<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
  • UP000008569 <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: Genome

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1140 – 1164HelicalPROSITE-ProRule annotationAdd BLAST25
Transmembranei1189 – 1209HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1217 – 1237HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1247 – 1267HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1281 – 1301HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1360 – 1380HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1568 – 1588HelicalPROSITE-ProRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane, Virion

<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_00004508941 – 3898Genome polyproteinAdd BLAST3898
ChainiPRO_00000380621 – 168N-terminal proteaseBy similarityAdd BLAST168
ChainiPRO_0000038063169 – 267Capsid protein CBy similarityAdd BLAST99
ChainiPRO_0000038064268 – 494E(rns) glycoproteinBy similarityAdd BLAST227
ChainiPRO_0000038065495 – 656Envelope glycoprotein E1By similarityAdd BLAST162
ChainiPRO_0000038066657 – 1062Envelope glycoprotein E2By similarityAdd BLAST406
ChainiPRO_00000380671063 – 1132Viroporin p7By similarityAdd BLAST70
ChainiPRO_00000380681133 – 2272Non-structural protein 2-3By similarityAdd BLAST1140
ChainiPRO_00003493621133 – 1589Cysteine protease NS2PROSITE-ProRule annotationAdd BLAST457
ChainiPRO_00000380691590 – 2272Serine protease NS3By similarityAdd BLAST683
ChainiPRO_00000380702273 – 2336Non-structural protein 4ABy similarityAdd BLAST64
ChainiPRO_00000380712337 – 2683Non-structural protein 4BBy similarityAdd BLAST347
ChainiPRO_00000380722684 – 3180Non-structural protein 5ABy similarityAdd BLAST497
ChainiPRO_00000380733181 – 3898RNA-directed RNA polymeraseBy similarityAdd BLAST718

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi157N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi269N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi278N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi332N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi362N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi410N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi425N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi500N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi594N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi805N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi810N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi874N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi918N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi949N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi1713N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2134N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2217N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2419N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2494N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2787N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2815N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi2891N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi3103N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi3211N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi3316N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi3689N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi3698N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi3794N-linked (GlcNAc...) asparagine; by hostSequence analysis1

<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

Heavily glycosylated.By similarity
The viral RNA of pestiviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing resulting in the production of at least eleven individual proteins. The N-terminal protease cleaves itself from the nascent polyprotein autocatalytically and thereby generates the N-terminus of the adjacent viral capsid protein C.By similarity
Cleavage between E2 and p7 is partial.

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>Sitei168 – 169Cleavage; by autolysisPROSITE-ProRule annotation2
Sitei267 – 268Cleavage; by host signal peptidaseBy similarity2
Sitei494 – 495CleavageBy similarity2
Sitei656 – 657Cleavage; by host signal peptidaseBy similarity2
Sitei1062 – 1063Cleavage; by host signal peptidase; partialBy similarity2
Sitei1132 – 1133Cleavage; by host signal peptidaseBy similarity2
Sitei1589 – 1590Cleavage; partial; by cysteine protease NS2By similarity2
Sitei2272 – 2273Cleavage; by serine protease NS3By similarity2
Sitei2336 – 2337Cleavage; by serine protease NS3By similarity2
Sitei2683 – 2684Cleavage; by serine protease NS3By similarity2
Sitei3180 – 3181Cleavage; by serine protease NS3By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P21530

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Translated cap independently from an internal ribosome entry site (IRES).1 Publication

<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 host IRF3.

By similarity

Interacts with host OS9.

By similarity

Homodimer; disulfide-linked.

Interacts with host RPSA.

By similarity

Homodimer; disulfide-linked (By similarity). Heterodimer with E1; disulfide-linked (By similarity).

By similarity

Homodimer; disulfide-linked (By similarity). Heterodimer with E1; disulfide-linked (By similarity).

Interacts with host TRX2 (By similarity).

By similarity

Interacts with host TRAF6; this interaction inhibits host NF-kappa-B pathway.

