L_PARVP
ID L_PARVP Reviewed; 2202 AA.
AC B2MW51;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000255|HAMAP-Rule:MF_04086};
DE Short=Protein L {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Large structural protein {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Replicase {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Transcriptase {ECO:0000255|HAMAP-Rule:MF_04086};
DE Includes:
DE RecName: Full=cap-snatching endonuclease {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04086};
GN Name=L {ECO:0000255|HAMAP-Rule:MF_04086};
OS Parana mammarenavirus (isolate Rat/Paraguay/12056/1965) (PARV) (Paran
OS mammarenavirus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=2169994;
OH NCBI_TaxID=530180; Sooretamys angouya (Paraguayan rice rat) (Oryzomys angouya).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18602020; DOI=10.1016/j.mib.2008.06.001;
RA Charrel R.N., de Lamballerie X., Emonet S.;
RT "Phylogeny of the genus Arenavirus.";
RL Curr. Opin. Microbiol. 11:362-368(2008).
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 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. {ECO:0000255|HAMAP-Rule:MF_04086}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
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 {ECO:0000255|HAMAP-Rule:MF_04086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Note=For polymerase activity. {ECO:0000255|HAMAP-Rule:MF_04086};
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. {ECO:0000255|HAMAP-Rule:MF_04086}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04086}. Host
CC cytoplasm {ECO:0000255|HAMAP-Rule:MF_04086}.
CC -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN). The
CC central region contains the RdRp activity. {ECO:0000255|HAMAP-
CC Rule:MF_04086}.
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 Bunyavirales RNA polymerase family.
CC {ECO:0000255|HAMAP-Rule:MF_04086}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU627613; ACC94302.1; -; Genomic_RNA.
DR RefSeq; YP_001936028.1; NC_010761.1.
DR SMR; B2MW51; -.
DR GeneID; 6334530; -.
DR KEGG; vg:6334530; -.
DR Proteomes; UP000009265; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule.
DR GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0039696; P:RNA-templated viral transcription; ISS:UniProtKB.
DR HAMAP; MF_04086; ARENA_L; 1.
DR InterPro; IPR026382; CapSnatchArena.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR010453; RNA_pol_arenavir.
DR Pfam; PF06317; Arena_RNA_pol; 1.
DR Pfam; PF17296; ArenaCapSnatch; 1.
DR PIRSF; PIRSF000836; L_ArenaV; 1.
DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE 3: Inferred from homology;
KW Cap snatching; Host cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..2202
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000361644"
