P17766 · POLG_PPVNA

Function

function

Helper component proteinase

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.

Cytoplasmic inclusion protein

Has helicase activity. It may be involved in replication.

6 kDa protein 1

Indispensable for virus replication (By similarity).
Reduces the abundance of host transcripts related to jasmonic acid biosynthesis therefore altering the host defenses (By similarity).
In order to increase its own stability, decreases host protein degradation pathways (By similarity).

6 kDa protein 2

Indispensable for virus replication.

Viral genome-linked protein

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 (By similarity).

Nuclear inclusion protein A

Has RNA-binding and proteolytic activities.

Nuclear inclusion protein B

An RNA-dependent RNA polymerase that plays an essential role in the virus replication.

Capsid protein

Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.

Catalytic activity

Features

Showing features for active site, site, binding site.

TypeIDPosition(s)Description
Active site216For P1 proteinase activity
Active site225For P1 proteinase activity
Active site259For P1 proteinase activity
Site308-309Cleavage; by P1 proteinase
Active site652For helper component proteinase activity
Active site725For helper component proteinase activity
Site766-767Cleavage; by autolysis
Site1116-1117Cleavage; by NIa-pro
Site1168-1169Cleavage; by NIa-pro
Binding site1253-1260ATP (UniProtKB | ChEBI)
Site1803-1804Cleavage; by NIa-pro
Site1856-1857Cleavage; by NIa-pro
Site2049-2050Cleavage; by NIa-pro
Active site2095For nuclear inclusion protein A activity
Active site2130For nuclear inclusion protein A activity
Active site2200For nuclear inclusion protein A activity
Site2292-2293Cleavage; by NIa-pro
Site2810-2811Cleavage; by NIa-pro

GO annotations

AspectTerm
Cellular Componenthelical viral capsid
Cellular Componenthost cell cytoplasmic vesicle
Cellular Componenthost cell nucleus
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 Processsymbiont-mediated suppression of host innate immune response
Biological Processviral RNA genome replication
Biological Processviral translational frameshifting
Biological Processvirus-mediated perturbation of host defense response

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    P17766

Proteomes

Subcellular Location

6 kDa protein 1

Note: Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts.

6 kDa protein 2

Note: 6K-induced vesicles associate with host chloroplasts.

Viral genome-linked protein

Host nucleus
Note: Binds to host plant eIF4E proteins in the host nucleus.

Capsid protein

Virion

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000403311-308P1 protease
ChainPRO_00004200071-3125Genome polyprotein
ChainPRO_0000040332309-766Helper component proteinase
ChainPRO_0000040333767-1116Protein P3
ChainPRO_00000403341117-11686 kDa protein 1
ChainPRO_00000403351169-1803Cytoplasmic inclusion protein
ChainPRO_00000403361804-18566 kDa protein 2
ChainPRO_00000403371857-2049Viral genome-linked protein
Modified residue1919O-(5'-phospho-RNA)-tyrosine
ChainPRO_00000403382050-2292Nuclear inclusion protein A
ChainPRO_00000403392293-2810Nuclear inclusion protein B
ChainPRO_00000403402811-3125Capsid protein
Modified residue2876Phosphoserine
Modified residue2896Phosphoserine
Modified residue2913Phosphoserine
Modified residue3049Phosphothreonine
Modified residue3108Phosphothreonine

Post-translational modification

Viral genome-linked protein

VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).

Genome polyprotein

Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).

Keywords

Interaction

Subunit

Viral genome-linked protein

Interacts with host eIF4E protein (via cap-binding region); this interaction mediates the translation of the VPg-viral RNA conjugates (By similarity).
Part of a complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction mediates the translation of the VPg-viral RNA conjugates (By similarity).

Family & Domains

Features

Showing features for domain, motif, compositional bias, region.

TypeIDPosition(s)Description
Domain165-308Peptidase S30
Motif360-363Involved in interaction with stylet and aphid transmission
Motif618-620Involved in virions binding and aphid transmission
Domain644-766Peptidase C6
Domain1240-1392Helicase ATP-binding
Motif1342-1345DECH box
Domain1411-1570Helicase C-terminal
Motif1897-1904Nuclear localization signal
Domain2050-2268Peptidase C4
Domain2534-2658RdRp catalytic
Compositional bias2869-2894Polar residues
Region2869-2897Disordered

Domain

Helper component proteinase

The N-terminus is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.