Interacts with NS5B; this interaction enhances RNA-dependent RNA polymerase activity.

Interacts with protein NS4A.

By similarity

Interacts with host RAB5, this interaction facilitates the formation of NS4B-related complex.

Interacts with host FTH1; this interaction plays a positive role in viral anti-apoptosis.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P21530, 61 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

3D structure databases

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

More...SMRi		P21530

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

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>Domaini1 – 168Peptidase C53PROSITE-ProRule annotationAdd BLAST168
Domaini1441 – 1589Peptidase C74PROSITE-ProRule annotationAdd BLAST149
Domaini1590 – 1763Peptidase S31PROSITE-ProRule annotationAdd BLAST174
Domaini1802 – 1960Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST159
Domaini1978 – 2179Helicase C-terminalPROSITE-ProRule annotationAdd BLAST202
Domaini3519 – 3642RdRp catalyticPROSITE-ProRule annotationAdd BLAST124

<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 pestivirus polyprotein family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.140.40, 1 hit
2.60.320.20, 1 hit
2.60.40.3000, 1 hit
3.30.1360.280, 1 hit
3.30.70.270, 2 hits
3.90.730.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR021824, Capsid-C_pestivirus
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR022120, NS2
IPR030399, NS2_C74
IPR027417, P-loop_NTPase
IPR008751, Peptidase_C53
IPR042542, Peptidase_C53_interaction
IPR032521, Pestivirus_E2
IPR042309, Pestivirus_E2_A
IPR042310, Pestivirus_E2_B
IPR042311, Pestivirus_E2_D
IPR000280, Pestivirus_NS3_S31
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR007094, RNA-dir_pol_PSvirus
IPR002166, RNA_pol_HCV
IPR036430, RNase_T2-like_sf
IPR033130, RNase_T2_His_AS_2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11889, DUF3409, 1 hit
PF07652, Flavi_DEAD, 1 hit
PF00271, Helicase_C, 1 hit
PF05550, Peptidase_C53, 1 hit
PF12387, Peptidase_C74, 1 hit
PF05578, Peptidase_S31, 1 hit
PF16329, Pestivirus_E2, 1 hit
PF00998, RdRP_3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00729, CDVENDOPTASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit
SSF55895, SSF55895, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51692, PESTIVIRUS_NS2_PRO, 1 hit
PS51535, PESTIVIRUS_NS3PRO, 1 hit
PS51876, PV_NPRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS00531, RNASE_T2_2, 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.

<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.

