ID   L_TSWV1                 Reviewed;        2875 AA.
AC   P28976;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=RNA-directed RNA polymerase L;
DE            Short=Protein L;
DE            EC=2.7.7.48 {ECO:0000250|UniProtKB:I0DF35};
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.-.- {ECO:0000250|UniProtKB:Q6GWS6};
GN   Name=L;
OS   Tomato spotted wilt virus (strain Brazilian Br-01) (TSWV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Tospoviridae; Orthotospovirus.
OX   NCBI_TaxID=36413;
OH   NCBI_TaxID=133901; Frankliniella occidentalis (Western flower thrips) (Euthrips occidentalis).
OH   NCBI_TaxID=163899; Scirtothrips dorsalis (Chilli thrips).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=161014; Thrips tabaci.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1895058; DOI=10.1099/0022-1317-72-9-2207;
RA   de Haan P., Kormelink R., de Oliveira Resende R., van Poelwijk F.,
RA   Peters D., Goldbach R.;
RT   "Tomato spotted wilt virus L RNA encodes a putative RNA polymerase.";
RL   J. Gen. Virol. 72:2207-2216(1991).
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).
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. {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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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       The divalent metal ions are crucial for catalytic activity.
CC       {ECO:0000250|UniProtKB:Q6GWS6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P14241};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P14241};
CC       Note=For polymerase activity. {ECO:0000250|UniProtKB:P14241};
CC   -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the
CC       polymerase activity. Interacts with nucleoprotein N.
CC       {ECO:0000250|UniProtKB:P27316}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P14241}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P14241}.
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 has a
CC       histidine upstream of the active site that coordinates the first
CC       cation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Bunyavirales RNA polymerase family.
CC       {ECO:0000305}.
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; D10066; BAA00955.1; -; Genomic_RNA.
DR   PIR; JQ1335; RRVUTW.
DR   PRIDE; P28976; -.
DR   Proteomes; UP000006674; Genome.
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:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR   GO; GO:0039696; P:RNA-templated viral transcription; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR   InterPro; IPR015841; RNA-dir_pol_tospovirus.
DR   InterPro; IPR007322; RNA_pol_bunyavir.
DR   Pfam; PF04196; Bunya_RdRp; 1.
DR   PIRSF; PIRSF036872; L_TospoV; 1.
DR   PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..2875
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000222027"
FT   DOMAIN          1347..1530
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          96..236
FT                   /note="Endonuclease"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         185
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         1492
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:I0DF35"
SQ   SEQUENCE   2875 AA;  331503 MW;  574B3B55CF07C6FB CRC64;
     MNIQKIQKLI ENGTTLLLSI EDCVGSNHDL ALDLHKRNSD EIPEDVIINN NAKNYETMRE
