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Entry version 128 (02 Jun 2021)
Sequence version 1 (25 Jul 2006)
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Protein

Genome polyprotein

Gene
N/A
Organism
Seneca Valley virus (isolate -/United States/SSV-001/2002) (SVV)
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

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:18940610).

Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 325 Angstroms (Probable). VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3 (By similarity).

All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity).

VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:18940610).

By similarity1 Publication1 Publication

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:18940610).

Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 270 Angstroms (Probable). VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3 (By similarity).

All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity).

VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:18940610).

By similarity1 Publication1 Publication

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (Probable). Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 270 Angstroms (PubMed:18420805).

VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity).

VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity).

By similarity1 Publication

Lies on the inner surface of the capsid shell (PubMed:18940610).

After binding to the host receptor, the capsid undergoes conformational changes (By similarity).

Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity).

After genome has been released, the channel shrinks (By similarity).

By similarity1 Publication

VP0 precursor is a component of immature procapsids.

By similarity

Mediates self-processing of the polyprotein by a translational effect termed 'ribosome skipping'. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B.

By similarity

Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.

By similarity

Associates with and induces structural rearrangements of intracellular membranes.

By similarity

Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.

By similarity

Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity).

Inactivates crucial host adapter molecules in order to suppress antiviral type-I interferon (type-I IFN) and NF-kappaB production to escape host antiviral innate immune responses (PubMed:30408499, PubMed:29427864, PubMed:28566380).

Deubiquitinase that acts on both lysine-48- and lysine-63-linked polyubiquitin chains and inhibits the ubiquitination of the ATP-dependent RNA helicase DDX58/RIG-I, TANK-binding kinase 1 (TBK1), and TNF receptor-associated factor 3 (TRAF3), thereby blocking the expression of IFN-beta and IFN stimulated gene 54 (ISG54) (PubMed:30408499).

Induces host IRF3 and IRF7 degradation thereby suppressing IRF3- and IRF7-induced type-I IFN production (PubMed:29427864).

Also decreases host IRF3 phosphorylation leading to negligible IRF3 activation (PubMed:29427864).

Cleaves host MAVS, TRIF and TANK, which are then unable to regulate pattern recognition receptor (PRR)-mediated type-I IFN production (PubMed:28566380).

By similarity3 Publications

Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity).

Performs VPg uridylylation (By similarity).

By similarity

<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

  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.PROSITE-ProRule annotation EC:3.4.22.28
  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).1 Publication EC:3.4.19.12

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 sitei1556For protease 3C activity and deubiquitinase activityPROSITE-ProRule annotation1 Publication1
Active sitei1592For protease 3C activityPROSITE-ProRule annotation1
Active sitei1668For protease 3C activity and deubiquitinase activityPROSITE-ProRule annotation1 Publication1
Active sitei1956For RdRp activityBy similarity1
Active sitei2054For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1197 – 1204ATPPROSITE-ProRule annotation8

<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 functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processHost-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host IRF7 by virus, Inhibition of host MAVS by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Inhibition of host TBK1 by virus, Inhibition of host TLR pathway by virus, Inhibition of host TRAFs by virus, Ion transport, Transport, Ubl conjugation pathway, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Rho
Virion protein 4
Alternative name(s):
Beta
P1B
Virion protein 2
Alternative name(s):
Gamma
P1C
Virion protein 3
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.4.13)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Viral protein genome-linked
Protease 3CPROSITE-ProRule annotation (EC:3.4.19.121 Publication, EC:3.4.22.28PROSITE-ProRule annotation)
Short name:
P3CPROSITE-ProRule annotation
Alternative name(s):
Picornain 3CPROSITE-ProRule annotation
p22
RNA-directed RNA polymerasePROSITE-ProRule annotation (EC:2.7.7.48PROSITE-ProRule annotation)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
<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>OrganismiSeneca Valley virus (isolate -/United States/SSV-001/2002) (SVV)Imported
<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 identifieri686944 [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 lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeSenecavirus
<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
  • UP000000672 <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

