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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)]

 A0A0M4N164_9MONO        Unreviewed;      2183 AA.
A0A0M4N164;
09-DEC-2015, integrated into UniProtKB/TrEMBL.
09-DEC-2015, sequence version 1.
20-DEC-2017, entry version 16.
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:ALE27154.1};
Measles virus genotype D4.
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Morbillivirus.
NCBI_TaxID=170525 {ECO:0000313|EMBL:ALE27154.1, ECO:0000313|Proteomes:UP000129669};
[1] {ECO:0000313|EMBL:ALE27154.1, ECO:0000313|Proteomes:UP000129669}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MVs/London.GBR/19.11/5/[D4] {ECO:0000313|EMBL:ALE27154.1};
PubMed=26569100;
Penedos A.R., Myers R., Hadef B., Aladin F., Brown K.E.;
"Assessment of the Utility of Whole Genome Sequencing of Measles Virus
in the Characterisation of Outbreaks.";
PLoS ONE 10:E0143081-E0143081(2015).
-!- 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|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847043}.
Virion {ECO:0000256|PIRNR:PIRNR000830}.
-!- SIMILARITY: Belongs to the paramyxovirus L protein family.
{ECO:0000256|PIRNR:PIRNR000830}.
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EMBL; KT732225; ALE27154.1; -; Viral_cRNA.
Proteomes; UP000129669; 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:UP000129669};
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, ECO:0000313|EMBL:ALE27154.1};
RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503441, ECO:0000313|EMBL:ALE27154.1};
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,
ECO:0000313|EMBL:ALE27154.1};
Viral RNA replication {ECO:0000256|PIRNR:PIRNR000830,
ECO:0000256|SAAS:SAAS00503417};
Virion {ECO:0000256|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847034}.
DOMAIN 656 840 RdRp catalytic.
{ECO:0000259|PROSITE:PS50526}.
DOMAIN 1755 1958 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000259|PROSITE:PS51590}.
SEQUENCE 2183 AA; 247861 MW; 4A3617DE84E4F4C7 CRC64;
MDSLSVNQIL YPEVHLDSPI VTNKIVAILE YARVPHAYSL EDPTLCQNIK HRLKNGFSNQ
MIINNVEVGN VIKSKLRSYP AHTHIPYPNC NQDLFNIEDK ESTRKIRELL KKGNLLYSKV
SDKVFQCLRD TNSRLGLGSE LREDIKEKII NLGVYMHSSQ WFEPFLFWFT VKTEMRSVIK
SQTHTCHRRR HTPAFFTGSS VELLISRDLV AIISKESQHV YYLTFELVLM YCDVIEGRLM
TETAMTIDAR YTELLGRVRY MWKLIDGFFP ALGNPTYQIV AMLEPLSLAY LQLRDITIEL
RGAFLNHCFT EIHDVLDQNG FSDEGTYHEL IEALDYIFIT DDIHLTGEIF SFFRSFGHPR
LEAVTAAENV RKYMNQPKVI VYETLMKGHA IFCGIIINGY RDRHGGSWPP LTLPLHAADT
IRNAQASGEG LTHEQCVDNW KSFAGVRFGC FMPLSLDSDL TMYLKDKALA ALQREWDSVY
PKEFLRYDPP KGTGSRRLVD VFLNDSSFDP YDMIMYVVSG DYLRDPEFNL SYSLKEKEIK
ETGRLFAKMT YKMRACQVIA ENLISNGIGK YFKDNGMAKD EHDLTKALHT LAVSGVPKDL
KESHRGGPVL KTYSRSPVHT STRNVKAEKG FIGFPHVIRQ DQDTDHPENM EAYETVSAFI
TTDLKKYCLN WRYETISLFA QRLNEIYGLP SFFQWLHKRL ETSVLYVSDP HCPPDLDAHV
PLCKVPNDQI FIKYPMGGIE GYCQKLWTIS TIPYLYLAAY ESGVRIASLV QGDNQTIAVT
KRVPSTWPYN LKKREAARVT RDYFVILRQR LHDIGHHLKA NETIVSSHFF VYSKGIYYDG
LLVSQSLKSI ARCVFWSETI VDETRAACSN IATTMAKSIE RGYDRYLAYS LNVLKVIQQI
LISLGFTINS TMTRDVVIPL LTNNDLLIRM ALLPAPIGGM NYLNMSRLFV RNIGDPVTSS
IADLKRMILA SLMPEETLHQ VMTQQPGDSS FLDWASDPYS ANLVCVQSIT RLLKNITARF
VLIHSPNPML KGLFHDDSKE EDEGLAAFLM DRHIIVPRAA HEILDHSVTG ARESIAGMLD
TTKGLIRASM RKGGLTSRVI TRLSNYDYEQ FRAGMVLLTG RKRNVLIDKE SCSVQLARAL
RSHMWARLAR GRPIYGLEVP DVLESMRGHL IRRHETCVIC ECGSVNYGWF FVPSGCQLDD
IDKETSSLRV PYIGSTTDER TDMKLAFVRA PSRSLRSAVR IATVYSWAYG DDDSSWNEAW
LLARQRANVS LEELRVITPI STSTNLAHRL RDRSTQVKYS GTSLVRVARY TTISNDNLSF
VISDKKVDTN FIYQQGMLLG LGVLETLFRL EKDTGSSNTV LHLHVETDCC VIPMIDHPRI
PSSRKLELRA ELCTNPLIYD NAPLIDRDAT RLYTQSHRRH LVEFVTWSTP QLYHILAKST
ALSMIDLVTK FEKDHMNEIS ALIGDDDINS FITEFLLIEP RLFTIYLGQC AAINWAFDIH
YHRPSGKYQM GELLSSFLSR MSKGVFKVLV NALSHPKIYK KFWHCGIIEP IHGPSLDAQN
LHTTVCNMVY TCYMTYLDLL LNEELEEFTF LLCESDEDVV PDRFDNIQAK HLCVLADLYC
QPGTCPPIRG LRPVEKCAVL TDHIKAEARL SPAGSSWNIN PIIVDHYSCS LTYLRRGSIK
QIRLRVDPGF IFDALADVNV SQPKICSNNI SNMSIKDFRP PHDDVAKLLK DINTSKHNLP
ISGGNLANYE IHAFRRIGLN SSACYKAVEI STLIRRCLEP GEDGLFLGEG SGSMLITYKE
ILKLNKCFYN SGVSANSRSG QRELAPYPSE VGLVEHKMGV GNIVKVLFNG RPEVTWVGSI
DCFNFIVSNI PTSSLGFIHS DIETLPNKDT TEKLEELAAI LSMALLLGKI GSILVIKLMP
FSGDFVQGFI SSVGSHYREV NLVYPRYSNF ISTESYLVMT DLKANRLMNP EKIKQQIIES
SVRTSPGLIG HILSIKQLSC IQAIVGDAVS RGDINPTLKK LTPIEQVLIN CGLAINGPKL
CKELIHHDVA SGQDGLLNSI LILYRELARF KENQRSQQGM FHAYPVLVSS RQRELISRIT
RKFWGHILLY SGNRKLINRF IQNLKSGYLI LDLHQNIFVK NLSKSEKQII MTGGLKREWV
FKVTVKETKE WYKLVGYSAL IKD


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