G3XEW3 · G3XEW3_9VIRU
- ProteinRNA-directed RNA polymerase L
- GeneL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2215 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.
Miscellaneous
Classified as His- endonuclease since it does not have a histidine upstream of the active site that coordinates the first cation. His- endonucleases display very low activity in vitro, although they are clearly active in vivo.
Catalytic activity
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: For polymerase activity.
Note: For endonuclease activity. Binds 2 Mn2+ ions in the active site. The divalent metal ions are crucial for catalytic activity.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 51 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 89 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 89 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 102 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 115 | |||||
Sequence: K | ||||||
Binding site | 1329 | Mg2+ (UniProtKB | ChEBI); catalytic; for RdRp activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Cellular Component | virion component | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | cap snatching | |
Biological Process | negative stranded viral RNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-directed RNA polymerase L
- EC number
- Short namesProtein L
- Alternative names
Including 1 domain:
- Recommended namecap-snatching endonuclease
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Arenaviridae > Mammarenavirus
Accessions
- Primary accessionG3XEW3
Proteomes
Subcellular Location
Interaction
Subunit
Homomultimer; the oligomeric structure is essential for the polymerase activity. Interacts with nucleoprotein N. Interacts with protein Z; this interaction inhibits viral transcription and replication.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1172-1367 | RdRp catalytic | ||||
Sequence: SMKLNVSLAQVCYSLDHSKWGPMMNPLLFLVVLQNIHWSSSDVLEDVKSRDYVSTLLSWHIHKLIEVPHPVVNAMMRSYLKTNLGLKKSLHETLTEAFFFRHFKLGVVPSHISSILDMGQGILHNASDFYGLITEKFINYSIGLLYEGTLKSYTSSDDQISLFDHKLTNLLDRDPDEFEYILEFHNYLSDRLNKFI |
Domain
The N-terminus contains the endonuclease activity (endoN). The central region contains the RdRp activity.
Sequence similarities
Belongs to the Bunyavirales RNA polymerase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,215
- Mass (Da)253,000
- Last updated2011-12-14 v1
- ChecksumDA9ED2597F7D1277