L_EBLV1
ID L_EBLV1 Reviewed; 2127 AA.
AC A4UHQ2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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 European bat lyssavirus 1 (strain Bat/Germany/RV9/1968) (EBLV1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=453115;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17374776; DOI=10.1099/vir.0.82692-0;
RA Marston D.A., McElhinney L.M., Johnson N., Muller T., Conzelmann K.K.,
RA Tordo N., Fooks A.R.;
RT "Comparative analysis of the full genome sequence of European bat
RT lyssavirus type 1 and type 2 with other lyssaviruses and evidence for a
RT conserved transcription termination and polyadenylation motif in the G-L 3'
RT non-translated region.";
RL J. Gen. Virol. 88:1302-1314(2007).
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; EF157976; ABO65247.1; -; Genomic_RNA.
DR RefSeq; YP_001285392.1; NC_009527.1.
DR SMR; A4UHQ2; -.
DR GeneID; 5219906; -.
DR KEGG; vg:5219906; -.
DR Proteomes; UP000008926; 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:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
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..2127
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297834"
FT DOMAIN 611..799
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1674..1871
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2127 AA; 242548 MW; D26808658BFD089E CRC64;
MIDSTEVYDD PVDPVEPEAD LRSNSVVPNI LRNSDYNLNS PLLEDPSRLM IEWLTTGNRP
SRLNLTDNLL RSYKVLRGYF KKLDVGSMRA GGLGAQAMIT LWLHGSHSES TRSRKCLTEL
SQFYKKSSPI EKLLNYTLEN RGLKTPTEGV LSSINKVQYD QAFGRYLGNT YSSYLFFHVI
ILYMNALDWD EEKTILALWK EIASIDVKSD LVKFRDQIWG SLVITKDFVY SQSANCLFDR
NYTLMLKDLF LSRFNSLLIL ISPPESRYSD DLVSNLCQLY IAGDKVLSAC GNSGYDVIKL
LEPYIVNKLV QKAEKFRPLI HSLGDFPQFI RDKTNQLEGT FGPSAREFFQ TMDLLDNIHD
LVFVYGCYRH WGHPYIDYRK GLSKLYDQVH VKKIIDRNYQ ECLASDLAKR ILRWGFDKYS
RWYLDSNLLP GDHPLSPYVK TQTWPPKHVV DMVGDTWHSL PITQIFEIPE SMDPSEILDD
KSHSFTRTRL ASWLSENRGG PVPSEKVIIT ALSRPPVNPR EFLRSIDVGG LPDDDLIIGL
KPKERELKIE GRFFALMSWN LRLYFVITEK LLATYILPLF DALTMTDNLN KVFKKLIDRV
TGQGLLDYSR VTYAFHLDYE KWNNHQRLES TKDVFSVLDK VFGLKKVFSR THEFFQKSWV
YYSDRSDLIG LWRDQIYCLD MTNGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQTRNT
RTKILAQGDN QVLCPTYMLS SGLNKEGLLY ELDSISRNAI SIYRAIEDGA SKLGLIIKKE
ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCISNDQI VNLANIMSTV STNALTVAQH
SQSLIKPMRD FLLMSVQAVY HYLLFSPILK DRVYKILVAD GTEFLLAMSR IIYLDPSLGG
VSGMSLGRFH IRQFSDPVSE GLSFWREIWL SSSESWIHAL CQEAGNPDLG DRSLESFTRL
LEDPTTLNIR GGASPTILLR EAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLRSV
EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRRS LSRTLEESFF NSEIHGISRM
TQVPQRIGRV WSCSAERADQ LREISWGRKV VGTTVPHPSE MLALIPKSSI SCTCGQSGDD
SPRISVSVLP SLDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
WFITRDSNLA QTLIRNIVSL TGPFFPLEEA PVFKRTGSAL HRFKSARYSE GGYSSICPNL
LSHISVSTDT MSDLTQDGTN FDFMFQPLML YAQTWTSELV QKDLRLRDST FHWHLRCLKC
IRPIDDITLE APKIFSFPDV SKRISRMVSG AVPQFRKLPE IGLKPGKFDS LKEKDKSRHI
GTAQGLLYSI LVATHDSGYN DGTIFPVNIY GKVSPRDYLR GLARGVLIGS SICFLTRMTN
ININRPLELI SGVISYILLR LDNHPSLYVM LKEPSLRSEI FSIPQKIPAA YPTTMKEGNR
SVLCYLQHVL RYEREAITTS PENDWLWIFS DFRSIKMTYL TLITYQSHLL LQRIDRNLSK
QMRVRLRQLN SLMRQVLGGH GEGTLDSDED IQGLLRDALQ RTRWVDQEVR HAAKTMKCDY
SPSKRVSRKA GCSEWICSAQ QVAVSTSSNP APISEIDIRA LSKKLQNPLI SGLRVVQWAT
GAHYKLKPIL NDLEAYPTLC LVVGDGSGGI SRAVLSMFPD AKLVFNSLLE VNDLMASGTH
PLPPSALMSG GEDIVSRVID FNSIWEKPSD LRNPSTWRYF QTVQSAANMS YDLIICDAEV
TDIPSINKIT LLMSDFSLSI NGPLSLIFKT YGTMLVNPDY KAVQHLSRAF PSVTGYITQM
TSSFSSELYL KFSKRGKFFR DSEYLTSSTL REMSLVLFNC SSSKSEMLRA RSLNYQDLVR
GFPEEIISNP YNEMIITLID NDVESFLVHK MVDDLELRQG AFSKMSIILT IMMVFSNRVF
NVSKPLNDPK FYPPSDPKIL RHFNICCGTL IYLSAALGDV LNFARLHELY NNPVTYYFKK
QTLGGRMYLA WSWTDNTPVF KRVACNSSLS LSSHWIRLIY KIVKTTRLVG SAKDLSQEVE
KHLKSYNRWI NFSDLRSRSS LLDYSCL
