L_SYNV
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 25-MAY-2022, entry version 112.
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 EC=2.1.1.375 {ECO:0000250|UniProtKB:P03523};
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; Nucleorhabdovirus.
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 concommitant 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=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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000250|UniProtKB:P03523};
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 + H(+) + S-adenosyl-L-homocysteine;
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 + H(+) + phosphate; 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}.
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; L32603; AAA50385.1; -; mRNA.
DR EMBL; M87829; AAA47896.1; -; mRNA.
DR PIR; A40230; ZLVNSY.
DR RefSeq; NP_042286.1; NC_001615.2.
DR SMR; P31332; -.
DR GeneID; 1489882; -.
DR KEGG; vg:1489882; -.
DR Proteomes; UP000002326; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' 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 Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 2.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
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"
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
