Q155Z9 · POLG_SVV1

Function

function

Capsid protein VP1

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).
Binds the host receptor ANTXR1 for attachment and uncoating (entry) (PubMed:30381454, PubMed:30514821).

Capsid protein VP2

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).
Binds the host receptor ANTXR1 for attachment and uncoating (entry) (PubMed:30381454, PubMed:30514821).

Capsid protein VP3

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 (Probable). 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).
Vp3 also seems to be involved in the binding to host receptor ANTXR1 for attachment and uncoating (entry) (PubMed:30381454).

Capsid protein VP4

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).

Capsid protein VP0

VP0 precursor is a component of immature procapsids.

Protein 2A

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.

Protein 2B

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.

Protein 2C

Associates with and induces structural rearrangements of intracellular membranes.

VPg

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

Protease 3C

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:28566380, PubMed:29427864, PubMed:30408499).
Deubiquitinase that acts on both lysine-48- and lysine-63-linked polyubiquitin chains and inhibits the ubiquitination of the ATP-dependent RNA helicase RIGI, 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).
Inhibits the integrated stress response (ISR) in the infected cell by disrupting eIF4GI-G3BP1 interaction (PubMed:33133097).
Stress granule formation is thus inhibited (PubMed:33133097).

RNA-directed RNA polymerase

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

Catalytic activity

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site79-80Cleavage; by protease 3C
Site150-151Cleavage
Site434-435Cleavage; by protease 3C
Site673-674Cleavage; by protease 3C
Site937-938Cleavage; by protease 3C
Site946-947Cleavage; by ribosomal skip
Site1074-1075Cleavage; by protease 3C
Binding site1197-1204ATP (UniProtKB | ChEBI)
Site1396-1397Cleavage; by protease 3C
Site1486-1487Cleavage; by protease 3C
Site1507-1508Cleavage; by protease 3C
Active site1556For protease 3C activity and deubiquitinase activity
Active site1592For protease 3C activity
Active site1668For protease 3C activity and deubiquitinase activity
Site1719-1720Cleavage; by protease 3C
Active site1956For RdRp activity
Active site2054For RdRp activity

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasmic vesicle membrane
Cellular Componenthost cell nucleolus
Cellular Componentmembrane
Cellular ComponentT=pseudo3 icosahedral viral capsid
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionchannel activity
Molecular Functioncysteine-type deubiquitinase activity
Molecular Functioncysteine-type endopeptidase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionstructural molecule activity
Biological Processadhesion receptor-mediated virion attachment to host cell
Biological ProcessDNA-templated transcription
Biological Processentry receptor-mediated virion attachment to host cell
Biological Processmonoatomic ion transmembrane transport
Biological Processproteolysis
Biological ProcessRNA-protein covalent cross-linking
Biological Processsymbiont entry into host cell
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity
Biological Processsymbiont-mediated suppression of host toll-like receptor signaling pathway
Biological Processsymbiont-mediated suppression of host TRAF-mediated signal transduction
Biological Processviral RNA genome replication
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    Q155Z9

Proteomes

Subcellular Location

Capsid protein VP2

Virion
Host cytoplasm

Capsid protein VP3

Virion
Host cytoplasm

Capsid protein VP1

Virion
Host cytoplasm

Protein 2A

Protein 2B

Host cytoplasmic vesicle membrane
; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.

Protein 2C

Host cytoplasmic vesicle membrane
; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.

Protein 3A

Host cytoplasmic vesicle membrane
; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.

VPg

Virion

Protease 3C

Host cytoplasm

RNA-directed RNA polymerase

Host cytoplasmic vesicle membrane
; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis31690% loss of viral replication.
Mutagenesis331Complete loss of viral replication; when associated with A-332 and A-333.
Mutagenesis332Complete loss of viral replication; when associated with A-331 and A-333.
Mutagenesis333Complete loss of viral replication; when associated with A-331 and A-332.
Mutagenesis336Complete loss of viral replication; when associated with A-337.
Mutagenesis337Complete loss of viral replication; when associated with A-336.
Mutagenesis76190% loss of viral replication.
Mutagenesis1556Complete loss of protease 3C deubiquitinating activity and ability to block IFN-beta induction.
Mutagenesis1668Complete loss of protease 3C deubiquitinating activity and ability to block IFN-beta induction.

PTM/Processing

Features

Showing features for chain, lipidation, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004469241-79Leader protein
ChainPRO_00004469231-2181Genome polyprotein
Lipidation80N-myristoyl glycine; by host
ChainPRO_000044692680-150Capsid protein VP4
ChainPRO_000044692580-434Capsid protein VP0
ChainPRO_0000446927151-434Capsid protein VP2
ChainPRO_0000446928435-673Capsid protein VP3
ChainPRO_0000446929674-937Capsid protein VP1
ChainPRO_0000446930938-946Protein 2A
ChainPRO_0000446931947-1074Protein 2B
ChainPRO_00004469321075-1396Protein 2C
ChainPRO_00004469331397-1486Protein 3A
ChainPRO_00004469341487-1507VPg
Modified residue1489O-(5'-phospho-RNA)-tyrosine
ChainPRO_00004469351508-1719Protease 3C
ChainPRO_00004469361720-2181RNA-directed RNA polymerase

Post-translational modification

Genome polyprotein

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).

Capsid protein VP0

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.

Capsid protein VP4

Myristoylation is required during RNA encapsidation and formation of the mature virus particle.

VPg

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.

Keywords

Interaction

Subunit

Capsid protein VP1

Interacts with host entry receptor ANTRX1.

Capsid protein VP2

Interacts with host entry receptor ANTRX1.

Capsid protein VP3

Interacts with host entry receptor ANTRX1.