P21530-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELNHFELLY KTNKQKPMGV EEPVYDVTGR PLFGDPSEVH PQSTLKLPHD 
        60         70         80         90        100
RGRGNIKTTL KNLPRRGDCR SGNHLGPVSG IYVKPGPVFY QDYMGPVYHR 
       110        120        130        140        150
APLEFFDEAQ FCEVTKRIGR VTGSDGKLYH IYVCIDGCIL LKLAKRGEPR 
       160        170        180        190        200
TLKWIRNLTD CPLWVTSCSD DGASASKEKK PDRINKGKLK IAPKEHEKDS 
       210        220        230        240        250
RTKPPDATIV VEGVKYQVKK KGKVKGKNTQ DGLYHNKNKP PESRKKLEKA 
       260        270        280        290        300
LLAWAVIAIM LYQPVAAENI TQWNLRDNGT NGIQHAMYLR GVSRSLHGIW 
       310        320        330        340        350
PEKICKGVPT YLATDTELRE IQGMMVASEG TNYTCCKLQR HEWNKHGWCN 
       360        370        380        390        400
WYNIDPWIQL MNRTQANLAE GPPSKECAVT CRYDKNADIN VVTQARNRPT 
       410        420        430        440        450
TLTGCKKGTN FSFAGTVIEG PCNFNVSVED ILYGDHECGS LLQDTALYLV 
       460        470        480        490        500
DGMTNTIERA RQGAARVTSW LGRQLRIAGK RLEGRSKTWF GAYALSPYCN 
       510        520        530        540        550
VTTKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI LHEMGGHLSE 
       560        570        580        590        600
FLLLSLVVLS DFAPETASAL YLILHYVIPQ SHEEPEGCDT NQLNLTVELR 
       610        620        630        640        650
TEDVIPSSVW NVGKYVCVRP DWWPYETKVA LLFEEAGQVV KLALRALRDL 
       660        670        680        690        700
TRVWNSASTT AFLICLIKVL RGQVVQGVIW LLLVTGAQGR LACKEDHRYA 
       710        720        730        740        750
ISTTNEIGLH GAEGLTTTWK EYNHNLQLDD GTVKAICMAG SFKVTALNVV 
       760        770        780        790        800
SRRYLASLHK DALPTSVTFE LLFDGTSPLT EEMGDDFGFG LCPYDTSPVV 
       810        820        830        840        850
KGKYNTTLLN GSAFYLVCPI GWTGVIECTA VSPTTLRTEV VKTFRREKPF 
       860        870        880        890        900
PYRRDCVTTT VENEDLFYCK WGGNWTCVKG EPVTYTGGPV KQCRWCGFDF 
       910        920        930        940        950
NEPDGLPHYP IGKCILANET GYRIVDSTDC NRDGVVISTE GSHECLIGNT 
       960        970        980        990       1000
TVKVHALDER LGPMPCRPKE IVSSAGPVRK TSCTFNYAKT LRNRYYEPRD 
      1010       1020       1030       1040       1050
SYFQQYMLKG EYQYWFDLDV TDRHSDYFAE FIVLVVVALL GGRYVLWLIV 
      1060       1070       1080       1090       1100
TYIVLTEQLA AGLQLGQGEV VLIGNLITHT DIEVVVYFLL LYLVMRDEPI 
      1110       1120       1130       1140       1150
KKWILLLFHA MTNNPVKTIT VALLMVSGVA KGGKIDGGWQ RLPETNFDIQ 
      1160       1170       1180       1190       1200
LALTVIVVAV MLLAKKDPTT VPLVITVATL RTAKITNGLS TDLAIATVST 
      1210       1220       1230       1240       1250
ALLTWTYISD YYKYKTLLQY LISTVTGIFL IRVLKGVGEL DLHTPTLPSY 
      1260       1270       1280       1290       1300
RPLFFILVYL ISTAVVTRWN LDIAGLLLQC VPTLLMVFTM WADILTLILI 
      1310       1320       1330       1340       1350
LPTYELTKLY YLKEVKIGAE RGWLWKTNFK RVNDIYEVDQ AGEGVYLFPS 
      1360       1370       1380       1390       1400
KQKTGTITGT MLPLIKAILI SCISNKWQFI YLLYLIFEVS YYLHKKIIDE 
      1410       1420       1430       1440       1450
IAGGTNFISR LVAALIEANW AFDNEEVRGL KKFFLLSSRV KELIIKHKVR 
      1460       1470       1480       1490       1500
NEVMVHWFGD EEVYGMPKLV GLVKAATLSK NKHCILCTVC ENREWRGETC 
      1510       1520       1530       1540       1550
PKCGRFGPPV TCGMTLADFE EKHYKRIFFR EDQSEGPVRE EYAGYLQYRA 
      1560       1570       1580       1590       1600
RGQLFLRNLP VLATKVKMLL VGNLGTEVGD LEHLGWVLRG PAVCKKVTEH 
      1610       1620       1630       1640       1650
EKCTTSIMDK LTAFFGVMPR GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ 
      1660       1670       1680       1690       1700
GGISSVDHVT CGKDLLVCDT MGRTRVVCQS NNKMTDESEY GVKTDSGCPE 
      1710       1720       1730       1740       1750
GARCYVFNRE AVNISGTKGA MVHLQKTGGE FTCVTASGTP AFFDLKNLKG 
      1760       1770       1780       1790       1800
WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK STTDLTEMVK 
      1810       1820       1830       1840       1850
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE 
      1860       1870       1880       1890       1900
SVYQYMRQKH PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMPQPKLRAA 
      1910       1920       1930       1940       1950
MVEYSFIFLD EYHCSTPEQL AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG 
      1960       1970       1980       1990       2000
QKHPIEEYIA PEVMKGEDLG PEYLDIAGLK IPVEEMKSNM LVFVPTRNMA 
