L_BEFVB
ID L_BEFVB Reviewed; 2144 AA.
AC Q9E784;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 97.
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 Bovine ephemeral fever virus (strain BB7721) (BEFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Ephemerovirus.
OX NCBI_TaxID=928297;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9970; Syncerus caffer (African buffalo).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11074128; DOI=10.1016/s0168-1702(00)00215-x;
RA Dhillon J., Cowley J.A., Wang Y., Walker P.J.;
RT "RNA polymerase (L) gene and genome terminal sequences of ephemeroviruses
RT bovine ephemeral fever virus and Adelaide River virus indicate a close
RT relationship to vesiculoviruses.";
RL Virus Res. 70:87-95(2000).
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; AF234533; AAG10420.1; -; Genomic_DNA.
DR RefSeq; NP_065409.1; NC_002526.1.
DR SMR; Q9E784; -.
DR GeneID; 911734; -.
DR KEGG; vg:911734; -.
DR Proteomes; UP000008588; 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; 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; Virion.
FT CHAIN 1..2144
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297833"
FT DOMAIN 624..810
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1687..1884
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2144 AA; 249787 MW; 4C6C3E6701D340BC CRC64;
MDSVDFLDSE DHDQNSWNGE EFGDDFLEYI WDQDEEESMD LINNKDYNLN SPLIIDPLVE
LRNWINNEKG HSESDLRSQQ SFEFKEFDII KRVLRNFINN VNLRRPEDSH HIFAKFLNQA
IVTNDYWNLG ETLSKIVEDI REVGASFYRG LDLDENIIID NIRRNWNDVP QLGKSWFLKF
FELHRVICVM NARSNIELKN LQSKNKLKKI KLPKELEERG HKCWIFDLDI SGRWIIFDNY
AYWELQRIVL NREFILMMKD VLISRFQTVL SMNVCTDEYK YTEENIETMM SLYREGDLIL
EEHGNKSYKG LKLLESICNL RLIKIVRKSR PKIPEFPNFE NHIYSSLNDL RVERGIDLSK
FSNIILREES IDMVLAFYSS FRHFGHPWID YLTGLDKLES QVNKDCQVDI QYANLLASDL
AFKILRKNFL EKKCWSVDKN KMDKKHKLYH HISHNTWPTQ QIIDEFGDHW HELPIIQCYE
IPDMIDISQI YSDKSHSLDR SEVLKIIKEQ KHKRIPTKRV LQTLLEKPAT NWPEFLKAVN
DYGLDWEKLV IGLKAKEREL KEEGRFFSLM SYELRDYFVS TEYLIKKYFV PLFEGLTMAD
DLNTVIKKML DVSSGQGTRE YEYITIANNI DYEKWNNYQR IESNGPVFTV MGRFLGLPNL
FTRTHEFFQK SLIYYNQRPD LMMVRGRECL NRLGVKVCWE GQKGGLEGLR QKGWSILNYL
MIERESRVRN TRVKILAQGD NQTISMCYKT ESWQNEEELD NHIKNMVSNN NQIMQAIING
TEKLGLRINL DETMTSADYI NYGKVPIIEG TIKGLPTKRW SRVNFTSNDQ LPSTSTVINS
SSTNALTVGH FSERPHDAIN GHLLFGSLGL LLLDYHNPAI RGQISEFIPE ANINNKLYNI
LLLYLDPSLG GIAGTSLTRF FIRGFPDGVT ESLTFWKIVG EYTNDQDIKR LASTVGSPEL
SPFKPEDLDK LIEKPESLNI KHGLSSSNMI KGEVKKNIIE NCSKIQNEII RDAARNLVSE
ENQLFLWLRT INPLFPRFLS QFAESTYYGV TKSLINLFTN SKTIRGIYKK KYRKELDQLM
IKGEVRSIFG LIKIVNRSKQ FVMPIWDCSA SLADSLRKRS WGKEVLGTTV PHPAEMFKGY
RGGEDSCSFC RGNGSNNNYL TVLMPRGIPM KCHYRGPYYP YLGSNTKEST SILQPWEKET
KVPVLKRACD LRKSINWFVT PDSLLAKSIF NNLKALTGED WEDQIKGYKR TGSSLHRFGC
SRVSSGGFSA SSPSCFTWCI ATTDTMCGLG EVNYDFMFQS TLVWCQMSSI IRERGNLHSK
IHHYHIKCNK CLREIQEPVL ESGWEYQPRN VSQILEKWRP KNMKTWGEEK IHMDIKDNDD
EWDNLTVEDK SYEIGKTIGW LVGDSLLSHK RNYEFKSLFP VSIRYKLEGL PFLEGILDGF
KICGSLNLTH RRNYMILKKP KLALQGTVFF LIDRSSFISE FTNFISHPKI YKAIKSLPHK
IPTSYPMNLS DLGSILRSFL KQLYYRRKEL IIKKSSWVFS DMRTNEVICS FGLSHLTYRI
LIQEGLNKDM KLRLQQCQDL YINIMTESKE ELDKSSAKRE IVECLRELKF VSSEIRHAVK
FRYITGEKGE VQLIKEMEER RTWGDEYTGK ANLLDVWYLT SQSSENKNLV KGIKIPYHSN
PTISGLRINQ IATGAHYKLR TLINMTRITY RDFICGGDGS GGMTSCLLRL KPLSRGVFNS
LLILDDKPLH GTRPSPPTAI MELGEDSLRC VNCYDVWKEP SDLSKQETWK YFVKLKKQNS
MMIDLIVLDM EIINDEVIED IYQNTKNHLI YLLEEGGCLI IKTYLTYLLK ENTNILDMLG
HLFTSVQLIN TNLSSMKTSE IYVLFKNYKN RLTPCLQFDR NIILDNWSFF YINKPIREEF
ERARELLNED LGMGMPKELE PNPLIELSQM LQNSGVDGVA MSAISQEENL SFFSTKELAV
ICLIIISESH LVTTKKHKND CNCLQKKPYS DQEIKSWMSG IIGIGLYLSL LDNKTNSFEI
LDYLINSDFK SIHVNFNKER ELCWSINYSS NEKKGKDLWK KRFSVKDKMA FMGNWIRLLH
RQKVKNQKCE YKEGRINNFL KFINKGLNLQ KVKSQYEEEI AKLL
