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Large structural protein (Protein L) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]

 L_RABVE                 Reviewed;        2127 AA.
A3F5L9;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 1.
15-MAR-2017, entry version 48.
RecName: Full=Large structural protein;
Short=Protein L;
AltName: Full=Replicase;
AltName: Full=Transcriptase;
Includes:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48 {ECO:0000250|UniProtKB:P03523};
Includes:
RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
EC=2.1.1.56 {ECO:0000250|UniProtKB:P03523};
Includes:
RecName: Full=GDP polyribonucleotidyltransferase;
EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
Includes:
RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2;
EC=2.1.1.296 {ECO:0000250|UniProtKB:P03523};
Name=L;
Rabies virus (strain ERA) (RABV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Rhabdoviridae; Lyssavirus.
NCBI_TaxID=11295;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=40674; Mammalia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R.,
Peterhans E., Cox J., Mueller T.;
"Complete nucleotide sequencing of SAD derivatives of attenuated
rabies virus vaccine strains.";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: RNA-directed RNA polymerase that catalyzes the
transcription of viral mRNAs, their capping and polyadenylation.
The template is composed of the viral RNA tightly encapsidated by
the nucleoprotein (N). The viral polymerase binds to the genomic
RNA at the 3' leader promoter, and transcribes subsequently all
viral mRNAs with a decreasing efficiency. The first gene is the
most transcribed, and the last the least transcribed. The viral
phosphoprotein acts as a processivity factor. Capping is
concommitant with initiation of mRNA transcription. Indeed, a GDP
polyribonucleotidyl transferase (PRNTase) adds the cap structure
when the nascent RNA chain length has reached few nucleotides.
Ribose 2'-O methylation of viral mRNA cap precedes and facilitates
subsequent guanine-N-7 methylation, both acticities being carried
by the viral polymerase. Polyadenylation of mRNAs occur by a
stuttering mechanism at a slipery stop site present at the end
viral genes. After finishing transcription of a mRNA, the
polymerase can resume transcription of the downstream gene.
{ECO:0000250|UniProtKB:P03523}.
-!- FUNCTION: RNA-directed RNA polymerase that catalyzes the
replication of viral genomic RNA. The template is composed of the
viral RNA tightly encapsidated by the nucleoprotein (N). The
replicase mode is dependent on intracellular N protein
concentration. In this mode, the polymerase replicates the whole
viral genome without recognizing transcriptional signals, and the
replicated genome is not caped or polyadenylated.
{ECO:0000250|UniProtKB:P03523}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000250|UniProtKB:P03523}.
-!- CATALYTIC ACTIVITY: 5'-triphospho-mRNA + GDP = diphosphate +
guanosine 5'-triphospho-mRNA. {ECO:0000250|UniProtKB:P03523}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-
(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-
methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-
ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA].
{ECO:0000250|UniProtKB:P03523}.
-!- SUBUNIT: May form homodimer. Interacts with the P protein.
{ECO:0000250|UniProtKB:P03523}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are
packaged asymmetrically towards the blunt end of the virus.
{ECO:0000250|UniProtKB:P03523}.
-!- SIMILARITY: Belongs to the rhabdoviruses protein L family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; EF206707; ABN11295.1; -; Viral_cRNA.
OrthoDB; VOG09000005; -.
Proteomes; UP000008619; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
InterPro; IPR026890; Mononeg_mRNAcap.
InterPro; IPR014023; Mononeg_RNA_pol_cat.
InterPro; IPR025786; Mononega_L_MeTrfase.
InterPro; IPR017234; RNA-dir_pol_rhabdovirus.
Pfam; PF14318; Mononeg_mRNAcap; 1.
Pfam; PF00946; Mononeg_RNA_pol; 1.
PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 1.
TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PROSITE; PS51590; SAM_MT_MNV_L; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Host cytoplasm; Methyltransferase;
mRNA capping; mRNA processing; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase;
RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
Viral RNA replication; Virion.
CHAIN 1 2127 Large structural protein.
/FTId=PRO_0000294420.
DOMAIN 611 799 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 1674 1871 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000255|PROSITE-
ProRule:PRU00923}.
REGION 1562 2127 Interaction with P protein.
{ECO:0000250}.
