L_TUPVT
ID L_TUPVT Reviewed; 2107 AA.
AC Q4VKV2;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
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 Tupaia virus (isolate Tupaia/Thailand/-/1986) (TUPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Tupavirus.
OX NCBI_TaxID=1560034;
OH NCBI_TaxID=9394; Tupaia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15890917; DOI=10.1128/jvi.79.11.6781-6790.2005;
RA Springfeld C., Darai G., Cattaneo R.;
RT "Characterization of the Tupaia rhabdovirus genome reveals a long open
RT reading frame overlapping with P and a novel gene encoding a small
RT hydrophobic protein.";
RL J. Virol. 79:6781-6790(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; AY840978; AAX47602.1; -; Genomic_RNA.
DR RefSeq; YP_238534.1; NC_007020.1.
DR SMR; Q4VKV2; -.
DR PRIDE; Q4VKV2; -.
DR GeneID; 3416615; -.
DR KEGG; vg:3416615; -.
DR Proteomes; UP000029771; 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:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
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 InterPro; IPR017234; RNA-dir_pol_rhabdovirus.
DR Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 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;
KW Viral transcription; Virion.
FT CHAIN 1..2107
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000432053"
FT DOMAIN 594..780
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1635..1832
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2107 AA; 241782 MW; BBA3684C7B8A872C CRC64;
MESWPEDNVD SFESSPFWEL EEDWVAPKNK GQLGSVKNTD YNLNNPLLSD GLTAFCRYLK
GKSFDKIFHL HRWISTKALM EESKIRVEGN PEALHHWMGE YFLNQDIPLS RFKPLWDLVI
KHSRLTHIVP ELFVRSLGRY HLPYLERGER NWEKLYLTKF MEWHLLVIVM NHFEDDLSSI
APLINLKKKS SAHGICYSAR VSGVGEVLVF DWILVLPNGL ILNKNFVLMI KDTLLARFQT
LITMYPRHDG KFTLEDVRTL LKVYSLGDRM LYTIGNEAYD LLKFVEPICN LRMTQLANKH
RPLIPEFPNF RQYLEAELPE LCKLSPIIME LWDTITSLDD PELVVQIFGC FRHWGHPFID
YGEGLQKLYE QVTMPKIIDD ELAQALGSDL AYLVLRSQFK KTKKWFVDPS KLPMNHPLKK
FVETSTWPTP KVIEDFGDKW HTLPLTQCFD IPDLVDPALI YSDKSHSVNR RSLIQHVSSG
AYSKFPTKRV LTTFLTEPAR DWKSFLQQIN DRGLPDDALC IGLRPKEREL KRAGRFFALM
SWELREYFVF TEYLIKEHFI PLFKGLTMAD DMTGVIKKLL ECSNGHGETD YSNITISNHL
DYSKWNNHQR YESNKYVFQV MGSFLGYPNL ISRTHEFFQK SLIYFINRPD LMVVKGNTLE
PKGQMRVCWN GQAGGLEGLR QKGWSIVNLL LIMRVGKLRN TEIKILAQGD NQVMNSHYKL
PAYRTDFELL ECISEIIRNN KYIMQEVDHW TQRLGLIINK DETMQSADFL IYGKVPIFRG
NITIPESKKW SRVNCVTNDQ LPTFGNVMST VSSTALSVSH FSNSFLDPIE FYNLLGNFSR
ILLEMFNPVL NKSLLQFFTD WSQFEDVGYL ISVLYLDPSL GGVCGMSLSR FLIRAFPDPV
TEGLSFWRRL STVTSDPNLR KLFLSFGNPP LGRFKMEDLT KLMEKPESLN IPSSLSAQIL
IRTEIREILR RNVRVIKNEI IVNAISYGMQ AEEHLIRFLY SIKPLFPRFL AEFKSSTYLG
LTESLVGLYE NSKTIRNRFL GQREREIDDL VQRSEYVGIK YLVQVRKERT TPGPWNCSAS
HADRLRRLSW GQPVIGATIP HPFEMLGKVC YLFRGSGCEC PDSSNYTTTF VNWDAESVMS
RKGPFLPYLG SKTSESTSLI NPWERETIIP LIKRAAKLRN AINWFVRSDS LLARSILNNL
RALTGEDPGQ GNPGFFRTGS ALHRFACSRQ SSGGFSALSP AYLSRFLTTT DTLQGIGDRN
YDFMFQSLIL YSQSSLCVQI NRNVQGIVHH HISCNECLRE ITEPFLEGSF EYKPKDVSRH
VRKWIPGGNQ ILTEKLRLEF QYGNWEAISD AEKTYHVGRA IGFVFSDYAF SSSAQLEESS
LFPLSIRNSL TPELFYEGLI DGLIRGCSIQ ITHRRNVALL KKPRETLVGS VFFAITKITL
NTPFLSLVRV GAIHDYIIRN SHRTPPSYPL SKWDLGGILR HYLKTRFLHL LRTGYSSRYT
SVWIFADLAG IEVGGLLCLS SHLLEYSVSP NKTKLGAERL RKFKEIEINM RQKTQVDLSC
LDLRRVYLCK SEVRHSVKSI DKKTVQSEAP LYKFEEEEVG YVVAWDVSYL SAPALSPKEE
LTVPRLQCPL ISGLRTIQLA TGAHYKVRSI LNHFNIQFDD FLCGGDGSGG LTAMCLRWNR
FSRGIFNSLL DLSGYDLRGS RPSEPSAIAA LGADAARCVN RQTCWQHPSD LTDKSTWNYF
VDLKAEFGLT IKLMIFDMEN RDEQSFLIED QIIDYLPRLL SRSGSLIFKT YCHRLISQQN
PLLLKRLGRH FKRSCLVQTE FTSNFSSEVY VVLMDYVPGN SLAGIVDYTE MTRFLGKRFV
FSNPVDEFKR ALGIKRKAME KGIPSELLPD PEVELATVLE ICGLESGRAA SVAEICCSKS
ISPKVKYLFV RSITFCSFFN LTSGFSERPH VPSDSKLLRF FSFFIGLEYW WSWVSEELPR
FERMNQFLRE DLFITHESKK GKDFWVRKVF LGAFDIGVVK RLRLQGSLAG IGSAIRSLRR
AVPLNETGLT LSVSELIGRF DRGLTPSVLS SRSNLLTYIQ DYRSNLDLPV SSEIINTGIR
GDMATTE
