A0A0S1VX69 · A0A0S1VX69_9POTV

Function

function

An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Has RNA-binding and proteolytic activities.
Has helicase activity. It may be involved in replication.
Indispensable for virus replication.
Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity).
Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity).
VPg-RNA directly binds EIF4E and is a template for transcription (By similarity).
Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation
Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.

Catalytic activity

  • Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
    EC:3.4.22.45 (UniProtKB | ENZYME | Rhea)
  • Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
    EC:3.4.22.44 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site729For helper component proteinase activity
Active site802For helper component proteinase activity

GO annotations

AspectTerm
Cellular Componenthelical viral capsid
Cellular Componenthost cell cytoplasmic vesicle
Cellular Componenthost cell nucleus
Cellular Componentvesicle
Molecular FunctionATP binding
Molecular Functioncysteine-type endopeptidase activity
Molecular Functionhelicase activity
Molecular Functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Molecular FunctionRNA binding
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionserine-type peptidase activity
Molecular Functionstructural molecule activity
Biological ProcessDNA-templated transcription
Biological Processproteolysis
Biological Processviral RNA genome replication

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CTCRI-II-14
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Pisuviricota > Stelpaviricetes > Patatavirales > Potyviridae > Potyvirus

Accessions

  • Primary accession
    A0A0S1VX69

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain240-385Peptidase S30
Domain721-843Peptidase C6
Domain1313-1465Helicase ATP-binding
Domain1480-1643Helicase C-terminal
Domain2119-2337Peptidase C4
Domain2603-2727RdRp catalytic
Region2885-2953Disordered
Compositional bias2891-2915Polar residues
Compositional bias2916-2931Pro residues

