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RNA-directed RNA polymerase L (Protein L) (Large structural protein) (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)]

 D0FH34_9MONO            Unreviewed;      2204 AA.
D0FH34;
24-NOV-2009, integrated into UniProtKB/TrEMBL.
24-NOV-2009, sequence version 1.
30-AUG-2017, entry version 54.
RecName: Full=RNA-directed RNA polymerase L {ECO:0000256|PIRNR:PIRNR000830};
Short=Protein L {ECO:0000256|PIRNR:PIRNR000830};
AltName: Full=Large structural protein {ECO:0000256|PIRNR:PIRNR000830};
AltName: Full=Replicase {ECO:0000256|PIRNR:PIRNR000830};
AltName: Full=Transcriptase {ECO:0000256|PIRNR:PIRNR000830};
Includes:
RecName: Full=RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830};
EC=2.7.7.48 {ECO:0000256|PIRNR:PIRNR000830};
Includes:
RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|PIRNR:PIRNR000830};
EC=2.1.1.56 {ECO:0000256|PIRNR:PIRNR000830};
Includes:
RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830};
EC=2.7.7.88 {ECO:0000256|PIRNR:PIRNR000830};
Includes:
RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|PIRNR:PIRNR000830};
EC=2.1.1.296 {ECO:0000256|PIRNR:PIRNR000830};
Name=L {ECO:0000313|EMBL:ACW83058.1};
Avian avulavirus 1.
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Avulavirus.
NCBI_TaxID=11176 {ECO:0000313|EMBL:ACW83058.1, ECO:0000313|Proteomes:UP000114204};
[1] {ECO:0000313|EMBL:ACW83058.1, ECO:0000313|Proteomes:UP000114204}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=QG/Hebei/07 {ECO:0000313|EMBL:ACW83058.1};
PubMed=20363269; DOI=10.1016/j.virusres.2010.03.015;
Zhang R., Wang X., Su J., Zhao J., Zhang G.;
"Isolation and analysis of two naturally-occurring multi-recombination
Newcastle disease viruses in China.";
Virus Res. 151:45-53(2010).
-!- 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 activities 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:0000256|PIRNR:PIRNR000830}.
-!- CATALYTIC ACTIVITY: 5'-triphospho-mRNA + GDP = diphosphate +
guanosine 5'-triphospho-mRNA. {ECO:0000256|PIRNR:PIRNR000830}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00361115}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000256|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847042}.
-!- 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:0000256|PIRNR:PIRNR000830}.
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000256|SAAS:SAAS00847043}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|PIRNR:PIRNR000830}. Host
cytoplasm {ECO:0000256|PIRNR:PIRNR000830}.
-!- SIMILARITY: Belongs to the paramyxovirus L protein family.
{ECO:0000256|PIRNR:PIRNR000830}.
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EMBL; GQ994434; ACW83058.1; -; Viral_cRNA.
Proteomes; UP000114204; 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.
InterPro; IPR026890; Mononeg_mRNAcap.
InterPro; IPR014023; Mononeg_RNA_pol_cat.
InterPro; IPR025786; Mononega_L_MeTrfase.
InterPro; IPR016269; RNA-dir_pol_paramyxovirus.
InterPro; IPR024352; RNA-pol_paramyxovirus_C_dom.
Pfam; PF12803; G-7-MTase; 1.
Pfam; PF14318; Mononeg_mRNAcap; 1.
Pfam; PF00946; Mononeg_RNA_pol; 1.
PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 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 {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503432};
Complete proteome {ECO:0000313|Proteomes:UP000114204};
Host cytoplasm {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00847045};
Methyltransferase {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00847038};
mRNA capping {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503423};
mRNA processing {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503423};
Multifunctional enzyme {ECO:0000256|SAAS:SAAS00503427};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503432};
Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503441};
RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503441};
S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503438};
Transferase {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503441, ECO:0000256|SAAS:SAAS00847038};
Viral RNA replication {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503417};
Virion {ECO:0000256|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847034}.
DOMAIN 634 818 RdRp catalytic.
{ECO:0000259|PROSITE:PS50526}.
DOMAIN 1745 1958 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000259|PROSITE:PS51590}.
