L_LNYV3
ID L_LNYV3 Reviewed; 2068 AA.
AC Q4W382;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Lettuce necrotic yellows virus (isolate 318) (LNYV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC Cytorhabdovirus.
OX NCBI_TaxID=928304;
OH NCBI_TaxID=43191; Embergeria.
OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH NCBI_TaxID=43208; Reichardia tingitana.
OH NCBI_TaxID=255580; Sonchus hydrophilus.
OH NCBI_TaxID=50207; Sonchus oleraceus (Common sowthistle).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16313992; DOI=10.1016/j.virusres.2005.10.024;
RA Dietzgen R.G., Callaghan B., Wetzel T., Dale J.L.;
RT "Completion of the genome sequence of Lettuce necrotic yellows virus, type
RT species of the genus Cytorhabdovirus.";
RL Virus Res. 118:16-22(2006).
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}.
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DR EMBL; AJ746199; CAG34091.1; -; Genomic_RNA.
DR EMBL; AJ867584; CAI30426.1; -; Genomic_RNA.
DR RefSeq; YP_425092.1; NC_007642.1.
DR SMR; Q4W382; -.
DR GeneID; 3844362; -.
DR KEGG; vg:3844362; -.
DR Proteomes; UP000008592; 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 GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 3: Inferred from homology;
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..2068
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297837"
FT DOMAIN 564..750
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1657..1847
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2068 AA; 236583 MW; 45AD5205F9A1B6EE CRC64;
MDLWNEETTP KKNAYDSLPD YHLQNPLYAI TDQLSMLKRG KRLNYRLTSS YKLMKSQSTD
IKEGDPILLK EWARNWFSET ELYVVDQTLS DCENRLSLDE TDDLHFDTHL LRESVRMWRC
EFPHDDWVRM RGMQNLLIVM NAISSRRPPP PRHTCIIPGL SKITVEGGVV LVTSSLLGFQ
PEGDKETTVF AADWVRAVSD VYTERFLVLS GAILGRCLSD EHYPQVLDLE FIINWGDTVL
RRKGNKGFKL LKAYEALVLG VVQGKSESDF IDPDRFLRNT LNDIIDDDKD LGAYAVLLIQ
RLQQIDSAHH LIQLFGLHRI WGHPLVDPAK GMEKMIIIGQ KDIVRETSRP EVMGVHFKKL
MAQGYREKHG VYPNVKGNGE LETLIKNNHD WKEVGSLDND NHWRLLRFDK TFSIPESFNL
SMIVADKSVS PTLSELKENI LRKKTVMNQE LRRGVLRWIN HDSIDPREFL EQVNDKKFPD
DHKIIGLRSK EREMNPTPRM FALMSHLMRV YVVITESMLS EHILPYFPQI TMTDSQLDLT
KKTYSTVKNQ AAKIRRSGAL YDTKTVCMSL DFEKWNGHMR KESTFHVFEA LGDLFGMENL
YNETYDIFKD SYFYLADGSY VPSMDAQGNF TPEPPYSFTG HKGGQEGLRQ KGWTIFTVVC
LDWICRKHNC TYKIMGMGDN QVLQLTMYTY RVDASGKATE RGREDMRRVL FGLFDDLLDV
FSDLGLPLKP LETWISEDLF VYGKYPVLKG VPLSMDLKKI MRIFPFSNQE TMTIENALNT
IAGNAQAATQ AAPFLGVSYL VGIFMISLCS HDMLVYHPLI AKGLREVLRE NRTWGLKFKG
AHQVKTDIKG EMVDETNLRR LMMNVPRILG GYVSFNLYGL MMRGFPDPVS LAYSQLFSWG
VPTGGSDQRD YMLRWLKPIF MPERSMRLLV EDVSSVNLLA PVTPTAGLRR VVEQYLTDGR
VIKNAEFRDL MMSRDNELED VISEHLCSGE HLHIRLIHDI MESTIFGYVK SITSKVTKSS
TIVSLAIGKA KGDPLTRLMS DEENYFRFFM WRSVINPHYD IPACPTDLAK QVRRIGWGKE
LIGVTVAYPW SFLKKTDCYE SGCLCTCDDG FISLFLPDSP VTPQEWDRSI GKNPPYLGSM
TKEKVVISTG SKVYSGEPLV RRPINLMRVI GWFVPEESET AKIIMSCVSA VSDVNPLIFK
GMTEGTSGSE IHRFRDTSLK HGALCSSNYL YSTRYHVSTD TFTRYAKGAQ NYDMLFQANL
CAIVETTHQY VLKTNQSKEP QRKTHHYKQT CYSCINPLDE SFYDVKSSKL SQLIPSKKTN
KYLYVPEAKI SMTLEHVPAK SWEFGTLSSD GFDQLSVNLR LQWLTDAVAD NVVIDILNPA
GEESYTTTSL MDIKEHNRLF YLTIRPRDFY DQLCNRILIL AEWRCMSLSD WKTPTTEAIS
RAAEAIIGDT PISRWYGVTG FFSWPSSMER YYVYPEIQEP DSIPVTALSA CRSVRNSLLG
LLGSSRKFRG RNTRIFSEDA KASKLSLKLM VYDWVKKKKK CRACHREIGI MSAHQLSSTL
PNSIICPKGH YVTQGLKDLD IMRSRVTLDS LRKCCSSDEI PTEPMEKKIT EWAPLTSTTC
RTLFDSSSMR SELIPYSPTG IESSINVQPI PKSDLYKLIS LPTNAMYKYM EVISRNIEGI
MNCKTAFVTG NGLGGTSKVL SNMWPGRIIT STLLDTGDAI PQVYPNCDKG SSSYARGTVI
SDLMVTRVND VNHLLWGEDW KPVFQSYETD LCISDIEING ELNGESRQTM IATVTMAHDW
KMVIMKDYIY NMREMENRLS ILLPVFKSLE LITCNSRQRV MPEVWWIMKA RRSSGKLLGY
HRSVIRQIWD GVKEGINTAD WAMESVFSEI NRTIASTADM IAMTIRLKAF FSLPIVGSVL
PYKGSYTRLL GYLQRGKKPE DISLITSDDG KRLYLSDYEK VRSVLFGLAV GMCSSATERD
RMLDESEYWA IDWIPSGPHI WLPYLFKGVE RSTLIHVYDY IPMLTLIMKR ERLLFKSSSD
IIEFKYTNNR DSCCFPITKT AKIKFNIK