A0A1J0MS65 · A0A1J0MS65_9PICO
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2225 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.
Affects membrane integrity and causes an increase in membrane permeability.
Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity.
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.
Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.
Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway.
Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF.
Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs.
May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA.
Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.
Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.
VP0 precursor is a component of the immature procapsids.
Catalytic activity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Heptrevirinae > Hepatovirus
Accessions
- Primary accessionA0A1J0MS65
Subcellular Location
UniProt Annotation
GO Annotation
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Host mitochondrion outer membrane ; Single-pass membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homodimer. Homomultimer; probably interacts with membranes in a multimeric form. Seems to assemble into amyloid-like fibers.
Homodimer. Monomer. Interacts with protein 3CD.
Homodimer; disulfide-linked.
Homopentamer. Homooligomer.
Interacts with capsid protein VP1. Interacts with capsid protein VP2.
Interacts with capsid protein VP1. Interacts with capsid protein VP3.
Interacts with capsid protein VP2. Interacts with capsid protein VP3.
Interacts with host ACBD3.
Interacts with human MAVS.
Interacts with protein 3AB.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1202-1364 | SF3 helicase | ||||
Sequence: HQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDM | ||||||
Domain | 1512-1726 | Peptidase C3 | ||||
Sequence: DPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMF | ||||||
Domain | 1974-2095 | RdRp catalytic | ||||
Sequence: DVGLDLDFSAFDASLSPFMIREAGRIMSELSGTPSHFGTALINTIIYSKHLLYNCCYHVCGSMPSGSPCTALLNSIINNVNLYYVFSKIFGKSPVFFCQALKILCYGDDVLIVFSRDVQIDN |
Sequence similarities
Belongs to the picornaviridae polyprotein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,225
- Mass (Da)251,294
- Last updated2017-02-15 v1
- Checksum614915C79DCDF2F7