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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_RABVB                 Reviewed;        2128 AA.
Q66T60;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
15-MAR-2017, entry version 57.
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 silver-haired bat-associated) (RABV) (SHBRV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Rhabdoviridae; Lyssavirus.
NCBI_TaxID=445793;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=40674; Mammalia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15520387; DOI=10.1073/pnas.0407289101;
Faber M., Pulmanausahakul R., Nagao K., Prosniak M., Rice A.B.,
Koprowski H., Schnell M.J., Dietzschold B.;
"Identification of viral genomic elements responsible for rabies virus
neuroinvasiveness.";
Proc. Natl. Acad. Sci. U.S.A. 101:16328-16332(2004).
-!- 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; AY705373; AAU11519.1; -; Genomic_RNA.
OrthoDB; VOG09000005; -.
Proteomes; UP000006845; 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 2128 Large structural protein.
/FTId=PRO_0000294418.
DOMAIN 612 800 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 1675 1872 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000255|PROSITE-
ProRule:PRU00923}.
REGION 1563 2128 Interaction with P protein.
{ECO:0000250}.
SEQUENCE 2128 AA; 243090 MW; A039BB2078B76EFD CRC64;
MMIDPGEVYD DPIDLIESEA EPKGNPTIPN ILRNSDYNLN SPLIEDPARL MLEWLKTGNR
PLRMTLTDNC SRSHKVLKDY FKRVDLGSLK VGGAAAQSMI SLWLYGAHSE SNRSRKCIND
LAQFYYKSSP IEKLLNCTLG NRGLKTPPEG VLSCLARVDY DKAFGRYLAN IYSSYLFFHV
ITLYMNALDW DEEKTILALW RDITSIDTGK DLVKFKDQIW GLLIVTKDFV YSQSTGCLFD
RNYTLMLKDL FLSRFNSLMI LLSPPEPRYS DDLISQLCQL YIAGDQVLSM CGNSGYEVIK
ILEPYVVNSL VQRAEKFRPL IHSLGDFPTF IRDKVGQLEG TFGPSAKRFF KVLDQFDNIH
DLVFVYGCYR HWGHPYIDYR KGLSKLYDQV HLKKVIDKSY QECLASDLAR RILRWGFDKY
SKWYLDSRLL SRDHPLIPYI KTQTWPPRHI VDLVGDTWHK LPITQIFEIP ESMDPSEILD
DKSHSFTRTR LASWLSENRG GPVPSEKVII TALSKPPVNP REFLKSIDLG GLPDEDLIIG
LKPKERELKI EGRFFALMSW NLRLYFVITE KLLANYILPL FDALTMTDNL NKVFKKLIDR
VTGQGLLDYS RVTYAFRLDY EKWNNHQRLE STEDVFSVLD QVFGLKRVFS RTHEFFQRSW
IYYSDRSDLI GLWEDQIYCL DMSDGPTCWN GQDGGLEGLR QKGWSLVSLL MIDRESQTRN
TRTKILAQGD NQVLCPTYML SPGLSREGLL YELESISRNA LSIYRAIEEG ASKLGLIIKK
EETMCSYDFL IYGKTPLFRG NILVPESKRW ARVSCISNDQ IVNLANTMST VSTNALTVAQ
HSQSLIKPMR DFLLMSVQAV FHYLLFSPIL KGRVYKILSA EGDNFLLAMS RIIYLDPSLG
GVSGMSLGRF HIRQFSDPVS EGLSFWREIW LSSNESWIHA LCQEAGNPDL GERTLESFTR
LLEDPTTLNI KGGASPTILL KDAIRKALYD EVDEVENSEF REAILLSKTH RDNFILFLKS
IEPLFPRFLS ELFSSSFLGI PESIIGLIQN SRTIRRQFRR SLSRTLEESF YNSETHGINR
MTQTPQRVGR VWPCSSERAD LLREISWGRK VVGTTVPHPS EMLGLIPKSS ISCTCGAAGG
GNPRISVSVL PSFDQSFFSR GPLKGYLGSS TSMSTQLFHA WEKVTNVHVV KRALSLKESI
NWFITRNSNR AQTLIRNIMS LTGPDFPLEE APVFKRTGSA LHRFKSARYS EGGYSSVCPN
LLSHISVSTD TMSDLTQDGR NYDFMFQPLM LYAQTWTSEL VQKDTRLKDS TFHWHLRCNK
CIRPIDDMTL DTSQVFEFPD VSRRISRMVS GAVPHFRKLP DIRLRPGDFE SLSGKEKSRH
IGSAQGLLYS ILVAIHDSGY NDGTIFPVNI YSKVSPRDYL RGLARGVLIG SSICFLTRMT
NININRPLEL ISGVISYILL RLDNHPSLYI MLREPSLRGE IFSIPQKVPA AYPTTMKEGN
RSILCYLQHV LRYEREAITA SPENDWLWIF SDFRSSKMTY LTLITYQSHL LLQRVDKNLS
KSMRANLRQM SSLMRQVLGG HGEDTLESDE DIQRLLKDSL RRTRWVDQEV RHAARTMTGS
YSPHRRVSRK AGCSEWVCSA QQVAVSTSAN PAPASELDIR TLSRRLQNPL ISGLRVVQWA
TGAHYKLKPI LDDLNVFPSL CLVVGDGSGG ISRAVLNMFP DARLVFNSLL EVNDLMASGT
HPLPPSAIMS GGDDIISRVI DFDSIWEKPS DLRNLTTWRY FQSVQEQVNM SYDLIICDAE
VTDIASINRI TLLMSDFALS IDGPLYLVFK TYGTMLVNPD YRAIQHLSRA FPAVTGFITQ
MTSSFSSELY LRFSKRGKFF RDAEYLTSST LREMSLVLFN CSSPKSEMQR ARSLNYQDLV
RGFPDEVISN PYNEMIITLI DSDVESFLVH KMVDDLELQR GTLSKVSIII AIMIVFSNRV
FNVSKPLTDP LFYPPFDPKI LRHFNICCST MMYLSTALGD VPSFARLHDL YNRPITYYFR
KQVIRGNIYL SWSWSDDTSV FKRVACNSSL SLSSHWIRLI YKIVKTTRLV GSIEDLSGEI
EKHLRGYNRW ITLDDIRSRS SLLDYSCL


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