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, Virion

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1556H → A: Complete loss of protease 3C deubiquitinating activity and ability to block IFN-beta induction. 1 Publication1
Mutagenesisi1668C → A: Complete loss of protease 3C deubiquitinating activity and ability to block IFN-beta induction. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004469231 – 2181Genome polyproteinAdd BLAST2181
ChainiPRO_00004469241 – 79Leader proteinAdd BLAST79
ChainiPRO_000044692580 – 434Capsid protein VP0Add BLAST355
ChainiPRO_000044692680 – 150Capsid protein VP4Add BLAST71
ChainiPRO_0000446927151 – 434Capsid protein VP2Add BLAST284
ChainiPRO_0000446928435 – ?673Capsid protein VP3Add BLAST239
ChainiPRO_0000446929?674 – 937Capsid protein VP1Add BLAST264
ChainiPRO_0000446930938 – 946Protein 2A9
ChainiPRO_0000446931947 – 1074Protein 2BAdd BLAST128
ChainiPRO_00004469321075 – 1396Protein 2CAdd BLAST322
ChainiPRO_00004469331397 – ?1486Protein 3AAdd BLAST90
ChainiPRO_0000446934?1487 – 1508VPgAdd BLAST22
ChainiPRO_00004469351509 – 1719Protease 3CAdd BLAST211
ChainiPRO_00004469361720 – 2181RNA-directed RNA polymeraseAdd BLAST462

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(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi80N-myristoyl glycine; by hostBy similarity1
<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 residuei1489O-(5'-phospho-RNA)-tyrosineBy 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

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (Probable). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond (By similarity). This process would release the P1-2A peptide from the translational complex (By similarity).By similarity1 Publication
During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle.By similarity
Myristoylation is required during RNA encapsidation and formation of the mature virus particle.By similarity
Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase.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>Sitei79 – 80Cleavage; by protease 3C1 Publication2
Sitei150 – 151Cleavage1 Publication2
Sitei434 – 435Cleavage; by protease 3C1 Publication2
Sitei937 – 938Cleavage; by protease 3C1 Publication2
Sitei946 – 947Cleavage; by ribosomal skipBy similarity2
Sitei1074 – 1075Cleavage; by protease 3C1 Publication2
Sitei1396 – 1397Cleavage; by protease 3C1 Publication2
Sitei1508 – 1509Cleavage; by protease 3C1 Publication2
Sitei1719 – 1720Cleavage; by protease 3C1 Publication2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

<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; this interaction is involved in the suppression of IRF3 and IRF7 expression and phosphorylation by the virus (PubMed:29427864).

Interacts with host IRF7; this interaction is involved in the suppression of IRF3 and IRF7 expression and phosphorylation by the virus (PubMed:29427864).

Interacts with host MAVS; this interaction allows the cleavage of MAVS and subsequent suppression of host immunity (PubMed:28566380).

Interacts with host TRIF; this interaction allows the cleavage of TRIF and subsequent suppression of host immunity (PubMed:28566380).

Interacts with host TANK; this interaction allows the cleavage of TANK and subsequent suppression of host immunity (PubMed:28566380).

Interacts with host DDX58 (PubMed:30408499).

Interacts with host TBK1 (PubMed:30408499).

Interacts with host TRAF3 (PubMed:30408499).

3 Publications

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-46244N

<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

12181
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
Q155Z9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q155Z9

<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>Domaini1165 – 1333SF3 helicasePROSITE-ProRule annotationAdd BLAST169
Domaini1511 – 1704Peptidase C3PROSITE-ProRule annotationAdd BLAST194
Domaini1950 – 2068RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1472 – 1500DisorderedSequence analysisAdd BLAST29

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00205, rhv_like, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.10.10, 1 hit
2.60.120.20, 3 hits
3.30.70.270, 2 hits
4.10.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037080, Capsid_VP4_sf_Picornavirus
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR044067, PCV_3C_PRO
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00548, Peptidase_C3, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 2 hits
PF00910, RNA_helicase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00918, CALICVIRUSNS

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_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.