SEQUENCE 2204 AA; 248136 MW; 125362D709C67C00 CRC64;
MAGSGPERAE HQIILPESHL SSPLVKHKLL YYWKLTGHPL PDECDFDHLI ISRQWKRILE
SATPDTERMI KLGRAVHQTL NHNSKITGVL HPRCLVELAS IEVPDSTNKF RKIEKKIQIH
NTRYGDLFTK LCTHVEKKLL GSSRSNNVPR SEEFSSIRTD PAFWFHSKWS RAKFASLHIK
QVQRHLIVAA RTRSAVNKLV TLNHKIGHVF VTPELVIVTH TDENKFTCLT QELVLMYADM
MEGRDMVNII SSTAAHLRNL SEKIDDILRL VDALAKDLGN QVYDVVALME GFAYGAVQLL
EPSGTFAGDF FAFNLQELKD TLIELLPNNI AESVTHAIAT VFSGLEQNQA AEMLCLLRLW
GHPLLESRSA ARAVRSQMCA PKMVDFDMIL QVLSFFKGTI INGYRKKNSG VWPRVKVDTI
YGNIIGQLHA DSAEISHDVM LREYKSLSAL GFEPCIDYDP VTNLSMFLKD KAIAHPSDNW
LASFRRNLLS EDQKKQTKEA TSTNRLLIEF LESNDFDPYK EMEYLTTLEY LRDDSVAVSY
SLKEKEVKVN GRIFAKLTKK LRNCQVMAEG ILADQIAPFF QGNGVIQDSI SLTKSMLAMS
QLSFNSNKKR ITGCKERVSS DRNHDPKSKN RRRVATFIST DLQTYCLNWR YQTVKLFAHT
INQLMGLPHF FEWIHLRLMD TTMFVGDPFN GPSDPTDCDL SRVPNDDIYI VSARGGIEGL
CQKLWTMISI AAIQLAAARS HCRVACMVQG DNQVIAVTRE VRSDDSPDMV LTQLHQASDN
FFKELIHVNH LIGHNLKDRE TIRSDTFFIY SKRIFKDGTI LSQVLKNSSK LVLISGDLSE
NTVMSCANIA STVARLCENG LPKDFCYYLN YLMSCMQTYF DSEFSITHSS QSDSNQCWIE
DISFVHSYVL TPAQLGGLSN LQYSRLYTRN IGDPGTTAFA EVKRLEAVGL LSPSIMTNIL
TRPPGNGDWA SVCNDPYSFN FETVASPNIV LKKHTQKVLF ETCSNPLLSG VHTEDNEAEE
KALAEFLLNQ EVIHPRVAHA IMEASSVGRR KQIQGLVDTT NTVIKIALTR RPLGIKRLMR
IINYSSMHAM LFRDDIFLSN RSNHPLVSSN MCSLTLADYA RNRSWSPLTG GRKILGVSNP
DTIELVEGEI LSVSGGCTKC DSGDEQFTWF HLPSNIELTD DTSKNPPMRV PYLGSKTQER
RAASLAKIAH MSPHVKAALR ASSVLIWAYG DNEVNWTAAL NIARSRCNIS SEYLRLLSPL
PTAGNLQHRL DDGITQMTFT PASLYRVSPY VHISNDSQRL FTEEGVKEGN VVYQQIMLLG
LSLIESLFPM TTTRTYDEIT LHLHSKFSCC IREAPVAVPF ELFRLALELR TVPSQKVLYD
PSPISERDFA RLDLAIFKSY ELNLESYSTL ELMNILSISS GKLIGQSVVS YDEDTSIKND
AIIVYDNTRN WISEAQNSDV VRLFEYAALE VLLDCAYQLY YLRVRGANNI VLYMNDLYKN
MPGILLSNIA ATISHPLIHS RLNAVGLINH DGSHQLADID FVEVSAKLLV SCTRRVVSGL
YAGNKYDLLF PSVLDDNLSE KMLQLISRLC CLYTVLFATT REIPKIRGLS AEEKCSILTE
YLLSDAVKPL LRSEQLSSIM SPNIITFPAN LYYMSRKSLN LIREREDRDT ILSLLFPQEP
LLELRPVRDI GARVKDPFTR QPASFIQELD LSAPARYDAF TLSKVCFEHT LPNPKEDYLV
RYLFRGIGTA SSSWYKASHL LSVSEVRCAR HGNSLYLAEG SGAIMSLLEL HIPHETIYYN
TLFSNEMNPP QRHFGPTPTQ FLNSVVYRNL QAEVPCKDGY VQEFYPLWRE NAEESDLTSD
KAVGYITSVV PYRSVSLLHC DIEIPPGSSQ SLLDQLATNL SLIAMHSVRE GGVVIIKVLY
AMGYYFHLLM NLFTPCSTKG YILSNGYACR GDMECYLIFV MGCLGGPTFV HEVVRMAKTL
IQRHGTLLSK SDEITLTKLF TSQQRRVTDL LSSPLPKLMK LLSENIDAAL IEAGGQPVRP
FCAESLVSTL TNMTQTTLII ASHIDTVIRS VIYMEAEGDL ADTVFLFTPY NLSTDGKKRT
SLKQCTKQIL EVTILGLRAK DINKVGDVIS LVLRGAVSLE DLIPLRTYLK HSTCPKYLKA
VLGITKLKEM FTDTSLLYLT RAQQKFYMKT IGNAAKGYYS NNDS


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