B1NKT1 · VP3_ROTHP
- ProteinProtein VP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids835 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not.
Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'-oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated.
Catalytic activity
- a 5'-end diphospho-ribonucleoside in mRNA + GTP + H+ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate
- 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 H2O = 2 AMP + ATP + 2 H+
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 718 | For 2'-5'-phosphodiesterase activity | ||||
Sequence: H | ||||||
Active site | 720 | For 2'-5'-phosphodiesterase activity | ||||
Sequence: T | ||||||
Active site | 797 | For 2'-5'-phosphodiesterase activity | ||||
Sequence: H | ||||||
Active site | 799 | For 2'-5'-phosphodiesterase activity | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | viral nucleocapsid | |
Molecular Function | GTP binding | |
Molecular Function | mRNA 5'-cap (guanine-N7-)-methyltransferase activity | |
Molecular Function | mRNA guanylyltransferase activity | |
Molecular Function | oligoribonucleotidase activity | |
Molecular Function | RNA binding | |
Biological Process | defense response to virus | |
Biological Process | symbiont-mediated suppression of host innate immune response | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein VP3
Including 3 domains:
- Recommended name2',5'-phosphodiesterase
- EC number
- Recommended namemRNA guanylyltransferase
- EC number
- Recommended namemRNA (guanine-N(7))-methyltransferase
- EC number
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A
- Virus hosts
Accessions
- Primary accessionB1NKT1
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000368086 | 1-835 | Protein VP3 | |||
Sequence: MKVLALRHSVAQVYADTQTYLHDDSKDEYENAFLISNLTTHNILYLNYSLKTLKILNKSGIAAVEVQSPDELFALIRCNFTYDYENNIIYLHDYSYYTNNEIRTDQHWITKTDIIDYLLPGWKLTYVGYNGKNTRGHYNFSFSCQNAATDDDIIIEYIYSNELDFQNFLLRKIKERMTTSLPIARLSNRVFRDKLFPSIVNIYKKVINVGPRNESMFTFLNFPTIKQFSNGAYIVKHTIKLKQEKWLGKRVSQFDIGQYKNMLNVVTTIYYYYNLYHSKPIIYMLGSAPSYWIHDIKQYSDFTFETWDPLDTPYSTIHHKELFFDKDVNKLKDNSVLYIDIRTDRKNMDWKEWRKVVEQQTVNNLNIAYKYLSTGKAKVCCVKLTAMDLELPITAKLLHHPTTEVRSEFYAILDAWDIITIKRFIPKGVFYAFINNITTENVFIQPPFKLKASPTDYIVALYALSNDFNSRQDVINLINKQKQSLITVRMNNTFKDEPKVNFKNIYDWTFLPTDFELKDSIITSYDGCLGMFGLSISLSSKPTGNNHLFIINGTDKYYKLDQYANHMGISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYAFDLKRWIYLHSIGKVTVEGGRYYEHAPIELIYACRSAKEFAILQDDLTVLRYANEIEGYINKVYSITYADDPNYFIGIKFNSIPYEYDVKVPHLTLGVLFISDNMIHDVVTVLKKMKTELFKTEISTSYTYMLSDNIYVANASGVLSTYFKLYNMFYRNHITFGQSRMFIPHITLSFSNKQTVRIESTRLKINSIYLRKIKGETVFDMSE |
Interaction
Subunit
Interacts with VP1. Interacts with VP2.
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 171-245 | N7-methyltransferase activity | ||||
Sequence: RKIKERMTTSLPIARLSNRVFRDKLFPSIVNIYKKVINVGPRNESMFTFLNFPTIKQFSNGAYIVKHTIKLKQEK | ||||||
Region | 246-428 | 2'-O-methyltransferase activity | ||||
Sequence: WLGKRVSQFDIGQYKNMLNVVTTIYYYYNLYHSKPIIYMLGSAPSYWIHDIKQYSDFTFETWDPLDTPYSTIHHKELFFDKDVNKLKDNSVLYIDIRTDRKNMDWKEWRKVVEQQTVNNLNIAYKYLSTGKAKVCCVKLTAMDLELPITAKLLHHPTTEVRSEFYAILDAWDIITIKRFIPKG | ||||||
Region | 429-555 | N7-methyltransferase activity | ||||
Sequence: VFYAFINNITTENVFIQPPFKLKASPTDYIVALYALSNDFNSRQDVINLINKQKQSLITVRMNNTFKDEPKVNFKNIYDWTFLPTDFELKDSIITSYDGCLGMFGLSISLSSKPTGNNHLFIINGTD | ||||||
Region | 556-692 | GTase/RTPase activity | ||||
Sequence: KYYKLDQYANHMGISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYAFDLKRWIYLHSIGKVTVEGGRYYEHAPIELIYACRSAKEFAILQDDLTVLRYANEIEGYINKVYSIT | ||||||
Region | 693-835 | 2'-5'-phosphodiesterase activity | ||||
Sequence: YADDPNYFIGIKFNSIPYEYDVKVPHLTLGVLFISDNMIHDVVTVLKKMKTELFKTEISTSYTYMLSDNIYVANASGVLSTYFKLYNMFYRNHITFGQSRMFIPHITLSFSNKQTVRIESTRLKINSIYLRKIKGETVFDMSE |
Domain
Contains a bipartite N7-methyltransferase domain, a 2'-O-methyltransferase domain and a GTase/RTPase domain. The C-terminus contains a phosphodiesterase domain that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell in response to IFN stimulation.
Sequence similarities
Belongs to the rotavirus VP3 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length835
- Mass (Da)97,856
- Last updated2008-04-29 v1
- Checksum134FE1363B1F05ED
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 294 | in Ref. 2; ABB18255 | ||||
Sequence: H → Y |