FT DOMAIN 1158..1353
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT REGION 26..287
FT /note="Endonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT ACT_SITE 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 1313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
SQ SEQUENCE 2202 AA; 252553 MW; B3F2709E75D5C991 CRC64;
MTEIISELKD LIRKWVPDEE HYIEQKSLTL SQVHTRAVVI EGLKLLSLIV EVDSCLKHKC
IPNRNKTVNM ILKDHKLVGP TLPECTPDGY YLCGDVLILL EVFVRSNQSA FEKKYAADFE
KLMSLAKDLT SYGITLVPVI DGRSNYYVEA IPDWVIERLR WLLLKVMDSL KDEGEDIEET
EYSRLIHSLS TMENQNLGLE SISQLKQTGL TYKKKLQALF TKNIRPNMSL GECRLKLIEI
FNEFRLRLES GTVERAYTQT NQDFLLNKLK EHSLLKVSRV SKFDSKGDCH LCSNHLIKVL
GLLKRQTTDE KEAPRIGMIR REYGLILSTC NKIKGQKILN TRRNTLLSLD VVMFNAFLSL
LRTYGEIVFD LMVGGCLQSV NDRLVSPSLI IDLYNKKCTR NPQWLSKVML KLNLLPGYIQ
EDFKVFVRPH LVELDLDLWS NYLELYSTTF ERRLEIQYTV SEEEVHEKTD PEVIEWLEMK
ESTFKQYLDS LSTLSLGLVN SMKTSGTSRF HINQPNDYYG TVKCEECFFQ SLHHAYGVSL
LYQKTGERNR CYSLCSNSGK VGHIVSFYCD PKRFFLPIMS QQVLLSMTQE MLSWLDFIKG
DDLNLISSML RRLILSVLAC PSKRVQLYLQ GLRYFLMAYV NEIHHVQLLA KLEVEVKSRS
EWATMTLADD LVVALLNMSN QPNMSKTFKF LLNVSYLCHL ITKETPDRLT DQIKCFEKFM
EPKIDFGSVI VNSSLNGNMT EEEESKILLD IDRLLSKQLN TSDQISKPGV NPTVMSLCCS
LFNLGELDVN GKLKRDPQSP SFTSTALDMS SNKSVVVPKL DELGNPLSTY DYAAVVSSVI
VDLSEGFKNK LRYKLDPHTL KYKIYKRFLS LVSDKTPKEN KLEMSQDEFL DEITDEQLEM
IEKIEMEVNE CLSKAANVEP RIGTGPDDKN PLKSLWAKEI LCVIESETSK HEVKDFDYTL
FHHETYKELV ELVFNSNSRN QYFTDRILNP CPLEYLMKNL CRKYYEEEDY FECFKYILVS
TGFDNKVGRY DHKNMCRLGF KQSATRIRED ARISCRESNS ESILKRLDKS FFTNSSLRNL
CFYSEESPTA FDSVSSDLGR LKFGLSYKEQ VGGNRELYVG DLNTKLMTRL IEDYFECLME
KMKYTCLNNE AEFERALLDM KSVVRRSGFT VSMDHSKWGP HMSPVIFSQL FKALQFSLPD
GSQIDKEPIL NLLSWHIHKV VEVPFNVVHA YTKGYLKRLC GLMDNRTSKT EDFMDKFFAD
EVIPSHISSV LDMGQGILHN VSDFYGLITE QFISYALQTC VGVLSMAFTS SDDEILLGVT
NDLKNQDESL DIDKSLEFLE FHNYLSATLN KFISPKTVAG TFACEFKSRF YIWSQEVPLL
TKFTAAALHN VKAKAPNQLC ETIDTIQDQC VANGVSVEVV GAISKRTNNI IKYSGHPSNP
FLCLNDMDVK DWVDGSRGYR LQRSVENVYN DDEIPEYVRD MAARLFYLIR NGQVQEEYLI
SSMQSDPDEC FTLLAGILGV PEQNISRLLD IRWLNLRAHG DLRMVLRTKL MGSNRVIQRE
EVPSLIKSVQ SKLSKNFVRG ARKIITDAVN KSAFQSCIAA GFVGICKSMG SKCVRDGKGG
FMYIKDILSK IQYHKNCDVC KVSSGIYCKE SLKAVSDFSR PLFWDYFALV LTNACELGNW
VFSKPKIPDV VYKLDNPNFF WPVKPASHTE LEDKIGMNHV LYSIKRNYPD IFEEHLAPYL
TDLNTLKLSW VQKVKFLDIC VAIDMVSESL GIISHMIKRK REELYIVKQN EQSMSHTRES
QELAGGFRVT NEQICHNFLL QILFDSMITP VLLTSSQFKK YFWYGEVELL PNDCEHPLGQ
LTQFIMDCKK LNLSRAMNLD DLDVGFVHST IKLSDVFLNF STFLTKVDWE NRKDYNNLEE
LLKSTLESQL VLSIGLTFTH LRRSLKYKYE RSTVYTIIAK VILDIEQLTL NEDDQICLIV
QEVECYVSQS GGDHISLDGA ALIPLTPIIS GTETLCLDEV AIRQDDMLKG VSKHLGNVKL
DFSSHIKELK NKFSYKIQGP QVGMNPLHID KGIIMEGDKV VSRLDVNVTA KSLFMALELL
TDDELIRKFL RSLFYYLKSV KKGTALISLL SSDLKDIAEV YFNHFKDILK EEADWVSFGS
FQLVYSKSLD TIMIGDEKGE FRLKGVNCKR LIPVIPAVQE IE
