ID   L_SYNV                  Reviewed;        2116 AA.
AC   P31332;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   04-NOV-2026, entry version 124.
DE   RecName: Full=RNA-directed RNA polymerase L;
DE            Short=Protein L;
DE   AltName: Full=Large structural protein;
DE   AltName: Full=Replicase;
DE   AltName: Full=Transcriptase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48 {ECO:0000250|UniProtKB:P28887};
DE   Includes:
DE     RecName: Full=GTP phosphohydrolase {ECO:0000250|UniProtKB:P03523};
DE              EC=3.6.1.- {ECO:0000250|UniProtKB:P03523};
DE   Includes:
DE     RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE              EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
DE     AltName: Full=PRNTase {ECO:0000305};
DE   Includes:
DE     RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE     AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE              Short=G-N7-MTase {ECO:0000250|UniProtKB:P03523};
DE     AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE              Short=N1-2'-O-MTase {ECO:0000250|UniProtKB:P03523};
GN   Name=L;
OS   Sonchus yellow net virus (SYNV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC   Betanucleorhabdovirus; Betanucleorhabdovirus retesonchi.
OX   NCBI_TaxID=11307;
OH   NCBI_TaxID=80764; Aphis.
OH   NCBI_TaxID=42337; Bidens pilosa (Hairy beggarticks) (Cobbler's pegs).
OH   NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH   NCBI_TaxID=50207; Sonchus oleraceus (Common sowthistle).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC PV-263;
RX   PubMed=1604816; DOI=10.1016/0042-6822(92)90678-i;
RA   Choi T.-J., Kuwata S., Koonin E.V., Heaton L.A., Jackson A.O.;
RT   "Structure of the L (polymerase) protein gene of sonchus yellow net
RT   virus.";
RL   Virology 189:31-39(1992).
CC   -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC       of viral mRNAs, their capping and polyadenylation. The template is
CC       composed of the viral RNA tightly encapsidated by the nucleoprotein
CC       (N). The viral polymerase binds to the genomic RNA at the 3' leader
CC       promoter, and transcribes subsequently all viral mRNAs with a
CC       decreasing efficiency. The first gene is the most transcribed, and the
CC       last the least transcribed. The viral phosphoprotein acts as a
CC       processivity factor. Capping is concomitant with initiation of mRNA
CC       transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase)
CC       adds the cap structure when the nascent RNA chain length has reached
CC       few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC       facilitates subsequent guanine-N-7 methylation, both activities being
CC       carried by the viral polymerase. Polyadenylation of mRNAs occur by a
CC       stuttering mechanism at a slipery stop site present at the end viral
CC       genes. After finishing transcription of a mRNA, the polymerase can
CC       resume transcription of the downstream gene.
CC       {ECO:0000250|UniProtKB:P03523}.
CC   -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of
CC       viral genomic RNA. The template is composed of the viral RNA tightly
CC       encapsidated by the nucleoprotein (N). The replicase mode is dependent
CC       on intracellular N protein concentration. In this mode, the polymerase
CC       replicates the whole viral genome without recognizing transcriptional
CC       signals, and the replicated genome is not caped or polyadenylated.
CC       {ECO:0000250|UniProtKB:P03523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC         adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC         triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC         adenosine in mRNA + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC         Evidence={ECO:0000250|UniProtKB:P03523};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC         mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC         adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC         Evidence={ECO:0000250|UniProtKB:P28887};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC         adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC         5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC         adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC         ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P28887};
CC   -!- SUBUNIT: May form homodimer. Interacts with the P protein.
CC       {ECO:0000250|UniProtKB:P03523}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged
CC       asymmetrically towards the blunt end of the virus.
CC       {ECO:0000250|UniProtKB:P03523}.
CC   -!- SIMILARITY: Belongs to the rhabdoviridae protein L family.
CC       {ECO:0000305}.
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DR   EMBL; L32603; AAA50385.1; -; mRNA.
DR   EMBL; M87829; AAA47896.1; -; mRNA.
DR   PIR; A40230; ZLVNSY.
DR   RefSeq; NP_042286.1; NC_001615.3.
DR   SMR; P31332; -.
DR   GeneID; 1489882; -.
DR   KEGG; vg:1489882; -.
DR   Proteomes; UP000002326; Segment.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0062105; F:RNA 2'-O-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR039736; L_poly_C.
DR   InterPro; IPR026890; Mononeg_mRNAcap.
DR   InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR   NCBIfam; TIGR04198; paramyx_RNAcap; 1.
DR   Pfam; PF14318; Mononeg_mRNAcap; 1.
DR   Pfam; PF00946; Mononeg_RNA_pol; 2.
DR   PROSITE; PS52108; MNV_L_PRNTASE; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW   Viral RNA replication; Virion; Zinc.