Sequence similarities

Belongs to the potyviridae genome polyprotein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    3,190
  • Mass (Da)
    362,238
  • Last updated
    2016-02-17 v1
  • Checksum
    727C02A0009A81BE
MACMVFGSFANSHLASTKVVTGKMREESRVKAKFNGGSILFPTIQEGNKPLSQNEPNFMIGSYNPLLAQSSGVGARSVHTEVRTIKMIGIHGATTVIAPNIMAPVVRVARPSITQINNYGRRLIKQAQDQVDRAFENFFSKPEMKESLFKKSHAKLVRGRKQSWRLSTPTIEIARERQVALDKERQEREAFLAGKYNPEDVVGGYVDIRDRTKRGEQISFKGPFWRRTPKTPRVVKEQPQIVVANALKVERDLLRSLQHTNIGVEYIGRKKQRLRASFVQAPNGGRYARVELPHMRNGTRLRREIDPQRWGSTIQRLASAVRYVKKIHDLEVSHGWSGIVMDQRQPLIHKISRSSIFVVRGRLNGKLVSACDDFLWNNALKIVQYAKTPEAQFFQGWREVFTGMGPQKDDHGCTIDFTNEQCGQVAAAISQTMFPVRKLSCLICRNALTRMSDEEYKAHIAANMECAKEILDIKEQELFGLSTVLKLVRRAVVENINLTTSTEIVRLTQNHTSTHMLQIQDINKALMKGSTVSQEDLDKASQQLLRMTQWFKKHLSPIGDGDLGSFRNKRASKALLNPSLLCDNQLDKNGNFVWGERGYHSKRFFSNYFEEIEPTDGYSKYIIRRNPSGARKLAIGSLIVSLNLERARIALMGEPIEKVPLTMACVSRQDNNYVYTCCCVTNEDGTPMLSELRSPTKHHLVLGNTGDSKFVDLPALETNRMYIAKNGFCYMNIFLAMLINVNENEAKNFTKMVRDRLVPMLGEWPTVQDLATSMYILTVFHPETRNAELPRILVDHTTQTMHVIDSYGSLSTGYHILKAGTVGQFLHFAADDLKSEMKFYRVGGDAEQRMRCETALIKGIFKPKLMMALLREDPYITLMGLVSPTILFHMYRMRNLEKGIELWINKNQEVGKIFIILEQLVRKMAVNDVLLDQLSIITNTAPHLLEIVQNCPREGHAYKPAIDLLNIFVEHQASNKVLIENGFSDISEQLYSEREKIFVQKLKQEWHALNLLEKCSLTLQQKKFSTLTENYLTAQAFKDSSETSKNCMRLCFTTPTKCIQRAKSLCVEKISRVGQAAVRKVVSILLGVFNKCYSDIIYLVNVCIIFSLLVQMVGVVRNIVNTARTEKAYIAAIKRQEDENTIVRIYNILSNDGVNRPTKHEFEKQLESLRPDLLSTFNYMVADDVVEVQAKTALQLQFEKIIAFLAIVTMCIDAERSDAVFRLLSKLKTVFTTVGEDVRIQSLDDIENIEDCKNLTVDFDITSTKEPPAMSFDVHFEDWWSKQLQLNRVVPHYRSSGKFLEFTRATAAKVANEIMLHEDHEFLIRGAVGSGKSTGLPHHLSKKGRVLLLEPTRPLAENVSKQLAKDPFFQQVTLRMRGMSVFGSSNIVVMTSGFAFHYYVNNPHQLSEFDFIIIDECHVMDAPTIAFNCALKEFNFSGKLLKVSATPPGRECEFTTQHPVKLIVEETLSLQGFAQAQGTQSNADMIKHGHNILVYVASYNDVDTLSRQLSERKYKVTKVDGRTMQMGNIEIKTEGCEGKPHFIIATNIIENGVTIDIDCVVDFGQKVVATLDSESRCMRYNKTSVSYGERIQRLGRVGRFKAGTALRIGHTERGIDEIPASIATEAAFLSFAYGLPVTTQGVTTDILSRCTVKQARVALNFEITPFFTVHFVRFDGSMHPEVHKLLKGFKLRESEMLLNKLAIPNQYVNQWISVREYDRLGVKLQCPETTRIPFYARGIPDTLFEHLWETVQSYKSDAGFGRISTVNASKISYTLSTDPHAIPRTVAIIDHLLSEEMIKKDHFDTIGSTVTGYSFSLTGIVEGIRKRYLKDFSTENIATLQQAKAQLLDINTRHINFSNYSDVADLGVLRAVQFQNKSEICKFLDLKGKWDGRKFTNDLIVGAITLLGGGWLIYEYFSRTMRDPVTAQGKKRQIQKLKFRDARDRKLGREIYCDDNTMEHTFGEAYTKKGKQKGSTHTKGMGKKNKNFVHIYGVEPEQYNFIRFVDPLTGYTLDENPRADMQLIQEEIGKVRRELINEGELEPQAIYSRPGIEAYFINNNAAEALKVDLTPHRPTLLQLNSNAIAGFPEREDELRQTGQPVKIYKDLVPKANEYVAMEGKSVYKGLRDYNSIATIVCHISNESNGHKMTLFGIGYGSIVITNSHLFKHNNGTITINTWHGEFIIKNSTQLKIHHVTGKDMVLIQMPKDFPPFIRKSQFRGPKREERVCMIGTNFQDKSMRATISESSLILPEGQGTFWKHWISTKDGECGIPMVAVNDGQIVGFHGLASNISERNYFVPFTDDFEQTHLKRLDSLEWTQHWHFQPDKIAWGSLKLVNDQPTDEFKISKLISDLFENPVQLQGFQSGWVLNSVEGNLKAMAQCESALVTKHTVKGPCRYFSEYLSVNQEAEKFFRPLMGAYAPSRLNREAFKKDFFKYGKPVEVNRVDFNAFQAAVASVETMMMETGFSECEYITDAQTIIDSLNMKAAVGAQYRGKKSEYFHDMEIYDKERLLFQSCERLFYGKKGVWNGSLKAELRPIEKTQLNKTRTFTAAPLDTLLGAKTCVDDFNNQFYNLNLKCPWTVGMTKFYKGWDTLMRKLPEGWVYCHADGSQFDSSLTPLLINAVVDIRKFFMEEWWIGEEMLDNLYAEIVYTPILTPDGTIFKKFRGNNSGQPSTVVDNTLMVVISVYYACIKQGWTEYDVSQRIVFFANGDDIILAVQQDDEPILNTFQNSFHELGLNYDFSERTLKREELWFMSHQAMKVGDIYIPKLERERIVSILEWDRSKEIMHRTEAICAAMIEAWGYTDLLQEIRKFYLWLLEKEEFKTLASEGRAPYIAETALKKLYTDENVKECELQRYLDAFNFELFCDHDKVVGQADDTVDAGKGTTPAAGGGNTTPAAGGGNNTNNTPPPANNTTNNTPPPPPPAVPKATETSANKQVVPTTSEKGKEIVKDVNAGTSGTYSVPRLNKITNKMNLPLVKGKCILNLNHLIEYKPEQRDIFNTRATHTQFEVWYNAVKREYELEDEQMHIVMNGFMVWCIDNGTSPDINGAWVMMDGNDQIEYPLKPIVENAKPTLRQIMHHFSDAAEAYIELRNAEKPYMPRYGLIRNLRDASLARYAFDFYEVNSKTPVRAREAVAQMKAAALSNVTTRLFGLDGNVSTSSENTERHTAKDVTPNMHTLLGVSPPQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias2891-2915Polar residues
Compositional bias2916-2931Pro residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KT026108
EMBL· GenBank· DDBJ
ALM55782.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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