SEQUENCE 2127 AA; 243070 MW; BAA9B514E59B6115 CRC64;
MLDPGEVYDD PIDPIELEDE PRGTPTVPNI LRNSDYNLNS PLIEDPARLM LEWLKTGNRP
YRMTLTDNCS RSFRVLKDYF KKVDLGSLKV GGMAAQSMIS LWLYGAHSES NRSRRCITDL
AHFYSKSSPI EKLLNLTLGN RGLRIPPEGV LSCLERVDYD NAFGRYLANT YSSYLFFHVI
TLYMNALDWD EEKTILALWK DLTSVDIGKD LVKFKDQIWG LLIVTKDFVY SQSSNCLFDR
NYTLMLKDLF LSRFNSLMVL LSPPEPRYSD DLISQLCQLY IAGDQVLSMC GNSGYEVIKI
LEPYVVNSLV QRAEKFRPLI HSLGDFPVFI KDKVSQLEET FGPCARRFFR ALDQFDNIHD
LVFVYGCYRH WGHPYIDYRK GLSKLYDQVH IKKVIDKSYQ ECLASDLARR ILRWGFDKYS
KWYLDSRFLA RDHPLTPYIK TQTWPPKHIV DLVGDTWHKL PITQIFEIPE SMDPSEILDD
KSHSFTRTRL ASWLSENRGG PVPSEKVIIT ALSKPPVNPR EFLRSIDLGG LPDEDLIIGL
KPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
TGQGLLDYSR VTYAFHLDYE KWNNHQRLES TEDVFSVLDQ VFGLKRVFSR THEFFQKAWI
YYSDRSDLIG LREDQIYCLD ASNGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQIRNT
RTKILAQGDN QVLCPTYMLS PGLSQEGLLY ELERISRNAL SIYRAVEEGA SKLGLIIKKE
ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCVSNDQI VNLANIMSTV STNALTVAQH
SQSLIKPMRD FLLMSVQAVF HYLLFSPILK GRVYKILSAE GDSFLLAMSR IIYLDPSLGG
VSGMSLGRFH IRQFSDPVSE GLSFWREIWL SSHESWIHAL CQEAGNPDLG ERTLESFTRL
LEDPTTLNIR GGASPTILLK DAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLTSV
EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRKS LSKTLEESFY NSEIHGISRM
TQTPQRVGGV WPCSSERADL LREISWGRKV VGTTVPHPSE MLGLLPKSSI SCTCGATGGG
NPRVSVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
WFITRDSNLA QALIRNIMSL TGPDFPLEEA PVFKRTGSAL HRFKSARYSE GGYSSVCPNL
LSHISVSTDT MSDLTQDGKN YDFMFQPLML YAQTWTSELV QRDTRLRDST FHWHLRCNRC
VRPIDDVTLE TSQIFEFPDV SKRISRMVSG AVPHFQRLPD IRLRPGDFES LSGREKSHHI
GSAQGLLYSI LVAIHDSGYN DGTIFPVNIY GKVSPRDYLR GLARGVLIGS SICFLTRMTN
ININRPLELI SGVISYILLR LDNHPSLYIM LREPSLRGEI FSIPQKIPAA YPTTMKEGNR
SILCYLQHVL RYEREIITAS PENDWLWIFS DFRSAKMTYL TLITYQSHLL LQRVERNLSK
SMRDNLRQLS SLMRQVLGGH GEDTLESDDN IQRLLKDSLR RTRWVDQEVR HAARTMTGDY
SPNKKVSRKV GCSEWVCSAQ QVAVSTSANP APVSELDIRA LSKRFQNPLI SGLRVVQWAT
GAHYKLKPIL DDLNVFPSLC LVVGDGSGGI SRAVLNMFPD AKLVFNSLLE VNDLMASGTH
PLPPSAIMRG GNDIVSRVID FDSIWEKPSD LRNLATWKYF QSVQKQVNMS YDLIICDAEV
TDIASINRIT LLMSDFALSI DGPLYLVFKT YGTMLVNPNY KAIQHLSRAF PSVTGFITQV
TSSFSSELYL RFSKRGKFFR DAEYLTSSTL REMSLVLFNC SSPKSEMQRA RSLNYQDLVR
GFPEEIISNP YNEMIITLID SDVESFLVHK MVDDLELQRG TLSKVAIIIA IMIVFSNRVF
NVSKPLTDPL FYPPSDPKIL RHFNICCSTM MYLSTALGDV PSFARLHDLY NRPITYYFRK
QFIRGNVYLS WSWSNDTSVF KRVACNSGLS LSSHWIRLIY KIVKTTRLVG SIKDLSREVE
RHLHRYNRWI TLEDIRSRSS LLDYSCL


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