Q155Z9 · POLG_SVV1
- ProteinGenome polyprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2181 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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).
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).
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).
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).
Performs VPg uridylylation (By similarity).
Catalytic activity
- RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 79-80 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 150-151 | Cleavage | ||||
Sequence: KD | ||||||
Site | 434-435 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 673-674 | Cleavage; by protease 3C | ||||
Sequence: HS | ||||||
Site | 937-938 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Site | 946-947 | Cleavage; by ribosomal skip | ||||
Sequence: GP | ||||||
Site | 1074-1075 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Binding site | 1197-1204 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GKPGCGKS | ||||||
Site | 1396-1397 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Site | 1486-1487 | Cleavage; by protease 3C | ||||
Sequence: EN | ||||||
Site | 1507-1508 | Cleavage; by protease 3C | ||||
Sequence: MQ | ||||||
Active site | 1556 | For protease 3C activity and deubiquitinase activity | ||||
Sequence: H | ||||||
Active site | 1592 | For protease 3C activity | ||||
Sequence: D | ||||||
Active site | 1668 | For protease 3C activity and deubiquitinase activity | ||||
Sequence: C | ||||||
Site | 1719-1720 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Active site | 1956 | For RdRp activity | ||||
Sequence: D | ||||||
Active site | 2054 | For RdRp activity | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
- Cleaved into 13 chains
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Caphthovirinae > Senecavirus > Senecavirus valles
- Virus hosts
Accessions
- Primary accessionQ155Z9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Capsid protein VP2
Capsid protein VP3
Capsid protein VP1
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
Protease 3C
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
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 316 | 90% loss of viral replication. | ||||
Sequence: D → A | ||||||
Mutagenesis | 331 | Complete loss of viral replication; when associated with A-332 and A-333. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 332 | Complete loss of viral replication; when associated with A-331 and A-333. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 333 | Complete loss of viral replication; when associated with A-331 and A-332. | ||||
Sequence: R → A | ||||||
