L_TAVCV
ID L_TAVCV Reviewed; 1928 AA.
AC Q5GA85;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
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 Taro vein chlorosis virus (TAVCV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC Alphanucleorhabdovirus.
OX NCBI_TaxID=2749935;
OH NCBI_TaxID=4460; Colocasia esculenta (Wild taro) (Arum esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15659770; DOI=10.1099/vir.0.80591-0;
RA Revill P., Trinh X., Dale J., Harding R.;
RT "Taro vein chlorosis virus: characterization and variability of a new
RT nucleorhabdovirus.";
RL J. Gen. Virol. 86:491-499(2005).
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; AY674964; AAV92087.1; -; Genomic_RNA.
DR RefSeq; YP_224083.1; NC_006942.1.
DR SMR; Q5GA85; -.
DR GeneID; 5076497; -.
DR KEGG; vg:5076497; -.
DR Proteomes; UP000007540; 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; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 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..1928
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297841"
FT DOMAIN 596..782
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 1928 AA; 217363 MW; 042E4E6FBC396429 CRC64;
MDSDYPDLDP EALTVLDSIR EGIQDEEEED NNDKILSGTG DYHLKSALRT LDDMTRHPIF
NKEYQKAVRH FGISPTMMMT PTAVLKLTVS QTKINKAVGF LFGDILVRLD SLPWAVDCYD
SIQAEIKTMH SHMMIFATPS WVEDVHNKVS SLVEYDHDAT LIWATVITLK NYLPAWREKG
ASLLDWRSVQ YDPESEYLVM KVDRDFIIYV GSDICVMEIG KQTLWAPVPY ILNGADKVAE
RYNVKYYCAL CDELDIPDRI SLEKLNQIIE VGDDCLQALG NKGYDIIGSY EALLAGIIQA
RDNPQVIPDR ELLQRTTLND PGNTIGVTFL KRWDALMEDL NPEQIACAHG LYRIWGHPAV
DILGGINKMR EVASIVKLPS SKILTDIGRQ FKEMFFTSYH SVHKHYPKHL IREYKSDSYI
HECLKDNRTL NSKVLSYHFP DWDSVALEKN FEVPYSWNLV HNLKDKAISP SRSELYETLS
TRNSIFGASN RRGILKSLTM ETVQLRAFLQ DVNDKGLPDN DKIIGVYPKE RELKIKARLF
SLMSFKLRLY FVSTEALLGD KILKYFPQIT MSLDMLSMIK KMFRVSGQTT RGDDSVTVIF
NLDFVKWNLQ MRKIICSPVF TQLGALFGMP NLFDITHDLF RESVIYLCSG EGDLRGDPVF
GVAPDGVWSW TGDESGKEGL RQKGWTILTV VTIMLIAKRH HVDVSLMGGG DNQVLGITIG
GMVRDSVGEL TQDSCKLAQC TIKRFTQDLI TTFGDLGLPL KASETWVSDS LFMYNKHMFY
KGMPLRSPLK AVSRIFPLAN DSIMTLDNMI NNISSGVKAA CMKERHGIPL VFIKTMAYRR
VAELSLIMHP LTVCFKKPEL PDHGIVARSG KKLKIPVTSK NLRQYFSLCT LGSSTMGHPG
TLHLPDIIMR GFPDPLTSHL SFISEMRRYI VDPGLASVVD KLSHLSTSPT TEYAKLVEDP
TSINHDAPTH GLNEIRQMSR DFLMSTTLAT NPHLKSLFSL LDRGTEKDFY DALCSAQELD
VKVLHEIAGA TLYGYTNGIA SRIDQTGTVR ALNENIDVLR RLALAETRYI GYLMARDTRE
HDLKPSSCSR ITAQQYRDLS WRKPILGVTV PHPMEMCQIM SSTETIYHDA VVCWSDRVSG
SEIYQSMGQG KIYQGSYTKE RFKATDIAAA YGNEDILVKA VRLQKLINWR YDEGSNFAKI
ISLTLEAITD ANTEGFHRSK EEIKGEFDHR RGVTGDISGG IPNFLVTPTS HFSSTTSSWV
SHSRGGKNEN IHFQSVLINL LYRAMVYRGS VPGLPEMIWY SKEKCSDCIT EIKDPDPIKT
TPSLHTLPSA KGNPFAYIES VNVKLDYHHQ IEITKGMEEE YLINSLWDGQ NVSGEEESGL
LLYLMLIGSR QISESFILLM RERINAATAL QYMLNRVILA RKLGLDSQFP IRSTSCVNLL
LGTDDNILSC RDRFNIELLS GSWESGVSCD MSVLYRDDLL TASELHVNVY LQNVPLQLAL
SRAASSTQLQ SCLECQAIVL DRPSQRELMR YLHWCCPYHT ANAPPRILRI HSEKLIKGIE
LRTDNPLLVP YVCNPVTLER VEKVPVMVDS WELPVHMHST WDSILPQLYL TLKSLLSQVT
ISSLIVDDDI TLINLAASVM LDLRRELPVY INVKGFSGTE INNKFDNLKL LPPNIRSSVS
VYHENRSLIE ASAAVWLPEP SSVESVGADW LVLWGDTWRM GAGVPGHVLV TESKLSTGMA
WVLHRDPLAS QSVLELCGAV QIWEKKALDW DMREGHCVPI QMNRTLACSR LGSRGVRWTM
WSTAAGLDKV TRILRSKLLS LSGNPGSSYH WRKGCQKILK AYVLSLYAHC VDNMLEASGR
LVGVSVHGSL SGIVPICDMH SSDRIQRAQY LFLKERCQGG PFILRNRLER RINLLSPVHD
LLDGPSQS
