G3XEW3 · G3XEW3_9VIRU

  • Protein
    RNA-directed RNA polymerase L
  • Gene
    L
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: For polymerase activity.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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.

TypeIDPosition(s)Description
Binding site51Mn2+ 1 (UniProtKB | ChEBI)
Binding site89Mn2+ 1 (UniProtKB | ChEBI)
Binding site89Mn2+ 2 (UniProtKB | ChEBI)
Binding site102Mn2+ 1 (UniProtKB | ChEBI)
Active site115
Binding site1329Mg2+ (UniProtKB | ChEBI); catalytic; for RdRp activity

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasm
Cellular Componentvirion component
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
Molecular FunctionRNA-dependent RNA polymerase activity
Biological Processcap snatching
Biological Processnegative stranded viral RNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RNA-directed RNA polymerase L
  • EC number
  • Short names
    Protein L
  • Alternative names
    • Large structural protein
    • Replicase
    • Transcriptase

Including 1 domain:

  • Recommended name
    cap-snatching endonuclease
  • EC number

Gene names

    • Name
      L

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NMW-1
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Arenaviridae > Mammarenavirus

Accessions

  • Primary accession
    G3XEW3

Proteomes

Subcellular Location

Keywords

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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1172-1367RdRp catalytic

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 status
    Complete
  • Length
    2,215
  • Mass (Da)
    253,000
  • Last updated
    2011-12-14 v1
  • Checksum
    DA9ED2597F7D1277
MEASVSEAKDLISKYLANDQRLSRQKLNFLIQSEPQNLLIEGLKLLSLCIELDSCEANGCEHNTDELSVEVILLNRGILSPGLPFVVPDGFKLTGNVLVLLECFVRSSPSNFEQKYNEDTVKLNSLKQDLQGVGVTLLPIIDGRTVFDHTFMPEWANEKFRSILFSLLQFAQESSRMLEESEYSRLCESLRNIEGKRSGIESINILQDCRAKHHEEILKLCHMGIDNSMSSIDVKREIINEFQAFRNGISSGTIPRQFRRVDKSEMLESFCKMYPSDYGVEAEDVEKLREEFFVLSPTITILYAKIDSIEELRTKHSCVPAWRSLLNKIKSLHILNTRRKTLLLFDSIILLCHATDKEVVGHFEESEWLGSSFLSVNDRLVSLTATKKELRQWIERRRMNQAKKLSSRCEDQELVYYNLVNSTLKKAEQALAVVGLKFSDYGVLENIISVSSFKKIMGVEVDGVMPSINYEKNDLNDFPYDLSPELETEDDLKRLSSISLAIVNSMKTSSVVKLRQNERGSGRFKKVICKEAYCQEFYMAGTRFRLLYQKTGECSKCYAINNSRKGEVCSFYADPKRFFPAIFSQSVISETIKVMVSWLNDCLELKQDLKDIEALLKMVFILILTHPSKRSQKFLQNLRYFIMAYVSEYYHKDLLSKLEEKLITKVEFFLFRVLRTLLCKVLNPSINTMLTNRFKFILNVSYICHFITKETPDRLTDQIKCFEKYLEPKLEFDSVNVNPFESAEATELSSLLMSGATFLGKPLCSDAGDIQFKRPGVSKKILSLVTSSFNNGVLFSKQEFKGEIKDPLVLSGCATAMDLASNKSVVINKYVDGERVLNYDYDKLVAAAVCQLSETFERKSKYFLSKEEYDYKIMKVIASLVIGSKNASGGGMPTEELDEILVNGTASSYLEDIKDSVRAVIEGYKNLGNEKLNKENTGDINDLHKIVDNTMHLKLILSELSNHLIEDFDQSLLSDDDYKVICDKVHSNSELKSKYFYSGPMDSCAISEITRAVTTRTYKNAEYFLCFKSILLQMNANRLVGKYSHYKSKCINFKLNRERLMDDCRLSDRESNSEALSKALSLTNCTTAVLKNLCFYSQESPQSYTSIGPDTGRLKFSLSYKEQVGGNRELYIGDLRTKMFTRLIEDYFESLTNQFRGSCLNSESEFENAVLSMKLNVSLAQVCYSLDHSKWGPMMNPLLFLVVLQNIHWSSSDVLEDVKSRDYVSTLLSWHIHKLIEVPHPVVNAMMRSYLKTNLGLKKSLHETLTEAFFFRHFKLGVVPSHISSILDMGQGILHNASDFYGLITEKFINYSIGLLYEGTLKSYTSSDDQISLFDHKLTNLLDRDPDEFEYILEFHNYLSDRLNKFISPKSVIGRFVAEFKSRFYVWGDEVPLLTKFVAAALHNVKCKEPHQLAETIDTIIDQSVANGVPVKLCNLIQQRTLDLLRYAQYPIDPFLMFCDSDVKDWVDGNRGYRIMRNIELICPGGTKKIRYLLRRLYNKLKTGELHEEFTAAYLSGDPSESLQRICSLLDVDPLEESELSLCWLNLSAYFPLRMVLRQKVVYTGALNLEEEKLPTLVKTLQNKLSSNFTRGAQKLLSEAINKSAFQSSIASGFVGLCRTLGSKCVRGPNKFNYYIKSLVSQLEGRVDVKGFVQKGMNLWSVPSDQRCSNDWLVKFLRPVLWDYMCIALSCALEIGPWVLGEPKLKARVSAINFKPCDYFPLKPTITKLLEDKVGFNHIIHSFRRLYPSLFERHLLPFMSDLASTKMKWSPRVKFLDLCVVLDVNCEAMSLISHVVKWKREEHYIVLSSELSEAHDRSHVSLVEERVVSTEDVAKNFLRQVYFESFIRPFVATSRTLGSFTWFPHRTSLPASEGLSLLGPFASFVEKVIYKGVERPMFKSDLYMGFSWMDMVIKPAFLNMNQLAASGLNHDQQFTSLDEFWEALQLLPKGSIQLTFSVYFTIKSKGETLSEEFAFHVETWGVINHTGSFVPSRLEVLYSGQVHRSLLLDCWRLVLNSDQFCKLKPVWTVDTDNLSEFLEDPKSVGQIVRLNVELSENIADLTEHDFVHIGPDVEPVPLVLENGYLVEGRKRIIPINPSIHDQDIEVLISEMDGSCVSSPPIVIGSILGQRLDQGLHWLELDLVGVVKKCIPNDYKAFLKEALQNVCEWLGFKGYSLCFSKTLGEIMVHSSQGKYRLKGRQCDRLFEEAEEIQDID

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB586647
EMBL· GenBank· DDBJ
BAL03418.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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