AC   MF_04086;
DC   Protein; auto
TR   HAMAP; MF_04086; -; 1; level=0
XX
Names: ARENA_L
XX
ID   L
DE   RecName: Full=RNA-directed RNA polymerase L;
DE            Short=Protein L;
DE            EC=2.7.7.48;
DE   AltName: Full=Large structural protein;
DE   AltName: Full=Replicase;
DE   AltName: Full=Transcriptase;
DE   Includes:
DE   RecName: Full=cap-snatching endonuclease;
DE            EC=3.1.-.-;
GN   Name=L;
XX
CC   -!- FUNCTION: RNA-dependent RNA polymerase, which is responsible for the
CC       replication and transcription of the viral RNA genome using antigenomic
CC       RNA as an intermediate. During transcription, synthesizes subgenomic
CC       RNAs and assures their capping by a cap-snatching mechanism, which
CC       involves the endonuclease activity cleaving the host capped pre-mRNAs.
CC       These short capped RNAs are then used as primers for viral
CC       transcription. The 3'-end of subgenomic mRNAs molecules are
CC       heterogeneous and not polyadenylated. The replicase function is to
CC       direct synthesis of antigenomic and genomic RNA which are encapsidated
CC       and non capped. As a consequence of the use of the same enzyme for both
CC       transcription and replication, these mechanisms need to be well
CC       coordinated. These processes may be regulated by proteins N and Z in a
CC       dose-dependent manner.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site.
CC       The divalent metal ions are crucial for catalytic activity;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=For polymerase activity;
CC   -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the
CC       polymerase activity. Interacts with nucleoprotein N. Interacts with
CC       protein Z; this interaction inhibits viral transcription and
CC       replication.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
CC   -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN). The
CC       central region contains the RdRp activity.
CC   -!- SIMILARITY: Belongs to the Bunyavirales RNA polymerase family.
CC   -!- MISCELLANEOUS: Classified as His(-) endonuclease since it does not have
CC       a histidine upstream of the active site that coordinates the first
CC       cation. His(-) endonucleases display very low activity in vitro,
CC       although they are clearly active in vivo.
XX
DR   PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1; trigger=no
DR   Pfam; PF06317; Arena_RNA_pol; 1; trigger=no
DR   Pfam; PF17296; ArenaCapSnatch; 1; trigger=no
DR   PIRSF; PIRSF000836; L_ArenaV; 1; trigger=no
XX
KW   Cap snatching
KW   Host cytoplasm
KW   Hydrolase
KW   Nucleotide-binding
KW   Nucleotidyltransferase
KW   RNA-directed RNA polymerase
KW   Transferase
KW   Viral RNA replication
KW   Virion
KW   Metal-binding
KW   Magnesium
KW   Manganese
XX
GO   GO:0030430; C:host cell cytoplasm
GO   GO:0000166; F:nucleotide binding
GO   GO:0003968; F:RNA-dependent RNA polymerase activity
GO   GO:0075526; P:cap snatching
GO   GO:0039689; P:negative stranded viral RNA replication
GO   GO:0039696; P:RNA-templated viral transcription
XX
FT   From: L_LYCVA (P14240)
FT   DOMAIN          1166..1360
FT                   /note="RdRp catalytic"
FT   REGION          26..287
FT                   /note="Endonuclease"
FT   ACT_SITE        115
FT   BINDING         51
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         89
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         89
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   BINDING         1322
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RdRp activity"
XX
Size: 2198-2238;
Related: None;
Template: P14240;
Scope:
 Viruses; Arenaviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.10 2022/11/19
//