Protease 3C

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 RIGI (PubMed:30408499).
Interacts with host TBK1 (PubMed:30408499).
Interacts with host TRAF3 (PubMed:30408499).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region316-337Interaction with host receptor ANTXR1
Region761-772Interaction with host receptor ANTXR1
Domain1165-1333SF3 helicase
Region1472-1500Disordered
Domain1511-1704Peptidase C3
Domain1950-2068RdRp catalytic

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,181
  • Mass (Da)
    240,620
  • Last updated
    2006-07-25 v1
  • Checksum
    FA8BF3068931AB9A
MQNSHFSFDTASGTFEDVTGTKVKIVEYPRSVNNGVYDSSTHLEILNLQGEIEILRSFNEYQIRAAKQQLGLDIVYELQGNVQTTSKNDFDSRGNNGNMTFNYYANTYQNSVDFSTSSSASGAGPGNSRGGLAGLLTNFSGILNPLGYLKDHNTEEMENSADRVTTQTAGNTAINTQSSLGVLCAYVEDPTKSDPPSSSTDQPTTTFTAIDRWYTGRLNSWTKAVKTFSFQAVPLPGAFLSRQGGLNGGAFTATLHRHFLMKCGWQVQVQCNLTQFHQGALLVAMVPETTLDVKPDGKAKSLQELNEEQWVEMSDDYRTGKNMPFQSLGTYYRPPNWTWGPNFINPYQVTVFPHQILNARTSTSVDINVPYIGETPTQSSETQNSWTLLVMVLVPLDYKEGATTDPEITFSVRPTSPYFNGLRNRYTAGTDEEQGPIPTAPRENSLMFLSTLPDDTVPAYGNVRTPPVNYLPGEITDLLQLARIPTLMAFERVPEPVPASDTYVPYVAVPTQFDDRPLISFPITLSDPVYQNTLVGAISSNFANYRGCIQITLTFCGPMMARGKFLLSYSPPNGTQPQTLSEAMQCTYSIWDIGLNSSWTFVVPYISPSDYRETRAITNSVYSADGWFSLHKLTKITLPPDCPQSPCILFFASAGEDYTLRLPVDCNPSYVFHSTDNAETGVIEAGNTDTDFSGELAAPGSNHTNVKFLFDRSRLLNVIKVLEKDAVFPRPFPTQEGAQQDDGYFCLLTPRPTVASRPATRFGLYANPSGSGVLANTSLDFNFYSLACFTYFRSDLEVTVVSLEPDLEFAVGWFPSGSEYQASSFVYDQLHVPFHFTGRTPRAFASKGGKVSFVLPWNSVSSVLPVRWGGASKLSSATRGLPAHADWGTIYAFVPRPNEKKSTAVKHVAVYIRYKNARAWCPSMLPFRSYKQKMLMQSGDIETNPGPASDNPILEFLEAENDLVTLASLWKMVHSVQQTWRKYVKNDDFWPNLLSELVGEGSVALAATLSNQASVKALLGLHFLSRGLNYTDFYSLLIEKCSSFFTVEPPPPPAENLMTKPSVKSKFRKLFKMQGPMDKVKDWNQIAAGLKNFQFVRDLVKEVVDWLQAWINKEKASPVLQYQLEMKKLGPVALAHDAFMAGSGPPLSDDQIEYLQNLKSLALTLGKTNLAQSLTTMINAKQSSAQRVEPVVVVLRGKPGCGKSLASTLIAQAVSKRLYGSQSVYSLPPDPDFFDGYKGQFVTLMDDLGQNPDGQDFSTFCQMVSTAQFLPNMADLAEKGRPFTSNLIIATTNLPHFSPVTIADPSAVSRRINYDLTLEVSEAYKKHTRLNFDLAFRRTDAPPIYPFAAHVPFVDVAVRFKNGHQNFNLLELVDSICTDIRAKQQGARNMQTLVLQSPNENDDTPVDEALGRVLSPAAVDEALVDLTPEADPVGRLAILAKLGLALAAVTPGLIILAVGLYRYFSGSDADQEETESEGSVKAPRSENAYDGPKKNSKPPGALSLMEMQQPNVDMGFEAAVAKKVVVPITFMVPNRPSGLTQSALLVTGRTFLINEHTWSNPSWTSFTIRGEVHTRDEPFQTVHFTHHGIPTDLMMVRLGPGNSFPNNLDKFGLDQMPARNSRVVGVSSSYGNFFFSGNFLGFVDSITSEQGTYARLFRYRVTTYKGWCGSALVCEAGGVRRIIGLHSAGAAGIGAGTYISKLGLIKALKHLGEPLATMQGLMTELEPGITVHVPRKSKLRKTTAHAVYKPEFEPAVLSKFDPRLNKDVDLDEVIWSKHTANVPYQPPLFYTYMSEYAHRVFSFLGKDNDILTVKEAILGIPGLDPMDPHTAPGLPYAINGLRRTDLVDFVNGTVDAALAVQIQKFLDGDYSDHVFQTFLKDEIRPSEKVRAGKTRIVDVPSLAHCIVGRMLLGRFAAKFQSHPGFLLGSAIGSDPDVFWTVIGAQLEGRKNTYDVDYSAFDSSHGTGSFEALISHFFTVDNGFSPALGPYLRSLAVSVHAYGERRIKITGGLPSGCAATSLLNTVLNNVIIRTALALTYKEFEYDMVDIIAYGDDLLVGTDYDLDFNEVARRAAKLGYKMTPANKGSVFPPTSSLSDAVFLKRKFVQNNDGLYKPVMDLKNLEAMLSYFKPGTLLEKLQSVSMLAQHSGKEEYDRLMHPFADYGAVPSHEYLQARWRALFD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ641257
EMBL· GenBank· DDBJ
ABG23522.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

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