L_LYCVW
ID L_LYCVW Reviewed; 363 AA.
AC P14241;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000250|UniProtKB:P14240};
DE Short=Protein L {ECO:0000250|UniProtKB:P14240};
DE EC=2.7.7.48 {ECO:0000250|UniProtKB:P14240};
DE AltName: Full=Large structural protein {ECO:0000250|UniProtKB:P14240};
DE AltName: Full=Replicase {ECO:0000250|UniProtKB:P14240};
DE AltName: Full=Transcriptase {ECO:0000250|UniProtKB:P14240};
DE Includes:
DE RecName: Full=cap-snatching endonuclease {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P14240};
DE Flags: Fragment;
GN Name=L;
OS Lymphocytic choriomeningitis virus (strain WE) (LCMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11627;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3984491; DOI=10.1016/0168-1702(85)90058-9;
RA Romanowski V., Bishop D.H.L.;
RT "Conserved sequences and coding of two strains of lymphocytic
RT choriomeningitis virus (WE and ARM) and Pichinde arenavirus.";
RL Virus Res. 2:35-51(1985).
RN [2]
RP REVIEW.
RX PubMed=28418734; DOI=10.1080/1040841x.2017.1307805;
RA Amroun A., Priet S., de Lamballerie X., Querat G.;
RT "Bunyaviridae RdRps: structure, motifs, and RNA synthesis machinery.";
RL Crit. Rev. Microbiol. 43:753-778(2017).
RN [3]
RP REVIEW.
RX PubMed=31948728; DOI=10.1016/j.tim.2019.12.006;
RA Olschewski S., Cusack S., Rosenthal M.;
RT "The Cap-Snatching Mechanism of Bunyaviruses.";
RL Trends Microbiol. 28:293-303(2020).
CC -!- FUNCTION: RNA-dependent RNA polymerase, which is responsible for the
CC replication and transcription of the viral RNA genome. During
CC transcription, synthesizes subgenomic RNAs and assures their capping by
CC a cap-snatching mechanism, which involves the endonuclease activity
CC cleaving the host capped pre-mRNAs. These short capped RNAs are then
CC used as primers for viral transcription. The 3'-end of subgenomic mRNAs
CC molecules are heterogeneous and not polyadenylated. The replicase
CC function is to direct synthesis of antigenomic and genomic RNA which
CC are encapsidated and non capped. As a consequence of the use of the
CC same enzyme for both transcription and replication, these mechanisms
CC need to be well coordinated. These processes may be regulated by
CC proteins N and Z in a dose-dependent manner.
CC {ECO:0000250|UniProtKB:P14240}.
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 Evidence={ECO:0000250|UniProtKB:Q6GWS6};
CC Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site
CC (By similarity). The divalent metal ions are crucial for catalytic
CC activity (By similarity). {ECO:0000250|UniProtKB:Q6GWS6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=For polymerase activity. {ECO:0000305};
CC -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the
CC polymerase activity. Interacts with nucleoprotein N (By similarity).
CC Interacts with protein Z; this interaction inhibits viral transcription
CC and replication (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P27316, ECO:0000250|UniProtKB:Q6IUF8}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN). The
CC central region contains the RdRp activity.
CC {ECO:0000250|UniProtKB:P14240}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_04086}.
CC -!- SIMILARITY: Belongs to the Arenaviridae RNA polymerase family.
CC {ECO:0000305}.
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DR EMBL; M22016; AAA46266.1; -; Genomic_RNA.
DR SMR; P14241; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR InterPro; IPR026382; CapSnatchArena.
DR InterPro; IPR010453; RNA_pol_arenavir.
DR Pfam; PF06317; Arena_RNA_pol; 1.
DR Pfam; PF17296; ArenaCapSnatch; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW Transferase; Viral RNA replication; Virion.
FT CHAIN 1..>363
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000079199"
FT REGION 26..287
FT /note="Endonuclease"
FT /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT ACT_SITE 115
FT /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT NON_TER 363
SQ SEQUENCE 363 AA; 41607 MW; 7AD2BA6A8DC90A51 CRC64;
MDETIADLRE LCLNYIEQDE RLSRQKLNFL GQREPRMVLI EGLKLLSRCI EIDSADKSGC
IHNHDDKSVE TILIDSGIVC PGLPLIIPDG YKLIDNSLIL LECFVRSTPA SFEKKFIEDT
NKLACIKEDL AVAGITLVPI VDGRCDYDNS FMPEWVNFKF RDLLFKLLEY SSQDEKVFEE
SEYFRLCESL KTTVDKRSGM DSMKILKDAR SFHNDEIMKM CHDGVNPNMS CDDVVFGINS
FFGRFRRDLL NGKLKRNFQK VSPGGLIKEF SELYETLTDN DDILMLSKEP VESCPLMRFI
TAETHGHERG SDANTEYERL LSMLNKVKSL KLLNTRRRQL LNLDVLCPSS LIKQSISKGL
END