     LIVKITADGE GLNKGMATVD VKKLSEMVSL FEQKYLETEL ARHDIFGELI SRHLRIKPKQ
     RNEVEIEHAL REYLDELNKK SCINKLSDDE FERINKEYVA TNATPDNYVI YKESKNSELC
     LIIYDWKISV DARTETKQWR NTYKNIWKSF KDIKVNGKPF LEEHPVFVSI VILKPIAGMP
     ITVTSSRVLE KFEDSPSALH GERIKHAKNA KLLNISYVGQ IVGTTPTVVR NYYANTQRIK
     SEVRGILGDD FGSKDVFFSH WTSKYKERNP TEIAYSEDIE RIIDSLVTDE IPREEIIHFL
     FGNFCFHIET MNDQHIADKF KGYQNSCINL KIEPKADLAD LKDHLIQKQQ IWESLYGKHL
     EKIMLRIREK KRKEKEIPDI TTAFNQNAAE YEERYPNCFN DLSELKLTFH DLVPSLKIEL
     SSEVDYNNAI INKFRESFKS SSRVIYNSPY SSINNQTNKA RDITNLVRLC LAELSCDTTK
     MEKQELEDEI DINTGSIKVE RTKKSKEWNK QGSCLTRNKN EFCMKDTGRE NKTTYFKGLA
     VMNIGMSSKK RILKKEEIKE RISKGLEYDT SERQADPNDD YSSIDMSSLT HMKKLIRHDN
     DDSLSGKRFK GSFFLLHNFN IIEDGKITSV FNNYAKNPEC LYIQDSVLKT ELETCKKINK
     LCNDLAIYHY SEDMMQFSKG LMVADRYMTK ESFKILTTAN TSMMLLAFKG DGMNTGGSGV
     PYIALHIVDE DMSDHFNICY TKEIYSYFRS GSNYIYIMRP QRLNQVRLLR LFKTPSKVPV
     CFPQFSKKAN EIGKSLKNKD IEKVNLFSMT MTVKQILINI VFSSVMIGTV TKLSRMGIFD
     FMRYAGFLRL SDYSNIKEYI RDKSDPDITN CGRYLFRNGI KKLLFRMEDL NLSTNAKPVV
     VDHENDIIGG ITNLNIKCPI TGSTLLTLED LYNNVYLAIY MMPKSLHNHV HNLTSLLNLP
     AEWELKFRKE LGFNIFEDIY PKKAMFDDKD LFSINGALNV KALSDYYLGN IENVGLMRSE
     IENKEDFLSP CYKISTLKSS KKCSQSNIIS TDEIIECLQD AKIQDIENWK GNNLAIIKGL
     IRTYNEEKNR LVEFFEDNCV NSLYLIEKLK EIISSGSITV GKSVTSKFIR NNHPLTVETY
     LKTKLYYRNN VTVLKSKKVS EELYDLVKQF HDMMEIDLDS VMNLGKGTEG KKLTFLQMLE
     FVMSKAKNVT GSVDFLVSVF EKMQRTKTDR EIYLMSMKVK MMLYFIEHTF KHVAQSDPSE
     AISISGDNKI RALSTLSLDT ITSYNDILNK NSKKSRLAFL SADQSKWSAS GLTTYKYVLA
     IILNPILTTG EASLMIECIL MYVKLKKVCI PTDIFLNLRK AQQTFGENET AIGLLTKGLT
     TNTYPVSMNW LQGNLNYLSS VYHSCAMKAY HNTLECYKNC DFQTRWIVHS DDNATSLIAS
     GEVDKMLTDF SSSSLPEMLF RSIEAHFKSF CITLNPKKSY ASSSEVEFIS ERISKWSDYS
     SLLQAFSKLL HRIFAYKLFD DLMSLSIHVT MLLRKGCPNE VIPFAYGAVQ VQALSIYSML
     PGEVNDSIRI FNKLGVSLKS NEIPTNMGGW LTSPIEPLSI LGPSSNDQII YYNVIRDFLN
     KKSLEEVKDS VSSSSYLQMR FRELKEKYER GTLEEKDKKM IFLINLFEKA SVSEDSDVLT
     IGMKFQTMLT QIIKLPNFIN ENALNKMSSY KDFSKLYPNL KKNEDLYKST KNLKIDEDAV
     LEEDELYKKI ASSLEMESVH DIMIKNPETI LIAPLNDRDF LLSQLFMYTS PSKRNQLSNQ
     STEKLALDRV LRSKARTFVN ISSTVKMTYE ENMEKKILEM LKFDLDSYCS FKTCVNLVIK
     DVNFSMLIPI LDSAYPCESR KRDNYNFRWF QTERWIPVVE GSPGLVVMHA VYGSNYIENL
     GLKNIPLTDD SINVLTSTFG TGLIMEDVKS LVNGKDSFET EAFSNSNECQ RLVKACNYMI
     AAQNRLLAIN TCFTRKSFPF YSKFNLGRGF ISNTLALLST IYSKEESYHF VSTASYKLDK
     TIRTVVSAQQ DMNLEKILDT AVYISDKLQS LFPTITREDI VLILQNVCLD SKPIWQSLED
     KMKKINNSTA SGFTVSNVIL SHNSELNTIQ KQIVWMWNMG LCSHRTLDFV IRYIRRRDVR
     YVKTEEQDES GNYVSGTMYK IGIMTRSCYV ELIASDQDVA VSLRTPFEIL NEREYLFDTY
     RESIEKLLAE IMFDKVNIIN QTTTDCFLRT RRSCIRMTTD NKMIVKVNAT SRQIRLENVK
     LVVKIKYENV NSDVWDIIES QKSLVLRLPE VGEFFSDMYK TADSETETIK TIKNRLMTSL
     TFIEAFGNLS QQIKEIVDDD IRETMDEFLM NIRDTCLEGL ENCKSVEEYD SYLDENGFND
     TVELFENLLR THDNFENEYS PLFSEIVDKA KQYTRDLEGF KEILLMLKYS LINDASGFKS
     YRATGMHAVE LMAKKHIEIG EFNLLGMIQL IKACETCHNN DSILNLASLR NVLSRTYATF
     GRRIRLDHDL DLQNNLMEKS YDFKTLVLPE IKLSELSREI LKENGFVISG ENLKMDRSDE
     EFVGLASFNV LRLDEEEMYE GLIKEMKIKR KKKGFLFPAN TLLLSELIKF LIGGIKGTSF
     DIETLLRNSF RPDIFSTDRL GRLSSSVPAL KVYATVYMEY KNVNCPLNEI ADSLEGYLKL
     TKSRSKEHFL SGRVKKALIQ LRDEQSRTKK LEVYKDIANF LARHPLCLSE KTLYGRYTYS
     DINDYIMQTR EIILSKISEL DEVVETDEDN FLLSYLRGEE DAFDEDELDE EEDTD