H9E9D0 · H9E9D0_HEV
- ProteinNon-structural polyprotein pORF1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1708 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m7GTP or m7GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m7GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure.
NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities. Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs. Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure. Participates also in viral genome replication, RNA translocation and genome packaging/unpackaging.
RNA-directed RNA polymerase: Plays an essential role in the virus replication. Binds to the 3'-end of the genomic RNA to initiate viral replication.
Y-domain: Indispensable for virus replication.
Catalytic activity
- GTP + S-adenosyl-L-methionine = N7-methyl-GTP + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-type peptidase activity | |
Molecular Function | helicase activity | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA methyltransferase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | DNA-templated transcription | |
Biological Process | mRNA modification | |
Biological Process | proteolysis | |
Biological Process | RNA processing | |
Biological Process | viral protein processing | |
Biological Process | viral RNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNon-structural polyprotein pORF1
- EC number
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Hepelivirales > Hepeviridae > Orthohepevirinae > Paslahepevirus
- Virus hosts
Accessions
- Primary accessionH9E9D0
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
The protease domain interacts with host EIF2AK4 (via C-terminus); this interaction inhibits dimerization of EIF2AK4 and prevents EIF2AK4-mediated phosphorylation of host EIF2A.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 56-240 | Alphavirus-like MT | |||
Region | 712-754 | Disordered | |||
Compositional bias | 728-742 | Pro residues | |||
Domain | 790-936 | Macro | |||
Domain | 949-1231 | +RNA virus helicase C-terminal | |||
Domain | 1469-1580 | RdRp catalytic | |||
Sequence similarities
Belongs to the hepevirus non-structural polyprotein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,708
- Mass (Da)187,196
- Last updated2012-05-16 v1
- Checksum720E069E8316A699
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 728-742 | Pro residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JQ679014 EMBL· GenBank· DDBJ | AFD33686.1 EMBL· GenBank· DDBJ | Genomic RNA |