L_DMSVA
ID L_DMSVA Reviewed; 2129 AA.
AC C6S3N3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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 Drosophila melanogaster sigma virus (isolate Drosophila/USA/AP30/2005)
OS (DMelSV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Sigmavirus.
OX NCBI_TaxID=666363;
OH NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AP30;
RX PubMed=17725574; DOI=10.1111/j.1365-294x.2007.03460.x;
RA Carpenter J.A., Obbard D.J., Maside X., Jiggins F.M.;
RT "The recent spread of a vertically transmitted virus through populations of
RT Drosophila melanogaster.";
RL Mol. Ecol. 16:3947-3954(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AP30;
RA Jiggins F.M.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; AM689309; CBA18272.1; -; Genomic_RNA.
DR RefSeq; YP_003126913.1; NC_013135.1.
DR SMR; C6S3N3; -.
DR PRIDE; C6S3N3; -.
DR GeneID; 8363508; -.
DR KEGG; vg:8363508; -.
DR Proteomes; UP000029768; 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 Pfam; PF14314; Methyltrans_Mon; 1.
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;
KW Viral transcription; Virion.
FT CHAIN 1..2129
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000432054"
FT DOMAIN 598..785
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1654..1851
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2129 AA; 241480 MW; ED3456F135C24DEB CRC64;
MDFEIEDPYD PFSMDAYLDP QDPSFGDLES MRHLSNVDYS LNSPMIADEL EAFIRWLQCG
CTDPRWNEDR WVRTKQGLFP GQSPTTIEGA ATFSGWFGNF NLKHRYYVVR QFRMILEKAQ
ADSEETKPVV DAFLRGWINH KGVTLTSKIA LPEEELKWGY YFWELHIVTL HLNCTTDQER
THLIKSFKSK SRGMPDVFDF TLYTRNFGPL SIAGGYVYMF DHNRMLDRNA ILMMKDTYVA
RFNSFLALSN RADCVFPEDA HYRLQMLYEL GDMVLDEGGT SGYNGLKMLE AMCSSRITDL
AQSRKPLIPD FPDFRAHVKA KVIEESVNTP SISKMYELIE GTTNYDTLLT FYGSFRHWGH
PYINYLAGLE KLYMQTTVEK EIDQEYVEKL ASDLAFLVIQ DRFRKTKKWP VDPLLIDKDH
PLVDYIRTSS WPNNSIIKNF GDGWHTLPLT KCYDIPDVID PSLLYSDKSH SMTRSEVREW
MTSHPGKPIP SRKVLSTLLN SPSTNWPMFL QQVNDSGIPI EQLIIGLMAK EREQKIDGRF
FSLMSWDIRD YFVMTEYLIK THFVPLFKGL TMADDLTTVI GKILENSRGQ GEADYENLTI
TDHIDYEKWN NHQRGEANNP IFLVMGKFLG YPHLIERTHE IFEKSWIYYL NRADLMDFDG
EGNLMNRTEL RVCWNGQKGG LEGLRQKGWS ICNLLVLRRE SLATNTVVKT LAQGDNQVLS
SRYRIRTSRD QNQLQSNIRD ICKNNRSLME RIRIGTGKLG LIINHDETIK STEYMNYGKT
CVIHGNIRNL ETKRWSRVTC VTNDQLPTLS NVMATIGSNA LTVSHYSDSP INSMYHYNFM
GNFVRIMNEI HNPALRGPVS SIEGVTGQSF SRLSYLLAVL YLDPSMGGAC GMSLTRFLIR
MFPDPITESL TFLRIVAMNV HSDEVRQTFI QFGNPKLKVF SPEDLSKLLE DPLSINVPKG
LSATNLIKDA IKLSLHKSVD EIANEIIAEA VIHQKDHEEG FLMHLTQISP LFPRFLSEYK
AGTYLGIAEG LIGLFQNSKT IRNQFRRNLD IGYDNIVIKS EIATIRDLTG YRFEDAEKVE
VWSCSSTQAD YLRRVSWQQV VYGATIPHPA ELFGLPLRAA PACPNCTTTF PMNLYISVLI
PLGFKGLKDT RGTCVAYLGS STTESTGIVN PWEKEAVVPV IKRAASLRNG IGWFIEPGSN
LAQSILNNLQ SLTGESWSQN SGGVRRTGSA LHRFSCSRQS SGGYTAQNPS KLTRMIATTN
YLADLGDENY DFMYQSCLLH ALISVGEIHP VDGSQGYYHQ HVNCTSCLRP IKEVTLESPA
PYSHTITSNL LDKWKPDGSK WSVSRPSIPL RSGKWECVSH DRQSYHVGFI QGFIYGDSVW
GIRSMADDPA LFPLSFRNKV NPRAYLLGIL HGLLRSCTVS VVHQRCFRSS RAVKQTTLGL
CSMTVSRLVQ NDGFLNILRD EQFTAVFRSI PHRIPPSYPM VTQDIGDLAS NYLKSQLMTE
GLAYFRSVKS GSGDEAWIFA DANHPMIVSL VTVSGLMTKI LAKDIWQKRD LEELKELRSL
SVQAREQDDP HTDITAMESL AAEWVVCSNQ ETRHAVKYNT RTESITDRRL TVTWGDEYTS
SADFVTVVFS VEEIRTPPGM LIPRIQNPLI SGLRTAQIAT GSHYKLRSIL SKLRLNVRGA
LVGGDGSGGL TALVCRMYPT SRVIFNSICD FSDVRLKGTT PAPPSALSHS LNDCTQVVNY
SDSWAHPSDL TDTKTWKYFV DITKSKSIQV DLIILDMEVV DEISISKIED NLMRYGPQLL
TRDGVILFKT YLTRIFKAQE MILTKCGHVF SQVELWYSDL SSSQTSEVYV LMSGQTKLSH
LQVRKPDLMQ LRTDVSSFPV FASPLLEFKR ARKVAGLDLT VGVPPLLLPE PGPEMINLLS
SLGVRPDISF SITRSFGDNL STEFLPLHLF LLALNGIYDV TTGYRTPPGP PSDQVCLKLG
IWIVGYRIWS GYVQDSYAKT SFGQRLIDNF VPFNFWNKQI GRSWFPHWSL IKPQTYTKNI
QLDSEMAHIG SVIRILHRNF PKARRNPPGD FVDRNCSRIN KGISCLNMDM KTGILRWMGD
GQDLSGTNVT TRISNFYVTQ DDQTASFRN