      2010       2020       2030       2040       2050
VETAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT NAIESGVTLP 
      2060       2070       2080       2090       2100
DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK 
      2110       2120       2130       2140       2150
PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE 
      2160       2170       2180       2190       2200
EDSLMITQLE ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP 
      2210       2220       2230       2240       2250
VLFPKIKNGE VTDSYDNYTF LNARKLGDDV PPYVYATEDE DLAVELLGLD 
      2260       2270       2280       2290       2300
WPDPGNQGTV EAGRALKQVV GLSTAENALL VALFGYVGYQ ALSKRHIPVV 
      2310       2320       2330       2340       2350
TDIYSIEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD VQRCMEAMTN 
      2360       2370       2380       2390       2400
YARDGIQFMK SQALKVKETP TYKETMDTVA DYVKKFMEAL ADSKEDIIKY 
      2410       2420       2430       2440       2450
GLWGTHTALY KSIGARLGNE TAFATLVVKW LAFGGESIAD HVKQAATDLV 
      2460       2470       2480       2490       2500
VYYIINRPQF PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE 
      2510       2520       2530       2540       2550
PALATLPYAA TALKLFAPTR LESVVILSTA IYKTYLSIRR GKSDGLLGTG 
      2560       2570       2580       2590       2600
VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN AIEASEQKRT LLMKVFVKNF 
      2610       2620       2630       2640       2650
LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHVYG VFYKGWEAKE 
      2660       2670       2680       2690       2700
LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDSIK 
      2710       2720       2730       2740       2750
SSVRQMAISW APAPFSCDWT PTDDRIGLPQ DNFLRVETKC PCGYKMKAVK 
      2760       2770       2780       2790       2800
NCAGELRLLE EEGSFLCRNK FGRGSRNYRV TKYYDDNLSE IKPVIRMEGH 
      2810       2820       2830       2840       2850
VELYYKGATI KLDFNNSKTI LATDKWEVDH STLVRVLKRH TGAGYCGAYL 
      2860       2870       2880       2890       2900
GEKPNHKHLI ERDCATITKD KVCFLKMKRG CAFTYDLSLH NLTRLIELVH 
      2910       2920       2930       2940       2950
KNNLEDKEIP AVTVTTWLAY TFVNEDIGTI KPAFGEKITP EMQEEITLQP 
      2960       2970       2980       2990       3000
AVLVDATDVT VTVVGETPTM TTGETPTTFT SSGPDPKGQQ VLKLGVGEGQ 
      3010       3020       3030       3040       3050
YPGTNPQRAS LHEAIQSADE RPSVLILGSD KATSNRVKTV KNVKVYRGRD 
      3060       3070       3080       3090       3100
PLEVRDMMRR GKILVIALSR VDNALLKFVD YKGTFLTRET LEALSLGRPK 
      3110       3120       3130       3140       3150
KKNITKAEAQ WLLRLEDQME ELPDWFAAGE PIFLEANIKH DRYHLVGDIA 
      3160       3170       3180       3190       3200
TIKEKAKQLG ATDSTKISKE VGAKVYSMKL SNWVMQEENK QSNLTPLFEE 
      3210       3220       3230       3240       3250
LLQQCPPGGQ NKTAHMVSAY QLAQGNWMPT SCHVFMGTIS ARRTKTHPYE 
      3260       3270       3280       3290       3300
AYVKLRELVE EHKMKTLCPG SSLRNDNEWV IGKIKYQGNL RTKHMLNPGK 
      3310       3320       3330       3340       3350
VAEQLHREGH RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR 
      3360       3370       3380       3390       3400
DKIDKEENLQ TPGLHKKLME VFNALKRPEL ESSYDAVEWE ELERGINRKG 
      3410       3420       3430       3440       3450
AAGFFERKNI GEILDSEKIK VEEIIDNLKK GRNIKYYETA IPKNEKRDVN 
      3460       3470       3480       3490       3500
DDWTAGDFVD EKKPRVIQYP EAKTRLAITK VMYKWVKQKP VVIPGYEGKT 
      3510       3520       3530       3540       3550
PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTNDLEL IKDIQKYYFK 
      3560       3570       3580       3590       3600
KKWHKFIDTL TMHMSEVPVI TADGEVYIRK GQRGSGQPDT SAGNSMLNVL 
      3610       3620       3630       3640       3650
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL 
      3660       3670       3680       3690       3700
YEAGKPQKIT EGDKMKVAYQ FADIEFCSHT PIQVRWSDNT SSYMPGRNTT 
      3710       3720       3730       3740       3750
TILAKMATRL DSSGERGTIA YEKAVAFSFL LMYSWNPLIR RICLLVLSTE 
      3760       3770       3780       3790       3800
LQVKPGKSTT YYYEGDPISA YKEVIGHNLF DLKRTSFEKL AKLNLSMSVL 
      3810       3820       3830       3840       3850
GAWTRHTSKR LLQDCVNMGV KEGNWLVNAD RLVSSKTGNR YVPGEGHTLQ 
      3860       3870       3880       3890 
GRHYEELALA RKQINSFQGT DRYNLGPIVN MVLRRLRVMM MTLIGRGV
Length:3,898
Mass (Da):438,430
Last modified:May 1, 1991 - 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:iEC6EB207A09D59FD
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
M31768 Genomic RNA Translation: AAA43843.1

