L_MMVR
ID L_MMVR Reviewed; 1922 AA.
AC Q6E0W6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 Maize mosaic virus (isolate Maize/United States/Reed/2005) (MMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Nucleorhabdovirus.
OX NCBI_TaxID=928305;
OH NCBI_TaxID=300124; Rottboellia.
OH NCBI_TaxID=4554; Setaria.
OH NCBI_TaxID=4558; Sorghum bicolor (Sorghum) (Sorghum vulgare).
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16005085; DOI=10.1016/j.jviromet.2005.05.013;
RA Reed S.E., Tsai C.W., Willie K.J., Redinbaugh M.G., Hogenhout S.A.;
RT "Shotgun sequencing of the negative-sense RNA genome of the rhabdovirus
RT Maize mosaic virus.";
RL J. Virol. Methods 129:91-96(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; AY618418; AAT66757.1; -; Genomic_RNA.
DR RefSeq; YP_052855.1; NC_005975.1.
DR PRIDE; Q6E0W6; -.
DR GeneID; 2886119; -.
DR KEGG; vg:2886119; -.
DR Proteomes; UP000008593; 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; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 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..1922
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297838"
FT DOMAIN 595..781
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 1922 AA; 216990 MW; 22E843B0BC00ADB6 CRC64;
MDPDYPDLDP ESLDVLNSLQ EGYDEEEEED SGVSLNGMGD YHLKSALRSY TDMMKHPIFK
KEFSKAVINF GISHDSMMSQ IETMFYILKS TPLSMHLGTL YGDLFTRQST LGHSEDVFDI
IQAEIRTLHP HLLLEMTPAK VEEMVLIADR KTYDERAASA FWSTLITIKN YIPAWTEKGA
CTLDWPSVSL DKKSGYVKVM AGKDTTIYIG TDICVIEKYP TVKWAPLSYL LNGADKVAER
LNVRYYSCLC DQLDIPDRIT LDMLDEIIKV GDDCLREMGN DGYNVIGSYE ALLAGIIQRR
DNQGLIPDRD LLWRTTMEEF TSSPGRKYLE EWSTMFSSLS PEQIACAHGL YRIWGHPIVD
ILGGIKKMQE VASVKKNPRQ SVLDEIRRQF KEMFFTSYHR IHKHYPLHTI LNSLDNSYIL
NCLKDNLTIN TSAISYNFQD WDCVMVEKNF EVPFSWNLVH NLKDKAISPN RQEIYQTIST
RGTIFGSQNR RGILKSLTME TVQLRDFLQG INDNGLDDID KIIGVYPKER ELKIKARLFS
LMSFRLRLYC VSTEALLGDK ILKYFPQITM SLDMLTMIKK MFKVSSQTTR EDDSVTVIFN
LDFIKWNLQM RRNICEPVFS QLGKLFGMEN LFNRTHETFR DSLIYLCSGE GVLSADPVYG
VFPDGTWAWA GDESGKEGLR QKGWTILTVV TIMLIAKRHN VDVSLMGGGD NQVLGITISG
VTRDLQGELI TESASLARRT IKQFTEDLLT TFSDLGLPLK ASETWVSDSL FMYNKHMFYK
GIPLRSPLKA ISRIFPLAND TIMTIDNMIN NISSGVKAAC MKERHGIPLV FMKTLAYRKV
AEGALILHPL TTCFRTPTLP ENGTVTRDGR KRSVKVTRNQ LRSFFTLCMV GSSTMGLPGT
IHLPDMIMRG FPDPLTSHLS FISELVPKIM DPRLASIIAT SGHMSINRMT EYAKLVEDPV
SINHDAPTHG LNEIRQLSRD FLMNTTLAAN THLKSLFTLL DRQREKEFYD ALCSAEELDV
KVLHEVAGAS LFGYTNGIAS RIDQTRTVRA LNETVNVMKR LADAEARYIA YLFARDIHKH
DLIPDQCSRV TADRYRYYSW KKKVLGVTVP HPIEMCQVTS ATQTAFEDAV ICWSDNLSGS
RIYTTMGLGK IYQGSYTKER FKATDIAAAY GNEDILTKAV RLQKLINWRY DEGSSFARII
QLALRAITDA STDGFHRXKE EIKGEFDHRR GISGDISGGI PNFLVTPTSH XSCTTSSWIS
HSRGGKNENI HFQSVLINLL YRAMVYRGSL PGLPEMVWYS KERCSHCIID IVEPSPERTT
PALSEMPSAP NNPFAFIESV NVKLDYHHQV EIEKGMEETN LLNSEWGGSS LTSVDEAGLV
LFLMLIGSRQ VSESFLLLMR EKIEPRPLLQ AALNRVILVR KLGLDRLFPI RNTKCINLIL
GSDRGITACH DGFGLELHGG SWEKGIECDT SFLYNDTHLK PCKLHVNLHL QNVPLQLALA
HASYNPDVCE CLECRAIIED RVSKRMVGQY KSWRCQYHAV LSFSPIIMRV HSERIIKSEG
AIYEGDLHVP YVEEIIALEN SQKLAIDVTS WRLPLLMHAT WESILPQLYI TMKACLVSLP
LEGVIVDDDL ALINLVSKVL VDLRRTIQVY IRAGTFSGSE INNKYDNIRL LPEDLRDSIH
ILTTTDKPDP AATVQLAADD TSPLDCAVYH LIWGDTWGMT RKVHGRILIP SSRVTTGFAG
VMVTDYYATV AVLELAGAVN LWEKKLIDLE HRNNLDVPLS MNRVLAGSRL GTRGIRWAQW
TSPAGLEIVV RKVRAKLSSI SGNPGNAAKW RRNCQKVLKA LMISLYAHSG EDMMRNASGL
VKVNIHGTLS SVTAVCDPSA ESRVQRAQFL FLKEKAPNGP FIXRSRLERR INLLSVVSDL
LG