Sequence similarities

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Ribosomal frameshifting.

P17766-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Genome polyprotein
  • Note
    Produced by conventional translation.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    3,125
  • Mass (Da)
    354,266
  • Last updated
    1990-08-01 v1
  • Checksum
    ED0DD33C439CB712
MSTIVFGSFTCHLDAAIHQDNADRLAKAWTRPENRQVSNAHLLCRRAAESLINTYESATASAWKGLEEKLQPMFAKREFSKTVTKRKGLRCFKESSEKFIEKKLRKQYQEERERLQFLNGPDAIVNQISVDKCEASVRVPSPHIIEKPSFVTPSMKKKVVFKKVRMSEASLQLFMRRVAANAKANGQKVEIIGRKRVVGNYTTKSRLTYFRTHVRHLDGSKPRYDLVLDEATKKILQLFANTSGFHHVHKKGEVTPGMSGFVVNPMNLSDPMQVYDTDLFIVRGKHNSILVDSRCKVSKKQSNEIIHYSDPGKQFSDGFTNSFMQCKLRETDHQCTSDLDVKECGYVAALVCQAIIPCGKITCLQCAQKYSYMSQQEIRDRFSTVIEQHEKTVMDNYPQFSHVLAFLKRYRELMRVENQNYEAFKDITHMIGERKEAPFSHLNKINELIIKGGMMSAQDYIEASDHLRELARYQKNRTENIRSGSIKAFRNKISSKAHVNMQLMCDNQLDTNGNFVWGQREYHAKRFFRNYFDVIDVSEGYRRHIVRENPRGIRKLAIGNLVMSTNLAALRKQLLGEECIHFEVSKECTSKRGENFVYQCCCVTHEDGTPLESEIISPTKNHLVVGNSGDSKYVDLPTAKGGAMFIAKAGYCYINIFLAMLININEDEAKSFTKTVRDTLVPKLGTWPSMMDLATACHFLAVLYPETRNAELPRILVDHEAKIFHVVDSFGSLSTGMHVLKANTINQLISFASDTLDSNMKTYLVGGLEVDKCDEFKNVKLLIRSIYKPQIMEQVLKEEPYLLLMSVLSPGVLMALFNSGSLEKATQYWITRSHSLAAITSMLSALAAKVSLASTLNAQMSVIDEHAAVLYDSVFVGTQPYASYMMAVKTLERMKARTESDHTLNDLGFSVLRQATPHLVEKSYLQELEQAWKELSWSEKFSAILESQRWRKHIPKPFIPKDGADLGGRYDISVRSLLGNQYKRLRDVVRWKRDDVVCYTYQSMGKLFCKAIGISPSFLPSTLKMLDMLIVFSLLLSIGATCNSMVNEHKHLKQLAADREDKKRFKRLQVLYTRLSEKVGCTPTADEFLEYVGDENPDLLKHAEDLIGDGQVVVHQSKRDSQANLERVVAFVALVMMLFDSERSDGVYKILNKLKGIMGSVDRAVHHQSLDDIEDILDEKKLTVDFVLQSNEVAPTVPFDSTFEKWWMNQLETGNVIPHYRTEGHFLEFTRENAAHIANEVMHGSHQDILIRGAVGSGKSTGLPFHLSKKGHVLLIEPTRPLAENVCKQLRGQPFNVNPTLRMRGMSTFGSTPITVMTSGYALHFLANNPTYLDNYKCIIFDECHVHDASAMAFRCLLSEYSYPGKILKVSATPPGHEVEFKTQKEVKVIVEESLSFQQFVSNLGTGCNSDILKHGVNVLVYVASYNEVDTLSKLLTDRSFKVSKVDGRTMKVGNVEIPTSGTQAKPHFVVATNIIENGVTLDIDVVVDFGLKVVPVLDIDNRLVRYTKKSISYGERIQRLGRVGRNKPGAALRIGFTEKGLTQIPPIIATEAAFLCFTYGLPVMTNGVSTSLLAMCTVKQARTMQQFELSPFYTVALVRFDGTMHQEIFRLLKSYRLRDSEVILNKLAIPNSNVCGWMSVRDYKRQGCNLDLDENIRVPFYVKDIPETLHERIWQAVETHKSDAGFGRICSSSACKIAYTLQTDIHSIPRTIKIIDALLEQERTKQAHFRAMTSQSCSSSNFSLSSITSAIRSKYAKDHTEENIGVLQMAKSQLLEFKNLNIDPSYPELIRNFGALECVHHQTKEGVSKALQLKGHWNKRLITRDATLMLGVLGGGAWMIFSYLRDSFKEEVIHQGFNRRQRQKLKFRQARDNRMAREVYGDDSTMEAYFGSAYSKKGKSKGKTRGMGTKTRKFVNMYGYDPTDYNFVRFVDPLTGHTLDESPLMDINLVQEHFSQIRNDYIGDDKITMQHIMSNPGIVAYYIKDATQKALKVDLTPHNPLRVCDKTATIAGFPEREFELRQTGHPVFVEPNAIPKINEEGDEEVDHESKSLFRGLRDYNPIASSICQLNNSSGARQSEMFGLGFGGLIVTNQHLFKRNDGELTIRSHHGEFVVKDTKTLKLLPCKGRDIVIIRLPKDFPPFPRRLQFRTPTTEDRVCLIGSNFQTKSISSTMSETSATYPVDNSHFWKHWISTKDGHCGLPIVSTRDGSILGLHSLANSTNTQNFYAAFPDNFETTYLSNQDNDNWIKQWRYNPDEVCWGSLQLKRDIPQSPFTICKLLTDLDGEFVYTQSKTTHWLRDRLEGNLKAVGACPGQLVTKHVVKGKCTLFETYLLTHPEEHEFFRPLMGAYQKSALNKDAYVKDLMKYSKPIVVGAVDCDQFERAVDVVISMLISKGFEECNYVTDPDDIFSALNMKAAVGALYSGKKRDYFENVSDQDKESFVRASCKRLFMGKKGVWNGSLKAELRPKEKVEANKTRSFTAAPIDTLLGGKVCVDDFNNQFYSLNLHCPWSVGMTKFRGGWDKLLKALPEGWIYCDADGSQFDSSLSPYLINAVLNIRLAFMEEWDIGEQMLSNLYTEIVYTPIATPDGTIVKKFKGNNSGQPSTVVDNTLMVILAMTYSLLKLGHHPDTHDCICRYFVNGDDLVLAVHPAYESIYDELQEHFSQLGLNYTFTTKTENKEELWFMSHKGVLYDDMYIPKLEPERIVSILEWDRSNEPIHRLEAICASMVEAWGYKELLREIRKFYSWVLEQAPYNALSKDGKAPYIAETALKKLYTDTEASETEIERYLEAFYDNINDDGESNVVVHQADEREDEEEVDALQPPPVIQPAPRTTAPMLNPIFTPATTQPATKPVSQVSGPQLQTFGTYSHEDASPSNSNALVNTNRDRDVDAGSTGTFTVPRLKAMTSKLSLPKVKGKAIMNLNHLAHYSPAQVDLSNTRAPQSCFQTWYEGVKRDYDVTDDEMSIILNGLMVWCIENGTSPNINGMWVMMDGETQVEYPIKPLLDHAKPTFRQIMAHFSNVAEAYIEKRNYEKAYMPRYGIQRNLTDYSLARYAFDFYEMTSTTPVRAREAHIQMKAAALRNVQNRLFGLDGNVGTQEEDTERHTAGDVNRNMHNLLGMRGV

P0CK02-1

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    P3N-PIPO polyprotein
  • See also
    sequence in UniParc or sequence clusters in UniRef

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias2869-2894Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D13751
EMBL· GenBank· DDBJ
BAA02898.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

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