Q155Z9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQNSHFSFDT ASGTFEDVTG TKVKIVEYPR SVNNGVYDSS THLEILNLQG
60 70 80 90 100
EIEILRSFNE YQIRAAKQQL GLDIVYELQG NVQTTSKNDF DSRGNNGNMT
110 120 130 140 150
FNYYANTYQN SVDFSTSSSA SGAGPGNSRG GLAGLLTNFS GILNPLGYLK
160 170 180 190 200
DHNTEEMENS ADRVTTQTAG NTAINTQSSL GVLCAYVEDP TKSDPPSSST
210 220 230 240 250
DQPTTTFTAI DRWYTGRLNS WTKAVKTFSF QAVPLPGAFL SRQGGLNGGA
260 270 280 290 300
FTATLHRHFL MKCGWQVQVQ CNLTQFHQGA LLVAMVPETT LDVKPDGKAK
310 320 330 340 350
SLQELNEEQW VEMSDDYRTG KNMPFQSLGT YYRPPNWTWG PNFINPYQVT
360 370 380 390 400
VFPHQILNAR TSTSVDINVP YIGETPTQSS ETQNSWTLLV MVLVPLDYKE
410 420 430 440 450
GATTDPEITF SVRPTSPYFN GLRNRYTAGT DEEQGPIPTA PRENSLMFLS
460 470 480 490 500
TLPDDTVPAY GNVRTPPVNY LPGEITDLLQ LARIPTLMAF ERVPEPVPAS
510 520 530 540 550
DTYVPYVAVP TQFDDRPLIS FPITLSDPVY QNTLVGAISS NFANYRGCIQ
560 570 580 590 600
ITLTFCGPMM ARGKFLLSYS PPNGTQPQTL SEAMQCTYSI WDIGLNSSWT
610 620 630 640 650
FVVPYISPSD YRETRAITNS VYSADGWFSL HKLTKITLPP DCPQSPCILF
660 670 680 690 700
FASAGEDYTL RLPVDCNPSY VFHSTDNAET GVIEAGNTDT DFSGELAAPG
710 720 730 740 750
SNHTNVKFLF DRSRLLNVIK VLEKDAVFPR PFPTQEGAQQ DDGYFCLLTP
760 770 780 790 800
RPTVASRPAT RFGLYANPSG SGVLANTSLD FNFYSLACFT YFRSDLEVTV
810 820 830 840 850
VSLEPDLEFA VGWFPSGSEY QASSFVYDQL HVPFHFTGRT PRAFASKGGK
860 870 880 890 900
VSFVLPWNSV SSVLPVRWGG ASKLSSATRG LPAHADWGTI YAFVPRPNEK
910 920 930 940 950
KSTAVKHVAV YIRYKNARAW CPSMLPFRSY KQKMLMQSGD IETNPGPASD
960 970 980 990 1000
NPILEFLEAE NDLVTLASLW KMVHSVQQTW RKYVKNDDFW PNLLSELVGE
1010 1020 1030 1040 1050
GSVALAATLS NQASVKALLG LHFLSRGLNY TDFYSLLIEK CSSFFTVEPP
1060 1070 1080 1090 1100
PPPAENLMTK PSVKSKFRKL FKMQGPMDKV KDWNQIAAGL KNFQFVRDLV
1110 1120 1130 1140 1150
KEVVDWLQAW INKEKASPVL QYQLEMKKLG PVALAHDAFM AGSGPPLSDD
1160 1170 1180 1190 1200
QIEYLQNLKS LALTLGKTNL AQSLTTMINA KQSSAQRVEP VVVVLRGKPG
1210 1220 1230 1240 1250
CGKSLASTLI AQAVSKRLYG SQSVYSLPPD PDFFDGYKGQ FVTLMDDLGQ
1260 1270 1280 1290 1300
NPDGQDFSTF CQMVSTAQFL PNMADLAEKG RPFTSNLIIA TTNLPHFSPV
1310 1320 1330 1340 1350
TIADPSAVSR RINYDLTLEV SEAYKKHTRL NFDLAFRRTD APPIYPFAAH
1360 1370 1380 1390 1400
VPFVDVAVRF KNGHQNFNLL ELVDSICTDI RAKQQGARNM QTLVLQSPNE
1410 1420 1430 1440 1450
NDDTPVDEAL GRVLSPAAVD EALVDLTPEA DPVGRLAILA KLGLALAAVT
1460 1470 1480 1490 1500
PGLIILAVGL YRYFSGSDAD QEETESEGSV KAPRSENAYD GPKKNSKPPG
1510 1520 1530 1540 1550
ALSLMEMQQP NVDMGFEAAV AKKVVVPITF MVPNRPSGLT QSALLVTGRT
1560 1570 1580 1590 1600
FLINEHTWSN PSWTSFTIRG EVHTRDEPFQ TVHFTHHGIP TDLMMVRLGP
1610 1620 1630 1640 1650
GNSFPNNLDK FGLDQMPARN SRVVGVSSSY GNFFFSGNFL GFVDSITSEQ
1660 1670 1680 1690 1700
GTYARLFRYR VTTYKGWCGS ALVCEAGGVR RIIGLHSAGA AGIGAGTYIS
1710 1720 1730 1740 1750
KLGLIKALKH LGEPLATMQG LMTELEPGIT VHVPRKSKLR KTTAHAVYKP
1760 1770 1780 1790 1800
EFEPAVLSKF DPRLNKDVDL DEVIWSKHTA NVPYQPPLFY TYMSEYAHRV
1810 1820 1830 1840 1850
FSFLGKDNDI LTVKEAILGI PGLDPMDPHT APGLPYAING LRRTDLVDFV
1860 1870 1880 1890 1900
NGTVDAALAV QIQKFLDGDY SDHVFQTFLK DEIRPSEKVR AGKTRIVDVP
1910 1920 1930 1940 1950
SLAHCIVGRM LLGRFAAKFQ SHPGFLLGSA IGSDPDVFWT VIGAQLEGRK
1960 1970 1980 1990 2000
NTYDVDYSAF DSSHGTGSFE ALISHFFTVD NGFSPALGPY LRSLAVSVHA
2010 2020 2030 2040 2050
YGERRIKITG GLPSGCAATS LLNTVLNNVI IRTALALTYK EFEYDMVDII
2060 2070 2080 2090 2100
AYGDDLLVGT DYDLDFNEVA RRAAKLGYKM TPANKGSVFP PTSSLSDAVF
2110 2120 2130 2140 2150
LKRKFVQNND GLYKPVMDLK NLEAMLSYFK PGTLLEKLQS VSMLAQHSGK
2160 2170 2180
EEYDRLMHPF ADYGAVPSHE YLQARWRALF D
Length:2,181
Mass (Da):240,620
Last modified:July 25, 2006 - 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:iFA8BF3068931AB9A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
DQ641257 Genomic RNA Translation: ABG23522.1

