Reviewed,
UniProtKB/Swiss-Prot P22602 (POLG_PVYO)
Last modified
November 25, 2008.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Genome polyprotein Cleaved into the following 3 chains: 1- Recommended name: P1 proteinase Alternative name(s): N-terminal protein 2- Recommended name: Helper component proteinase Short name=HC-pro EC=3.4.22.45 3- Recommended name: Protein P3 |
| Organism | Potato virus Y (strain O) (PVY) |
| Taxonomic identifier | 12220 [NCBI] |
| Taxonomic lineage | Viruses › ssRNA positive-strand viruses, no DNA stage › Potyviridae › Potyvirus |
| Virus host | Capsicum (peppers) [TaxID: 4071] Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081] Nicotiana [TaxID: 4085] Solanum tuberosum (Potato) [TaxID: 4113] |
Protein attributes
| Sequence length | 856 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Helper component proteinase is required for aphid transmission and also has proteolytic activity. Interacts with virions and aphid stylets. Seems to act as suppressor of 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. |
| Domain | 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. |
| Post-translational modification | The viral RNA of potyviruses is expressed as a single polyprotein which 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 By similarity. |
| Sequence similarities | Belongs to the potyviruses polyprotein family. Contains 1 peptidase C6 domain. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Hydrolase Protease Thiol protease |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Molecular function | cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 284 | 284 | P1 proteinase Potential | PRO_0000040420 | |||||
| Chain | 285 – 740 | 456 | Helper component proteinase Potential | PRO_0000040421 | |||||
| Chain | 741 – ›856 | ›116 | Protein P3 | PRO_0000040422 | |||||
Regions | |||||||||
| Motif | 334 – 337 | 4 | Involved in interaction with stylet and aphid transmission By similarity | ||||||
| Motif | 592 – 594 | 3 | Involved in virions binding and aphid transmission By similarity | ||||||
Sites | |||||||||
| Active site | 192 | 1 | For P1 proteinase activity By similarity | ||||||
| Active site | 201 | 1 | For P1 proteinase activity Potential | ||||||
| Active site | 235 | 1 | For P1 proteinase activity By similarity | ||||||
| Active site | 626 | 1 | For helper component proteinase activity By similarity | ||||||
| Active site | 699 | 1 | For helper component proteinase activity By similarity | ||||||
| Site | 284 – 285 | 2 | Cleavage; by P1 proteinase Potential | ||||||
| Site | 740 – 741 | 2 | Cleavage; by HC-pro Potential | ||||||
Experimental info | |||||||||
| Non-terminal residue | 856 | 1 | |||||||
Sequences
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References
| [1] | "Comparative sequence of the helper component (HC) region of potato virus Y and a HC-defective strain, potato virus C." Thornbury D.W., Patterson C.A., Dessens J.T., Pirone T.P. Virology 178:573-578(1990) [PubMed: 2219708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | "Potyvirus proteins: a wealth of functions." Urcuqui-Inchima S., Haenni A.L., Bernardi F. Virus Res. 74:157-175(2001) [PubMed: 11226583] [Abstract] Cited for: REVIEW. |
Cross-references
Sequence databases | |
|---|---|
| M37180 Genomic RNA. Translation: AAA47184.1. | |
| PIR | A46341. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C06.001. |
Family and domain databases | |
| InterPro | IPR002540. Pept_S30_P1_potyvir. IPR001456. Peptidase_C6. [Graphical view] |
| Pfam | PF00851. Peptidase_C6. 1 hit. PF01577. Peptidase_S30. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | POLG_PVYO | ||||||||
| Accession | Primary (citable) accession number: P22602 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


