A0A7S5DXB7 · A0A7S5DXB7_FMDVO

Function

function

Associates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.
Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys-48' and 'Lys-63'-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host RIGI, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this modifier that can no longer be attached to target proteins. Also cleaves host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly.
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.
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome. Upon acidifcation in the endosome, dissociates into pentamers.
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

GO annotations

AspectTerm
Cellular Componentcytoplasmic vesicle membrane
Cellular Componenthost cell cytoplasmic vesicle membrane
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell nucleus
Cellular ComponentT=pseudo3 icosahedral viral capsid
Molecular FunctionATP binding
Molecular Functionchannel activity
Molecular Functioncysteine-type endopeptidase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionstructural molecule activity
Biological Processclathrin-dependent endocytosis of virus by host cell
Biological ProcessDNA-templated transcription
Biological Processmodulation by virus of host chromatin organization
Biological Processmonoatomic ion transmembrane transport
Biological Processproteolysis
Biological Processregulation of translation
Biological ProcessRNA-protein covalent cross-linking
Biological Processviral protein processing
Biological Processviral RNA genome replication
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

Accessions

  • Primary accession
    A0A7S5DXB7

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Forms homooligomers.
Homohexamer. Interacts with host VIM. Interacts with host BECN1.
Interacts (via R-G-D motif) with host ITGAV/ITGB6. Interacts with host MAVS; this interaction inhibits binding of host TRAF3 to MAVS, thereby suppressing interferon-mediated responses.
Interacts with 3B-1; 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 3B-2; this interaction allows 3B-2 to act as a primer. Interacts with 3B-3; this interaction allows 3B-3 to act as a primer.
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.
Interacts with host DCTN3.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain29-182Peptidase C28
Region199-218Disordered
Compositional bias203-218Polar residues
Region237-265Disordered
Domain1189-1353SF3 helicase
Region1529-1608Disordered
Domain1652-1848Peptidase C3
Domain2096-2214RdRp catalytic

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,332
  • Mass (Da)
    258,679
  • Last updated
    2021-06-02 v1
  • Checksum
    9FBD9B71FBBA8EA0
MNTTDCFIALIHIFREIKSLFLLQTQGKMEFTLHNGEKKTFYSRPNNHDNCWLNAILQLFRYVDEPFFDWVYDSPENLTVDAIRQLEELTGLELHEGGPPALVIWNIKHLLYTGVGTASRPSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWFAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGDWKAKVQRRLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVAQAERFFKTHLFDWVTSDPFGRCHLLELPTDHKGVYGGLIDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELCSIQKRELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNSEGAPQIKVYANIAPTNVHVAGELPSKEGIFPVACSDGYGGLVTTDPKTADPAYGKVFNPPRNMLPGRFTNLLDVAEACPTFLHFEGDVPYVTTKTDSDRTLAQFDLSLAAKHMSNTFLAGLAQYYTQYSGTINLHFMFTGPTDAKARYMIAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFTFSIPYLSAADYAYTASSTAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFDLRLPVDARTQTTSPGESADPVTATVENYGGATQVQRRQHTDVSFILDRFVKVAPQDQINVLDLMQIPAHTLVGALLRASTYYFADLELAVTHEGNLTWVPNGAPEAALDNTTNPTAYHKAPLTRLALPYTAPHRVLATVYNGNCKYSDSSATNVRGDLQVLAQKAARTLPTSFNYGAIKATRVTELLYRMKRAETYCPRPLLAIHPSEARHKQKIVAPVKQLLNFDLLKLAGDVESNPGPFFFSDVRSNFSKLVETINQMQEDMSTKHGPDFNRLVSAFEELAAGVKAIRTGLDEAKPWYKLIKLLSRLSCMAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKISDSLSSLFHVPAPVFSFGAPLLVAGLVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAWIASEEKFVTMTDLVPGILEKQRDLNDPSKYKEAKEWLDNARQACLKSGNVHIANLCKVVAPAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRTDSVWYCPPDPDHFDGYNQQTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFTPRTMVCPDALNRRFHFDIDVSAKDGYKINNKLDIIKALEDTHTNPVAMFQYDCALLNGMAVEMKRMQQDVFKPQPPLQNVYQLVQEVIERVELHEKVSSHPIFKQISIPSQKSVLYFLIEKGQHEAAIEFFEGMVHDSIKEELRPLIQNTSFVKRAFKRLKENFEVVALCLTLLANILIMIRETRRRQQMVDDAVNEYIEKANITTDDKTLDEAEKNPLETSGASTVGFRERTLPGQKASDDVNSEPANPVEEQPQAEGPYAGPLERQKPLKVRSKLPQREGPYAGPMERQKPLKVKAKAPVVKEGPYEGPVKKPVALKVKAKNLIVTESGAPPTDLQKMVMGNTKPVELILDGKTVAICCATGVFGTAYLVPRHLFAEKYDKIMLDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLHRGNRVRDITKHFRDTARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGLFAYKAATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLLKMKAHIDPEPHHEGLIVDTRDVEERVHVMRKTKLAPTVAHGVFNPEFGPAALSNKDPRLNEGVVLDEVIFSKHKGDTKMSEEDKALFRRCAADYASRLHSELGTANAPLSIYEAIKGVDGLDAMEPDTAPGLPWALQGKRRGALIDFENGVVGPEVAAALELMEKREYKFACQTFLKDEIRPMEKVRAGKTRIVDVLPVEHILYTRMMIGRFCAQMHSNNGPRIGSAVGCNPDVDWQRFGTHFAQYRNVWDVDYSAFDANHCSDAMNIMFEEVFRTEFGFHPNAEWILKTLVNTEHAYENKRITVEGGMPSGCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFKSLGQTITPADKSDKGFVLGHSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRGTIQEKLISVAGLAVHSGPDEYRRLFEPFQGLFEIPSYRSLYLRWVNAVCGDA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias203-218Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MH167964
EMBL· GenBank· DDBJ
QCS60947.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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