E9NH99 · E9NH99_FMDVO

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

GO annotations

AspectTerm
Cellular Componentcytoplasmic vesicle membrane
Cellular Componenthost cell cytoplasmic vesicle membrane
Cellular ComponentT=pseudo3 icosahedral viral capsid
Molecular FunctionATP binding
Molecular Functionchannel activity
Molecular Functioncysteine-type endopeptidase activity
Molecular Functionribonucleoside triphosphate phosphatase 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 Processviral protein processing
Biological Processviral RNA genome replication
Biological Processvirion attachment to host cell

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

Accessions

  • Primary accession
    E9NH99

Proteomes

Subcellular Location

Cytoplasmic vesicle membrane
; Peripheral membrane protein
Endoplasmic reticulum membrane
Host cytoplasmic vesicle membrane
; Peripheral membrane protein
Host nucleus
Membrane
; Peripheral membrane protein
Virion

Keywords

PTM/Processing

Keywords

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.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain29-182Peptidase C28
Region198-218Disordered
Compositional bias200-218Polar residues
Region237-265Disordered
Domain1189-1353SF3 helicase
Region1529-1577Disordered
Domain1641-1837Peptidase C3
Domain2085-2203RdRp catalytic

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,321
  • Mass (Da)
    257,954
  • Last updated
    2011-04-05 v1
  • Checksum
    8E38C42EF5B923FC
MTTTDCFIALLHAIREIKARLFLKTQEKMEFTLHNGEKKTFYSRPNTHDNCWLNTILQLFRYVDEPFFDWVYESPENLTLEAIKQLEEITGLELREGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFLKGHEHAVFACVTSDGWYAIDDEDFYPWTPEPSDVLVFVPYDQEPLNGEWKTKVQRRLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDSFGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELCSLKERELYQLTLFPHQFINPRTNMTAHISVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGAQQIKVYANIAPTNVHVAGELPSKEGIFPVACSDGYGGLVTTDPKTADPAYGKVYNPPRNMLPGRFTNLLDVAEACPTFLHFEGGVPYVTTKTDSDRVLTLFDLSLAAKHMSNTFLAGLAQYYAQYSGTINLHFMFTGPTDAKARYMIAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFTFSIPYLSAADYAYTASDTAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVDARTQTTSAGESADPVTATVENYGGETQVQRRQHTDVAFILDRFVKVTPKDQINVLDLMQTPSHTLVGALLRTATYYFADLEVAVKHEGNLTWVPNGAPETALDNTTNPTAYHKAPLTRLALPYTAPHRVLATVYNGNCKYAQGPLANVRGDLQVLAQKAARPLPTSFNYGAIKATRVTELLYRMKRAETYCPRPLLAIHPHEARHKQKIVAPERQLLNFDLLKLAGDVESNPGPFFFSDVRSNFTKLVDTINQMQEDMSTKHGPDFNRLVSAFEELATGVKAIRTGLDEAKPWYKLIKLLSRLSCMAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKISDSLSSLFHVPAPAFSFGAPILLAGLVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAWIASEEKFVTMTDLVPGILEKQRDLNDPSKYKEAKEWLDNARQACLKSGNVHIANLCKVVAPAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRTDSVWYCPPDPDHFDGYNQQTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFTPRTMVCPDALNRRFHFDIDVSAKDGYKINNKLDIIKALEDTHTNPVAMFQYDCALLNGMAVEMKRMQQDMFKPQPPLQNVYQLVQEVIDRVELHEKVSSHPIFKQISIPSQKSVLYFLIEKGQHEAAIEFFEGMVHDSIKEELRPLIQQTSFVKRAFKRLKENFEIVVLCLTLLANIVIMIRETHKRQQMVDDAVNEYIEKANITTDDKTLDEAEKNPLETSGASTVGFRERPLPGHDPVEEQPQAEGPYAGPLERQKPLKVKAKLPQQEGPYAGPMERQKPLKVKAKAPVVKEGPYEGPVKKPVALKVKAKNLIVTESGAPPTDLQKMVMGNTKPVELILDGKTVAICCATGVFGTAYLVPRHLFAEKYDKIMLDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLHRGNRVRDITKHFRDTARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGLFAYRAATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLLKMKAHVDPEPHHEGLIVDTRDVEERVHVMRKTKLAPTVAHGVFNPEYGPAALSNKDPRLNEGVVLDEVIFSKHKGDTKMSPEDKELFRRCAADYASRLHSVLGTANAPLSIYEAIKGVDGLDAMEPDTAPGLPWALQGKRRGALIDFENGTVGPEVQAALELMEKREYKFACQTFLKDEIRPMEKVRAGKTRIVDVLPVEHILYTRMMIGRFCAQMHSNNGPQIGSAVGCNPDVDWQRFGTHFAQYRNVWDVDYSAFDANHCSDAMNIMFEEVFRTDFGFHPNAEWILKTLVNTEHAYENKRITVEGGMPSGCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFKSLGQTITPADKSDKGFVLGHSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRGTIQEKLISVAGLAVHSGPDEYRRLFEPFQGLFEIPSYRSLYLRWVNAVCGDA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias200-218Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HQ632769
EMBL· GenBank· DDBJ
ADV52244.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

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