FT   CHAIN           1..2116
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000222842"
FT   DOMAIN          634..818
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   DOMAIN          937..1387
FT                   /note="PRNTase (capping)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   REGION          1213..1229
FT                   /note="priming-capping loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   MOTIF           1151..1165
FT                   /note="PRNTase motif A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   MOTIF           1208..1213
FT                   /note="PRNTase motif B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   MOTIF           1244
FT                   /note="PRNTase motif C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   MOTIF           1284..1285
FT                   /note="PRNTase motif D"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   MOTIF           1323..1332
FT                   /note="PRNTase motif E"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   ACT_SITE        1284
FT                   /note="Nucleophile; for GDP polyribonucleotidyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01452"
FT   BINDING         641
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RNA-directed RNA polymerase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P28887"
FT   BINDING         748
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RNA-directed RNA polymerase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P28887"
SQ   SEQUENCE   2116 AA;  241538 MW;  74D188F3D4CF1D80 CRC64;
     MEGMDHWENA KYFQGIEDIE EDTRQPTVDS MSSGTYHCKS ALRSHKDNMK LFLYRRDFLI
     FSHRFNGLPY DEQYLGVLPK LWSCFYDKTH DLSGFLDQYA SREHCTPSDS FSRWADPTVL
     HLYDDPIIRN LLASENKVLN FLEGGISDIL DKYQICIKRN IRLIYLHLFL NLALIVLNHT
     DADSMPDRRV ELNGVTFKLE EGVILCEYNE YLKIYVLKGA VIWDMPAYRQ VLQKDLFLTI
     CDKISERINI VIGATIITAL SHKTNLDDPD SHLYDACINM IKIGDNILVN HGNRGFDLLG
     KFEAYCVACI LTYDDQRIWN PLEFLNNLIE DDRINQPDLY NDANNLVAFL RKQPIVILAE
     LHGLWRIWGH PIIDLEGGMK KMEATCTKQS PVSVEETRVC ERTMKLTFFT NYYDKHHHYP
     LSTLTHPDHF NLYSQYLSER DKIEYLANKD IAFEHSYIMR CIRRNKKIFQ RSSLYNHKDW
     DQVVILQSFQ IPKSVNLATM IKDKAISMTR SELIESVNTK NSVFDSTKRR GILKWLNEQS
     DKIYNFLMRI DDKGLDEDDC IIGLYPKERE MKTKARFFSL MSYKLRMYVT STEELLGKYV
     LKYFPMITMS DNLLSMVIRL FDMTTLIGDK GVAVTYSMNI DFSKWNQNMR ERTNAGIFDN
     LDRILGFRSL ISRTHSIFKA CYLYLCSGEY VPVISNNQLT AQSPWSRTGD ESGKEGLRQK
     GWTITTVCDI LSLAFKYNAR IQLIGGGDNQ VLTVTMLPSE SMQSQGRDSQ LLKVRERMTS
     FRNALAKKMV KRGLPLKLEE TWISHNLLMY NKIMYYSGVP LRGRLKVISR LFSNSNVGVT
     SLGGITSTLG TGFQSISTKD YTPTLAWLIS RVFTDIYIST YHLLNPISGT QRLDKQVLMS
     RGNIRQGRNE LGGETSVPII NKIRNHAALA TDHTLDLDSL LICVLYYHKI LGGPGIGPPT
     AYVMKGFPDP LSEGLTFNYL VITNVLNERT KRKIISVTKV MKNRNQHWEH LLEDPVSVNH
     DAPPHGIAAL RAQAEAVMRS AKITNIGFKN LIDIGDNQYL RDLSEKLCSP NDLEPRLLHD
     IVGSTIPGFV NSVLSRVDQS TTINKIAGNS DVVTSIYLSE MSYYLYLSKK VNTQDGHAIG
     SCPTRDSKML RNWTWGKNII GVTTPHPLGY LKRERHSESS SCDNNYIRVL TKRIGNSWEL
     RRGQFRPYFG SYTEEKFKMT TLASAYGDES ILKRAIKIQK LLGWRYHQGS SLYNLIQKIL
     TCVTDADPNK FLPLPDEITG DVEHRYHDMA TKHGGIPSNL IHLYTHASCN TSTFINHSKG
     AANESLHFQA AIIWTCMQSI CRTSASSSVS DISHYHEACN QCIVKLEDPI ESDYSTSDIS
     LMSCPANDLM YVKEDDIPVH FHTTMEFYRA SSSSTVLKKI KKIEDAEVIS SRMTWVVTLC
     SHLLNQDTIK HSTWKLISED LSKEEVMFIV MSITMYIMSE QDIPVHSASL SDFRTLYEKN
     KDIIDRVLGI EALNDAVSGV SFYNNRCSDD QCLRWKETSD QILSHYKTTG TCAVKYQAPH
     FRICTRLVYL MTNPSCQSCP CCLGVIKDDS NDGPIMCQLH GELAGPCGYH LCSLDKLNKT
     KKGLNMSKVF YTDGTISAQH DAKNRPTKKR PHGENSLTEM FKRAKTSREN RILKQNKESY
     LFIQPRLMVD LFIDMGSMWE KTQISDQGSH IIPAHTNPIV LSKKSDLYVP AAISKFVSNG
     FLIMDAVERA LGKPSKPITE HSQLSVNISY GIEYHPEIKR ETVQLLRFVN ELAYTGYGGG
     VTICITLFPI FISDIEAVDP RLISDIIYRY RADSSDYACI RLTDMGDMCF DINNILSDCD
     ACLSYDPGCW SQDANLVYII SDTSDIMIKA KEFETLHSFN KFYSVECLAP RFFMSSSTVS
     ALVISKSSSI NSIDYDRLAE IHLDRRGTQM WDLSRLFANM TMRDGLTEMI KCIYNNVSGE
     ATILTSQSLV DAAISKIKVD ILRGLIDMVR GERMNWRTQY MIQILLGVMI LTSDNPEDYR
     REISKYNNAV VLLQKPRRIK LIRDHLGGAD RKFYHATTNN GLLGSSLNDV THILEGILYI
     THRTSRKLCT SISLEV
//