P09814 (POLG_TVMV) Reviewed, UniProtKB/Swiss-Prot
Last modified May 29, 2013. Version 121. History...
Names and origin
|Protein names||Recommended name:|
Cleaved into the following 10 chains:
|Organism||Tobacco vein mottling virus (TVMV) [Complete proteome]|
|Taxonomic identifier||12228 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Potyviridae › Potyvirus|
|Virus host||Nicotiana tabacum (Common tobacco) [TaxID: 4097]|
Rumex [TaxID: 3618]
|Sequence length||3023 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.
Nuclear inclusion protein B: a RNA-dependent RNA polymerase that plays an essential role in the virus replication.
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 By similarity.
Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.
Both 6K peptides are indispensable for virus replication By similarity.
Nuclear inclusion protein A: has RNA-binding and proteolytic activities.
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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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.
The N-terminus of helper component proteinase 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.
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.
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.
Belongs to the potyviridae genome polyprotein family.
Contains 1 helicase ATP-binding domain.
Contains 1 helicase C-terminal domain.
Contains 1 peptidase C4 domain.
Contains 1 peptidase C6 domain.
Contains 1 peptidase S30 domain.
Contains 1 RdRp catalytic domain.
|This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]|
|Isoform Genome polyprotein (identifier: P09814-1) |
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.
|Note: Produced by conventional translation.|
|Isoform P3N-PIPO polyprotein (identifier: P0CK10-1) |
The sequence of this isoform can be found in the external entry P0CK10.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
|Note: Produced by -1 ribosomal frameshifting in P3 ORF.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 3023||3023||Genome polyprotein||PRO_0000420031|
|Chain||1 – 274||274||P1 proteinase Potential||PRO_0000040483|
|Chain||275 – 731||457||Helper component proteinase Potential||PRO_0000040484|
|Chain||732 – 1078||347||Protein P3 By similarity||PRO_0000040485|
|Chain||1079 – 1130||52||6 kDa protein 1 By similarity||PRO_0000040486|
|Chain||1131 – 1765||635||Cytoplasmic inclusion protein By similarity||PRO_0000040487|
|Chain||1766 – 1818||53||6 kDa protein 2 By similarity||PRO_0000040488|
|Chain||1819 – 2001||183||Viral genome-linked protein By similarity||PRO_0000040489|
|Chain||2002 – 2242||241||Nuclear inclusion protein A By similarity||PRO_0000040490|
|Chain||2243 – 2758||516||Nuclear inclusion protein B By similarity||PRO_0000040491|
|Chain||2759 – 3023||265||Capsid protein By similarity||PRO_0000040492|
|Domain||1202 – 1354||153||Helicase ATP-binding|
|Domain||1367 – 1532||166||Helicase C-terminal|
|Domain||2002 – 2218||217||Peptidase C4|
|Domain||2484 – 2608||125||RdRp catalytic|
|Nucleotide binding||1215 – 1222||8||ATP Potential|
|Motif||325 – 328||4||Involved in interaction with stylet and aphid transmission By similarity|
|Motif||583 – 585||3||Involved in virions binding and aphid transmission By similarity|
|Motif||1304 – 1307||4||DEFH box|
|Motif||1856 – 1863||8||Nuclear localization signal Potential|
|Active site||183||1||For P1 proteinase activity By similarity|
|Active site||192||1||For P1 proteinase activity Potential|
|Active site||225||1||For P1 proteinase activity By similarity|
|Active site||617||1||For helper component proteinase activity By similarity|
|Active site||690||1||For helper component proteinase activity By similarity|
|Active site||2047||1||For nuclear inclusion protein A activity By similarity|
|Active site||2082||1||For nuclear inclusion protein A activity By similarity|
|Active site||2152||1||For nuclear inclusion protein A activity By similarity|
|Site||274 – 275||2||Cleavage; by P1 proteinase Potential|
|Site||731 – 732||2||Cleavage; by HC-pro Potential|
|Site||1078 – 1079||2||Cleavage; by NIa-pro By similarity|
|Site||1130 – 1131||2||Cleavage; by NIa-pro By similarity|
|Site||1765 – 1766||2||Cleavage; by NIa-pro By similarity|
|Site||1818 – 1819||2||Cleavage; by NIa-pro By similarity|
|Site||2001 – 2002||2||Cleavage; by NIa-pro By similarity|
|Site||2242 – 2243||2||Cleavage; by NIa-pro By similarity|
|Site||2758 – 2759||2||Cleavage; by NIa-pro By similarity|
Amino acid modifications
|||"The nucleotide sequence of tobacco vein mottling virus RNA."|
Domier L.L., Franklin K.M., Shahabuddin M., Hellmann G.M., Overmeyer J.H., Hiremath S.T., Siaw M.F.E., Lomonossoff G.P., Shaw J.G., Rhoads R.E.
Nucleic Acids Res. 14:5417-5430(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
|||"A tyrosine residue in the small nuclear inclusion protein of tobacco vein mottling virus links the VPg to the viral RNA."|
Murphy J.F., Rychlik W., Rhoads R.E., Hunt A.G., Shaw J.G.
J. Virol. 65:511-513(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1874-1888, COVALENT RNA-LINKAGE OF VPG, URIDYLYLATION AT TYR-1878.
|||"Potyvirus proteins: a wealth of functions."|
Urcuqui-Inchima S., Haenni A.L., Bernardi F.
Virus Res. 74:157-175(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
|X04083 Genomic RNA. Translation: CAA27720.1.|
|PIR||GNVSTV. A23647. |
|RefSeq||NP_056867.1. NC_001768.1. |
3D structure databases
|SMR||P09814. Positions 2010-2221. |
Protein family/group databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|InterPro||IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. |
|Pfam||PF00270. DEAD. 1 hit. |
PF00271. Helicase_C. 1 hit.
PF00863. Peptidase_C4. 1 hit.
PF00851. Peptidase_C6. 1 hit.
PF01577. Peptidase_S30. 1 hit.
PF00767. Poty_coat. 1 hit.
PF08440. Poty_PP. 1 hit.
PF00680. RdRP_1. 1 hit.
|PRINTS||PR00966. NIAPOTYPTASE. |
|SMART||SM00487. DEXDc. 1 hit. |
SM00490. HELICc. 1 hit.
|SUPFAM||SSF50494. Pept_Ser_Cys. 1 hit. |
SSF52540. SSF52540. 2 hits.
|PROSITE||PS51192. HELICASE_ATP_BIND_1. 1 hit. |
PS51194. HELICASE_CTER. 1 hit.
PS51436. POTYVIRUS_NIA_PRO. 1 hit.
PS51195. Q_MOTIF. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
|Accession||Primary (citable) accession number: P09814|
Secondary accession number(s): Q84898 Q84902
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|