Q6XW15 (POLG_BTMV) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 72. History...
Names and origin
|Sequence length||3085 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
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 By similarity.
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 By similarity.
Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten 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: Q6XW15-1) |
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: P0CJ96-1) |
The sequence of this isoform can be found in the external entry P0CJ96.
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 – 3085||3085||Genome polyprotein||PRO_0000419994|
|Chain||1 – 313||313||P1 proteinase Potential||PRO_0000040246|
|Chain||314 – 770||457||Helper component proteinase Potential||PRO_0000040247|
|Chain||771 – 1117||347||Protein P3 Potential||PRO_0000040248|
|Chain||1118 – 1169||52||6 kDa protein 1 By similarity||PRO_0000040249|
|Chain||1170 – 1803||634||Cytoplasmic inclusion protein By similarity||PRO_0000040250|
|Chain||1804 – 1855||52||6 kDa protein 2 By similarity||PRO_0000040251|
|Chain||1856 – 2046||191||Viral genome-linked protein By similarity||PRO_0000040252|
|Chain||2047 – 2293||247||Nuclear inclusion protein A By similarity||PRO_0000040253|
|Chain||2294 – 2809||516||Nuclear inclusion protein B By similarity||PRO_0000040254|
|Chain||2810 – 3085||276||Capsid protein||PRO_0000040255|
|Domain||1241 – 1393||153||Helicase ATP-binding|
|Domain||1412 – 1571||160||Helicase C-terminal|
|Domain||2047 – 2266||220||Peptidase C4|
|Domain||2535 – 2659||125||RdRp catalytic|
|Nucleotide binding||1254 – 1261||8||ATP Potential|
|Motif||365 – 368||4||Involved in interaction with stylet and aphid transmission By similarity|
|Motif||622 – 624||3||Involved in virions binding and aphid transmission By similarity|
|Motif||1343 – 1346||4||DESH box|
|Motif||1895 – 1904||10||Nuclear localization signal Potential|
|Active site||656||1||For helper component proteinase activity By similarity|
|Active site||729||1||For helper component proteinase activity By similarity|
|Active site||2092||1||For nuclear inclusion protein A activity By similarity|
|Active site||2127||1||For nuclear inclusion protein A activity By similarity|
|Active site||2198||1||For nuclear inclusion protein A activity By similarity|
|Site||313 – 314||2||Cleavage; by P1 proteinase Potential|
|Site||770 – 771||2||Cleavage; by HC-pro Potential|
|Site||1117 – 1118||2||Cleavage; by NIa-pro By similarity|
|Site||1169 – 1170||2||Cleavage; by NIa-pro By similarity|
|Site||1803 – 1804||2||Cleavage; by NIa-pro By similarity|
|Site||1855 – 1856||2||Cleavage; by NIa-pro By similarity|
|Site||2046 – 2047||2||Cleavage; by NIa-pro By similarity|
|Site||2293 – 2294||2||Cleavage; by NIa-pro By similarity|
|Site||2809 – 2810||2||Cleavage; by NIa-pro By similarity|
Amino acid modifications
|Modified residue||1919||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|||"The complete nucleotide sequence, genome organization, and specific detection of beet mosaic virus."|
Nemchinov L.G., Hammond J., Jordan R., Hammond R.W.
Arch. Virol. 149:1201-1214(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"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.
|AY206394 Genomic RNA. Translation: AAP41071.1.|
|RefSeq||NP_954611.1. NC_005304.1. |
3D structure databases
|SMR||Q6XW15. Positions 2055-2269. |
Protocols and materials 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. |
|PROSITE||PS51192. HELICASE_ATP_BIND_1. 1 hit. |
PS51194. HELICASE_CTER. 1 hit.
PS51436. POTYVIRUS_NIA_PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
|Accession||Primary (citable) accession number: Q6XW15|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|