Protein sequence database of the Protein Information Resource

More...PIRi		A35317, GNWVHB

<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
M31768 Genomic RNA Translation: AAA43843.1
PIRiA35317, GNWVHB

3D structure databases

SMRiP21530
ModBaseiSearch...

Protein-protein interaction databases

IntActiP21530, 61 interactors

Protein family/group databases

MEROPSiS31.001

Proteomic databases

PRIDEiP21530

Family and domain databases

Gene3Di2.30.140.40, 1 hit
2.60.320.20, 1 hit
2.60.40.3000, 1 hit
3.30.1360.280, 1 hit
3.30.70.270, 2 hits
3.90.730.10, 1 hit
InterProiView protein in InterPro
IPR021824, Capsid-C_pestivirus
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR022120, NS2
IPR030399, NS2_C74
IPR027417, P-loop_NTPase
IPR008751, Peptidase_C53
IPR042542, Peptidase_C53_interaction
IPR032521, Pestivirus_E2
IPR042309, Pestivirus_E2_A
IPR042310, Pestivirus_E2_B
IPR042311, Pestivirus_E2_D
IPR000280, Pestivirus_NS3_S31
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR007094, RNA-dir_pol_PSvirus
IPR002166, RNA_pol_HCV
IPR036430, RNase_T2-like_sf
IPR033130, RNase_T2_His_AS_2
PfamiView protein in Pfam
PF11889, DUF3409, 1 hit
PF07652, Flavi_DEAD, 1 hit
PF00271, Helicase_C, 1 hit
PF05550, Peptidase_C53, 1 hit
PF12387, Peptidase_C74, 1 hit
PF05578, Peptidase_S31, 1 hit
PF16329, Pestivirus_E2, 1 hit
PF00998, RdRP_3, 1 hit
PRINTSiPR00729, CDVENDOPTASE
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF55895, SSF55895, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51692, PESTIVIRUS_NS2_PRO, 1 hit
PS51535, PESTIVIRUS_NS3PRO, 1 hit
PS51876, PV_NPRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS00531, RNASE_T2_2, 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 nameiPOLG_CSFVB
<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: P21530
<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: May 1, 1991
Last sequence update: May 1, 1991
Last modified: December 2, 2020
This is version 155 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 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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