Mutagenesis | 336 | Complete loss of viral replication; when associated with A-337. | ||||
Sequence: N → A | ||||||
Mutagenesis | 337 | Complete loss of viral replication; when associated with A-336. | ||||
Sequence: W → A | ||||||
Mutagenesis | 761 | 90% loss of viral replication. | ||||
Sequence: R → A | ||||||
Mutagenesis | 1556 | Complete loss of protease 3C deubiquitinating activity and ability to block IFN-beta induction. | ||||
Sequence: H → A | ||||||
Mutagenesis | 1668 | Complete loss of protease 3C deubiquitinating activity and ability to block IFN-beta induction. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for chain, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446924 | 1-79 | Leader protein | |||
Sequence: MQNSHFSFDTASGTFEDVTGTKVKIVEYPRSVNNGVYDSSTHLEILNLQGEIEILRSFNEYQIRAAKQQLGLDIVYELQ | ||||||
Chain | PRO_0000446923 | 1-2181 | Genome polyprotein | |||
Sequence: MQNSHFSFDTASGTFEDVTGTKVKIVEYPRSVNNGVYDSSTHLEILNLQGEIEILRSFNEYQIRAAKQQLGLDIVYELQGNVQTTSKNDFDSRGNNGNMTFNYYANTYQNSVDFSTSSSASGAGPGNSRGGLAGLLTNFSGILNPLGYLKDHNTEEMENSADRVTTQTAGNTAINTQSSLGVLCAYVEDPTKSDPPSSSTDQPTTTFTAIDRWYTGRLNSWTKAVKTFSFQAVPLPGAFLSRQGGLNGGAFTATLHRHFLMKCGWQVQVQCNLTQFHQGALLVAMVPETTLDVKPDGKAKSLQELNEEQWVEMSDDYRTGKNMPFQSLGTYYRPPNWTWGPNFINPYQVTVFPHQILNARTSTSVDINVPYIGETPTQSSETQNSWTLLVMVLVPLDYKEGATTDPEITFSVRPTSPYFNGLRNRYTAGTDEEQGPIPTAPRENSLMFLSTLPDDTVPAYGNVRTPPVNYLPGEITDLLQLARIPTLMAFERVPEPVPASDTYVPYVAVPTQFDDRPLISFPITLSDPVYQNTLVGAISSNFANYRGCIQITLTFCGPMMARGKFLLSYSPPNGTQPQTLSEAMQCTYSIWDIGLNSSWTFVVPYISPSDYRETRAITNSVYSADGWFSLHKLTKITLPPDCPQSPCILFFASAGEDYTLRLPVDCNPSYVFHSTDNAETGVIEAGNTDTDFSGELAAPGSNHTNVKFLFDRSRLLNVIKVLEKDAVFPRPFPTQEGAQQDDGYFCLLTPRPTVASRPATRFGLYANPSGSGVLANTSLDFNFYSLACFTYFRSDLEVTVVSLEPDLEFAVGWFPSGSEYQASSFVYDQLHVPFHFTGRTPRAFASKGGKVSFVLPWNSVSSVLPVRWGGASKLSSATRGLPAHADWGTIYAFVPRPNEKKSTAVKHVAVYIRYKNARAWCPSMLPFRSYKQKMLMQSGDIETNPGPASDNPILEFLEAENDLVTLASLWKMVHSVQQTWRKYVKNDDFWPNLLSELVGEGSVALAATLSNQASVKALLGLHFLSRGLNYTDFYSLLIEKCSSFFTVEPPPPPAENLMTKPSVKSKFRKLFKMQGPMDKVKDWNQIAAGLKNFQFVRDLVKEVVDWLQAWINKEKASPVLQYQLEMKKLGPVALAHDAFMAGSGPPLSDDQIEYLQNLKSLALTLGKTNLAQSLTTMINAKQSSAQRVEPVVVVLRGKPGCGKSLASTLIAQAVSKRLYGSQSVYSLPPDPDFFDGYKGQFVTLMDDLGQNPDGQDFSTFCQMVSTAQFLPNMADLAEKGRPFTSNLIIATTNLPHFSPVTIADPSAVSRRINYDLTLEVSEAYKKHTRLNFDLAFRRTDAPPIYPFAAHVPFVDVAVRFKNGHQNFNLLELVDSICTDIRAKQQGARNMQTLVLQSPNENDDTPVDEALGRVLSPAAVDEALVDLTPEADPVGRLAILAKLGLALAAVTPGLIILAVGLYRYFSGSDADQEETESEGSVKAPRSENAYDGPKKNSKPPGALSLMEMQQPNVDMGFEAAVAKKVVVPITFMVPNRPSGLTQSALLVTGRTFLINEHTWSNPSWTSFTIRGEVHTRDEPFQTVHFTHHGIPTDLMMVRLGPGNSFPNNLDKFGLDQMPARNSRVVGVSSSYGNFFFSGNFLGFVDSITSEQGTYARLFRYRVTTYKGWCGSALVCEAGGVRRIIGLHSAGAAGIGAGTYISKLGLIKALKHLGEPLATMQGLMTELEPGITVHVPRKSKLRKTTAHAVYKPEFEPAVLSKFDPRLNKDVDLDEVIWSKHTANVPYQPPLFYTYMSEYAHRVFSFLGKDNDILTVKEAILGIPGLDPMDPHTAPGLPYAINGLRRTDLVDFVNGTVDAALAVQIQKFLDGDYSDHVFQTFLKDEIRPSEKVRAGKTRIVDVPSLAHCIVGRMLLGRFAAKFQSHPGFLLGSAIGSDPDVFWTVIGAQLEGRKNTYDVDYSAFDSSHGTGSFEALISHFFTVDNGFSPALGPYLRSLAVSVHAYGERRIKITGGLPSGCAATSLLNTVLNNVIIRTALALTYKEFEYDMVDIIAYGDDLLVGTDYDLDFNEVARRAAKLGYKMTPANKGSVFPPTSSLSDAVFLKRKFVQNNDGLYKPVMDLKNLEAMLSYFKPGTLLEKLQSVSMLAQHSGKEEYDRLMHPFADYGAVPSHEYLQARWRALFD | ||||||
