A6XP79 · A6XP79_FMDA1
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2328 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.
Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease.
Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. 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. After genome has been released, the channel shrinks.
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. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally 'trimmed' from the C-terminus of the upstream protein 1D by 3C proteinase.
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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.
Catalytic activity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphate
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | host cell cytoplasmic vesicle membrane | |
Cellular Component | T=pseudo3 icosahedral viral capsid | |
Molecular Function | ATP binding | |
Molecular Function | channel activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Molecular Function | structural molecule activity | |
Biological Process | clathrin-dependent endocytosis of virus by host cell | |
Biological Process | DNA-templated transcription | |
Biological Process | modulation by virus of host chromatin organization | |
Biological Process | monoatomic ion transmembrane transport | |
Biological Process | proteolysis | |
Biological Process | regulation of translation | |
Biological Process | viral protein processing | |
Biological Process | viral RNA genome replication | |
Biological Process | virion attachment to host cell |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Organism names
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Caphthovirinae > Aphthovirus > Foot-and-mouth disease virus
Accessions
- Primary accessionA6XP79
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Forms homooligomers.
Interacts with RNA-dependent RNA polymerase; this interaction allows 3B-1 to binds 2 polymerases and act as a primer. It also allows the recruitment of the RNA-dependent RNA polymerase to host membranes.
Interacts with RNA-dependent RNA polymerase; this interaction allows 3B-2 to act as a primer.
Interacts with RNA-dependent RNA polymerase; this interaction allows 3B-3 to act as a primer.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-182 | Peptidase C28 | ||||
Sequence: MEFTLYNGEKKTFYSRPNNHDNCWLNTIPQLFRYVDEPFFDWVYESPANLTLEAIKQLEKVTGLELTEGGPPALVIWNIRHLLHTGIGTASRPSEVCMVGGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVYVP | ||||||
Region | 199-218 | Disordered | ||||
Sequence: RLKGAGQSSPATGSQNQSGN | ||||||
Compositional bias | 203-218 | Polar residues | ||||
Sequence: AGQSSPATGSQNQSGN | ||||||
Region | 238-265 | Disordered | ||||
Sequence: QLGDNAISGGSNEGSTDTTSTHTNNTQN | ||||||
Domain | 1185-1349 | SF3 helicase | ||||
Sequence: NVHIANLCKVVAPAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRTDSVWYCPPDPDHFDGYNQQTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFTPRTMVCPDALNRRFHFDIDVSAKDGYKTNNKLD | ||||||
Region | 1525-1580 | Disordered | ||||
Sequence: KTLDEAEKNPLETSGASTVGFRERTLPGHKVSDDVNSEPTKPAEEQPQAEGPYAGP | ||||||
Compositional bias | 1550-1564 | Basic and acidic residues | ||||
Sequence: LPGHKVSDDVNSEPT | ||||||
Domain | 1648-1844 | Peptidase C3 | ||||
Sequence: APPTDLQKMVMGNTKPVELILDGKTVAICCATGVFGTAYLVPRHLFAEKYDKIMLDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLHRGNRVRDITKHFRDTARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGLFAYRAATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSML | ||||||
Domain | 2092-2210 | RdRp catalytic | ||||
Sequence: RNVWDVDYSAFDANHCSDAMNIMFEEVFRTEFGFHPNAEWILKTLVNTEHAYENKRITVEGGMPSGCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEA |
Sequence similarities
Belongs to the picornaviruses polyprotein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,328
- Mass (Da)258,835
- Last updated2007-08-21 v1
- ChecksumFBDB6A0A7891DD5C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 203-218 | Polar residues | ||||
Sequence: AGQSSPATGSQNQSGN | ||||||
Compositional bias | 1550-1564 | Basic and acidic residues | ||||
Sequence: LPGHKVSDDVNSEPT |