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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)]

 L_MEASE                 Reviewed;        2183 AA.
P12576;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
23-MAY-2018, entry version 98.
RecName: Full=RNA-directed RNA polymerase L;
Short=Protein L;
AltName: Full=Large structural protein;
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;
Measles virus (strain Edmonston) (MeV) (Subacute sclerose
panencephalitis virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Morbillivirus.
NCBI_TaxID=11235;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2835864; DOI=10.1016/0042-6822(88)90563-6;
Blumberg B.M., Crowley J.C., Silverman J.I., Menonna J., Cook S.D.,
Dowling P.C.;
"Measles virus L protein evidences elements of ancestral RNA
polymerase.";
Virology 164:487-497(1988).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=2596022; DOI=10.1016/0042-6822(89)90554-0;
Cattaneo R., Schmid A., Spielhofer P., Kaelin K., Baczko K.,
Meulen V., Pardowitz J., Flanagan S., Rima B.K., Udem S.A.;
"Mutated and hypermutated genes of persistent measles viruses which
caused lethal human brain diseases.";
Virology 173:415-425(1989).
-!- 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: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: Interacts with the P protein. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
{ECO:0000250}.
-!- SIMILARITY: Belongs to the paramyxovirus L protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M20865; AAA46430.1; -; mRNA.
EMBL; K01711; AAA75501.1; -; Genomic_RNA.
PIR; A28919; ZLNZMV.
PRIDE; P12576; -.
OrthoDB; VOG09000005; -.
Proteomes; UP000000833; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019013; C:viral nucleocapsid; IDA:CACAO.
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.
2: Evidence at transcript level;
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 2183 RNA-directed RNA polymerase L.
/FTId=PRO_0000142729.
DOMAIN 656 840 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 1755 1958 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000255|PROSITE-
ProRule:PRU00923}.
NP_BIND 1785 1794 ATP. {ECO:0000255}.
SEQUENCE 2183 AA; 247648 MW; 1B0B03CA2E2B6EA5 CRC64;
MDSLSVNQIL YPEVHLDSPI VTNKIVAILE YARVPHAYSL EDPTLCQNIK HRLKNGFSNQ
MIINNVEVGN VIKSKLRSYP AHSHIPYPNC NQDLFNIEDK ESTRKIRELL KKGNSLYSKV
SDKVFQCLRD TNSRLGLGSE LREDIKEKVI NLGVYMHSSQ WFEPFLFWFT VKTEMRSVIK
SQTHTCHRRR HTPVFFTGSS VELLISRDLV AIISKESQHV YYLTFELVLM YCDVIEGRLM
TETAMTIDAR YTELLGRVRY MWKLIDGFFP ALGNPTYQIV AMLEPLSLAY LQLRDITVEL
RGAFLNHCFT EIHDVLDQNG FSDEGTYHEL IEALDYIFIT DDIHLTGEIF SFFRSFGHPR
LEAVTAAENV RKYMNQPKVI VYETLMKGHA IFCGIIINGY RDRHGGSWPP LTLPLHAADT
IRNAQASGEG LTHEQCVDNW KSFAGVKFGC FMPLSLDSDL TMYLKDKALA ALQREWDSVY
PKEFLRYDPP KGTGSRRLVD VFLNDSSFDP YDVIMYVVSG AYLHDPEFNL SYSLQEKEIK
ETGRLFAKMT YKMRACQVIA ENLISNGIGK YFKDNGMAKD EQDLTKALHT LAVSGVPKDL
KESHRGGPVL KTYSRSPVHT STRNVRAAKG FIGFPQVIRQ DQDTDHPENM EAYETVSAFI
TTDLKKYCLN WRYETISLFA QRLNEIYGLP SFFQWLHKRL ETSVLYVSDP HCPPDLDAHI
PLYKVPNDQI FIKYPMGGIE GYCQKLWTIS TIPYLYLAAY ESGVRIASLV QGDNQTIAVT
KRVPSTWPYN LKKREAARVT RDYFVILRQR LHDIGHHLKA NETIVSSHFF VYSKGIYYDG
LLVSQSLKSI ARCVFWSETI VDETRAACSN IATTMAKSIE RGYDRYLAYS LNFLKVIQQI
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 AAINWAFDVH
YHRPSGKYQM GELLSSFLSR MSKGVFKVLV NALSHPKIYK KFWHCGIIEP IHGPSLDAQN
LHTTVCNMVY TCYMTYLDLL LNEELEEFTF LLCESDEDVV PDRFDNIQAK HLCVLADLYC
QPGTCPPIQG LRPVEKCAVL TDHIKAEAML SPAGSSWNIN PIIVDHYSCS LTYLRRGSIK
QIRLRVDPGF IFDALAEVNV SQPKIGSNNI SNMSIKAFRP PHDDVAKLLK DINTSKHNLP
ISGGNLANYE IHAFRRIGLN SSACYKAVEI STLIRRCLEP GEDGLFLGEG SGSMLITYKE
ILKLSKCFYN SGVSANSRSG QRELAPYPSE VGLVEHRMGV GNIVKVLFNG RPEVTWVGSV
DCFNFIVSNI PTSSVGFIHS DIETLPDKDT IEKLEELAAI LSMALLLGKI GSILVIKLMP
FSGDFVQGFI SYVGSHYREV NLVYPRYSNF ISTESYLVMT DLKANRLMNP EKIKQQIIES
SVRTSPGLIG HILSIKQLSC IQAIVGDAVS RGDINPTLKK LTPIEQVLIN CGLAINGPKL
CKELIHHDVA SGQDGLLNSI LILYRELARF KDNQRSQQGM FHAYPVLVSS RQRELISRIT
RKFWGHILLY SGNRKLINKF IQNLKSGYLI LDLHQNIFVK NLSKSEKQII MTGGLKREWV
FKVTVKETKE WYKLVGYSAL IKD


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