Lipidation | 80 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Chain | PRO_0000446926 | 80-150 | Capsid protein VP4 | |||
Sequence: GNVQTTSKNDFDSRGNNGNMTFNYYANTYQNSVDFSTSSSASGAGPGNSRGGLAGLLTNFSGILNPLGYLK | ||||||
Chain | PRO_0000446925 | 80-434 | Capsid protein VP0 | |||
Sequence: GNVQTTSKNDFDSRGNNGNMTFNYYANTYQNSVDFSTSSSASGAGPGNSRGGLAGLLTNFSGILNPLGYLKDHNTEEMENSADRVTTQTAGNTAINTQSSLGVLCAYVEDPTKSDPPSSSTDQPTTTFTAIDRWYTGRLNSWTKAVKTFSFQAVPLPGAFLSRQGGLNGGAFTATLHRHFLMKCGWQVQVQCNLTQFHQGALLVAMVPETTLDVKPDGKAKSLQELNEEQWVEMSDDYRTGKNMPFQSLGTYYRPPNWTWGPNFINPYQVTVFPHQILNARTSTSVDINVPYIGETPTQSSETQNSWTLLVMVLVPLDYKEGATTDPEITFSVRPTSPYFNGLRNRYTAGTDEEQ | ||||||
Chain | PRO_0000446927 | 151-434 | Capsid protein VP2 | |||
Sequence: DHNTEEMENSADRVTTQTAGNTAINTQSSLGVLCAYVEDPTKSDPPSSSTDQPTTTFTAIDRWYTGRLNSWTKAVKTFSFQAVPLPGAFLSRQGGLNGGAFTATLHRHFLMKCGWQVQVQCNLTQFHQGALLVAMVPETTLDVKPDGKAKSLQELNEEQWVEMSDDYRTGKNMPFQSLGTYYRPPNWTWGPNFINPYQVTVFPHQILNARTSTSVDINVPYIGETPTQSSETQNSWTLLVMVLVPLDYKEGATTDPEITFSVRPTSPYFNGLRNRYTAGTDEEQ | ||||||
Chain | PRO_0000446928 | 435-673 | Capsid protein VP3 | |||
Sequence: GPIPTAPRENSLMFLSTLPDDTVPAYGNVRTPPVNYLPGEITDLLQLARIPTLMAFERVPEPVPASDTYVPYVAVPTQFDDRPLISFPITLSDPVYQNTLVGAISSNFANYRGCIQITLTFCGPMMARGKFLLSYSPPNGTQPQTLSEAMQCTYSIWDIGLNSSWTFVVPYISPSDYRETRAITNSVYSADGWFSLHKLTKITLPPDCPQSPCILFFASAGEDYTLRLPVDCNPSYVFH | ||||||
Chain | PRO_0000446929 | 674-937 | Capsid protein VP1 | |||
Sequence: STDNAETGVIEAGNTDTDFSGELAAPGSNHTNVKFLFDRSRLLNVIKVLEKDAVFPRPFPTQEGAQQDDGYFCLLTPRPTVASRPATRFGLYANPSGSGVLANTSLDFNFYSLACFTYFRSDLEVTVVSLEPDLEFAVGWFPSGSEYQASSFVYDQLHVPFHFTGRTPRAFASKGGKVSFVLPWNSVSSVLPVRWGGASKLSSATRGLPAHADWGTIYAFVPRPNEKKSTAVKHVAVYIRYKNARAWCPSMLPFRSYKQKMLMQ | ||||||
Chain | PRO_0000446930 | 938-946 | Protein 2A | |||
Sequence: SGDIETNPG | ||||||
Chain | PRO_0000446931 | 947-1074 | Protein 2B | |||
Sequence: PASDNPILEFLEAENDLVTLASLWKMVHSVQQTWRKYVKNDDFWPNLLSELVGEGSVALAATLSNQASVKALLGLHFLSRGLNYTDFYSLLIEKCSSFFTVEPPPPPAENLMTKPSVKSKFRKLFKMQ | ||||||
Chain | PRO_0000446932 | 1075-1396 | Protein 2C | |||
Sequence: GPMDKVKDWNQIAAGLKNFQFVRDLVKEVVDWLQAWINKEKASPVLQYQLEMKKLGPVALAHDAFMAGSGPPLSDDQIEYLQNLKSLALTLGKTNLAQSLTTMINAKQSSAQRVEPVVVVLRGKPGCGKSLASTLIAQAVSKRLYGSQSVYSLPPDPDFFDGYKGQFVTLMDDLGQNPDGQDFSTFCQMVSTAQFLPNMADLAEKGRPFTSNLIIATTNLPHFSPVTIADPSAVSRRINYDLTLEVSEAYKKHTRLNFDLAFRRTDAPPIYPFAAHVPFVDVAVRFKNGHQNFNLLELVDSICTDIRAKQQGARNMQTLVLQ | ||||||
