A0A2P1JNT3 · A0A2P1JNT3_LASV

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+ 2 (UniProtKB | ChEBI)
Binding site89Mn2+ 1 (UniProtKB | ChEBI)
Binding site102Mn2+ 1 (UniProtKB | ChEBI)
Active site115
Binding site1334Mg2+ (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

Accessions

  • Primary accession
    A0A2P1JNT3

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
Domain1177-1372RdRp 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
    2,220
  • Mass (Da)
    253,956
  • Last updated
    2018-05-23 v1
  • Checksum
    1F9C8990C036F77D
MEEDIANAKDLISKYLADNEKLSRQKLAFLVQTEPRMLLMEGLKLLSLCIEIDSCKANGCEHNTEDKTVESILSDHGILTPALCFVVPDGYKLTGNVLILLECFVRSSPANFEQKYLEDHKKLEQLKNDLESVGINLIPLIDGRTTFYNEQIPDWVNDKLRDTLFTLLKYSQESNALFEESEYSRLCESLALTSGRLSGIESINVLTDKRAKHFEEIISSCHQGINNKLTSHEVKSLIEEEYQIFRNKLRQGDIENQFVRTDKVRLLEDFKKLYSDKIDTCDDSIEQLTFQFRRASPVLKFLYADLDSGEERAADSQSEQMQCWRSFLNKIKSLRILNTRRKLLLIFDVLILLASRLDRIKHGDGLLAGWLGSCFVSVNDRLVSLESTKRDLKRWIDSRKRTRDRNVGVLSPKEERNCELLAIINRVLTRATNALREVGIETNSYGIDFKILDCDVYDAIMDIEITGITPTISYQKTQEDMFPYTLGVIDILDATDLERLSSLSLALINSMKTSSTVKLRQNEFGPSRYQVVRCKEAYCQEFFINRMGFKLLYQKTGECSKCYAINNNITGEVCSFYADPKRFFPSVFSSDVLQKVVDVMVSWIEECTELSEQLITIKLLTKMILVLILTHPSKRCQKFLQNIRYFVMAFVSDFYHKDLIEKIREDLITEVEYLLYRLVRHLLKIILSEEVVSMMTNRFKFVLNVSYMCHFITKETPDRLTDQIKCFEKFLEPKLEFGHVSVNPKDDASEEELAEMVHNARRFLSKECCADAEKIRYKKPGVSKKFISLLVSSFNNGSLFKEKEVKRTLRDPLITSGCATALDLASNKSVVVNKYTDGSRILDYDFNKLTALAVTQLTEVFARKGKFLLNKQDYDYKIQQAMSNLVLGSKGGSGDTNNADLDEILLDGGASEYFDQLRCTVDNIVSQYREQPERQQQADCNAPSISDLDKVVEEKLLIRLIKSELSNHMIEDFDREILSEDQYIKICENIYNDADLRSKYFYVGPMNSCPISELTKAVVTRTFLDQEYFQCFKSILLVMNGNKLMGRYSHYKSKCLNFKFDTGRLAEDVRISERESNSEALSKALSLTNCTTAMLKNLCFYSQESPQSYNSTGPDTGRLKFSLSYKEQVGGNRELYIGDLRTKMFTRLIEDYFEALTSQLAGSCLNNEKEFDNAILSMKLNVSSAHVSYSMDHSKWGPMMCPFLFLTIIQNLILLSDDLQADLKGKDYLSTLLTWHMHKMVEIPFNVVSAMMKSYIKSQLGLKKKTTQSVTEDFFNSNFQIGTVPSHISSILDMGQGILHNTSDFYALISERFINFAVRCVSGGQIDAYTSSDDQISLFDQNLTELLSRDAEEFKTLLEFHYYMSDQLNKFVSPKSAIGRFVAEFKSRFYVWGDEVPLLTKFVAAALHNIKCKEPHQLAETIDTIIDQSVANGVPVDLCNQIQKRTLSLLCYAKYPIDPFLLNCETDVRDWVDGNRSYRIMRQIERLIPDACKKMRSMLRILFNKLKTGELHEEFTTNYLSGEHTTSLQNLFKLLGIEPLSDSDLGYHWLNLATHHPLRMVLRQKIIYSGAVNLEDEKVPTIVKTLQNRLSSTFTRGAQKLLSEAINKSAFQSSIASGFVGLCRTLGSKCVRGPNKENLYIRSIQTQLLGTQGVEVVMGDNGIQIWKVSPEVKDGGDTVVTYLRPLLWDYMCITLSTAIELGAWVLGEPKQAQILDFFKHNPCDYFPLRPTVSKLLEDRVGMSHIIHSLRRLYPSLFEKHILPFMSDLASTKMKWSPRIKFLDLCVALDVNCEALSLVSHIVKWKREEHYVVLASELRNSHSRTHEPMMEERVVSTTDAVDNFMRQIYFESYVRSFVATTRTLGSFTWFPHKTSIPEGEGLQRLGPFSSFIEKAIYKGIERPMFKFDLMMGYAWIDFDIEPAQINLNQLIASGLTEELRLDSLEDFFDLLSTMPMDSVQFYQTIRYKIKSQDASFKETFSIHLNMIGLVNQCGEFVVNDVQALYSGSVSPCVLSDCWRLALSGPTFKGRSAWFVESDVVNEFLKDTQQLGDVIPMKLIINPDKLQFSEFDFTKVGPDNEPVPLVVCRGALWESDRRVATFSPSIQDQDLEMFVREIGDGSPHLLVGALKSMMSDRLKQRIQWTGVDIVSILTKQRPLDYADILSELLESLGEWIDFKGYALCYSKSKQKVMIQSSGGSLRLKGRTCSELFGPERCVEDIE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MH053512
EMBL· GenBank· DDBJ
AVO03702.1
EMBL· GenBank· DDBJ
Genomic RNA
MH053587
EMBL· GenBank· DDBJ
AVO03770.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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