NCBI Reference Sequences

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RefSeqi
YP_002268402.1, NC_011349.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6966369

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:6966369

<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
DQ641257 Genomic RNA Translation: ABG23522.1
RefSeqiYP_002268402.1, NC_011349.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CJIX-ray2.30A674-936[»]
B435-673[»]
C151-434[»]
D80-150[»]
6ADLelectron microscopy3.08B182-427[»]
6L0TX-ray1.90A/B1509-1719[»]
SMRiQ155Z9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-46244N

Genome annotation databases

GeneIDi6966369
KEGGivg:6966369

Miscellaneous databases

EvolutionaryTraceiQ155Z9

Family and domain databases

CDDicd00205, rhv_like, 2 hits
Gene3Di2.40.10.10, 1 hit
2.60.120.20, 3 hits
3.30.70.270, 2 hits
4.10.90.10, 1 hit
InterProiView protein in InterPro
IPR037080, Capsid_VP4_sf_Picornavirus
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR044067, PCV_3C_PRO
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat
PfamiView protein in Pfam
PF00548, Peptidase_C3, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 2 hits
PF00910, RNA_helicase, 1 hit
PRINTSiPR00918, CALICVIRUSNS
SUPFAMiSSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

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_SVV1
<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: Q155Z9
<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 8, 2019
Last sequence update: July 25, 2006
Last modified: June 2, 2021
This is version 128 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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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