Chain | PRO_0000446933 | 1397-1486 | Protein 3A | |||
Sequence: SPNENDDTPVDEALGRVLSPAAVDEALVDLTPEADPVGRLAILAKLGLALAAVTPGLIILAVGLYRYFSGSDADQEETESEGSVKAPRSE | ||||||
Chain | PRO_0000446934 | 1487-1507 | VPg | |||
Sequence: NAYDGPKKNSKPPGALSLMEM | ||||||
Modified residue | 1489 | O-(5'-phospho-RNA)-tyrosine | ||||
Sequence: Y | ||||||
Chain | PRO_0000446935 | 1508-1719 | Protease 3C | |||
Sequence: QQPNVDMGFEAAVAKKVVVPITFMVPNRPSGLTQSALLVTGRTFLINEHTWSNPSWTSFTIRGEVHTRDEPFQTVHFTHHGIPTDLMMVRLGPGNSFPNNLDKFGLDQMPARNSRVVGVSSSYGNFFFSGNFLGFVDSITSEQGTYARLFRYRVTTYKGWCGSALVCEAGGVRRIIGLHSAGAAGIGAGTYISKLGLIKALKHLGEPLATMQ | ||||||
Chain | PRO_0000446936 | 1720-2181 | RNA-directed RNA polymerase | |||
Sequence: GLMTELEPGITVHVPRKSKLRKTTAHAVYKPEFEPAVLSKFDPRLNKDVDLDEVIWSKHTANVPYQPPLFYTYMSEYAHRVFSFLGKDNDILTVKEAILGIPGLDPMDPHTAPGLPYAINGLRRTDLVDFVNGTVDAALAVQIQKFLDGDYSDHVFQTFLKDEIRPSEKVRAGKTRIVDVPSLAHCIVGRMLLGRFAAKFQSHPGFLLGSAIGSDPDVFWTVIGAQLEGRKNTYDVDYSAFDSSHGTGSFEALISHFFTVDNGFSPALGPYLRSLAVSVHAYGERRIKITGGLPSGCAATSLLNTVLNNVIIRTALALTYKEFEYDMVDIIAYGDDLLVGTDYDLDFNEVARRAAKLGYKMTPANKGSVFPPTSSLSDAVFLKRKFVQNNDGLYKPVMDLKNLEAMLSYFKPGTLLEKLQSVSMLAQHSGKEEYDRLMHPFADYGAVPSHEYLQARWRALFD |
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).
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
- PTM
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).
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
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 316-337 | Interaction with host receptor ANTXR1 | ||||
Sequence: DYRTGKNMPFQSLGTYYRPPNW | ||||||
Region | 761-772 | Interaction with host receptor ANTXR1 | ||||
Sequence: RFGLYANPSGSG | ||||||
Domain | 1165-1333 | SF3 helicase | ||||
Sequence: LGKTNLAQSLTTMINAKQSSAQRVEPVVVVLRGKPGCGKSLASTLIAQAVSKRLYGSQSVYSLPPDPDFFDGYKGQFVTLMDDLGQNPDGQDFSTFCQMVSTAQFLPNMADLAEKGRPFTSNLIIATTNLPHFSPVTIADPSAVSRRINYDLTLEVSEAYKKHTRLNFD | ||||||
Region | 1472-1500 | Disordered | ||||
Sequence: EETESEGSVKAPRSENAYDGPKKNSKPPG | ||||||
Domain | 1511-1704 | Peptidase C3 | ||||
Sequence: NVDMGFEAAVAKKVVVPITFMVPNRPSGLTQSALLVTGRTFLINEHTWSNPSWTSFTIRGEVHTRDEPFQTVHFTHHGIPTDLMMVRLGPGNSFPNNLDKFGLDQMPARNSRVVGVSSSYGNFFFSGNFLGFVDSITSEQGTYARLFRYRVTTYKGWCGSALVCEAGGVRRIIGLHSAGAAGIGAGTYISKLGL | ||||||
Domain | 1950-2068 | RdRp catalytic | ||||
Sequence: KNTYDVDYSAFDSSHGTGSFEALISHFFTVDNGFSPALGPYLRSLAVSVHAYGERRIKITGGLPSGCAATSLLNTVLNNVIIRTALALTYKEFEYDMVDIIAYGDDLLVGTDYDLDFNE |
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,181
- Mass (Da)240,620
- Last updated2006-07-25 v1
- ChecksumFA8BF3068931AB9A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ641257 EMBL· GenBank· DDBJ | ABG23522.1 EMBL· GenBank· DDBJ | Genomic RNA |