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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_PI3H4                 Reviewed;        2233 AA.
P12577;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
15-MAR-2017, entry version 95.
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;
Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human
parainfluenza 3 virus (strain NIH 47885)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11217;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE.
PubMed=2841798; DOI=10.1016/0042-6822(88)90594-6;
Galinski M.S., Mink M.A., Pons M.W.;
"Molecular cloning and sequence analysis of the human parainfluenza 3
virus gene encoding the L protein.";
Virology 165:499-510(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
PubMed=2822598; DOI=10.1159/000149722;
Storey D.G., Cote M.-J., Dimock K., Kang C.Y.;
"Nucleotide sequence of the coding and flanking regions of the human
parainfluenza virus 3 hemagglutinin-neuraminidase gene: comparison
with other paramyxoviruses.";
Intervirology 27:69-80(1987).
-!- 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 (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M21649; AAA46854.1; -; Genomic_RNA.
EMBL; M20402; AAA46857.1; -; mRNA.
PIR; B46451; B46451.
PRIDE; P12577; -.
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.
2: Evidence at transcript level;
ATP-binding; 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 2233 RNA-directed RNA polymerase L.
/FTId=PRO_0000142733.
DOMAIN 656 840 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 1775 1982 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000255|PROSITE-
ProRule:PRU00923}.
NP_BIND 1805 1814 ATP. {ECO:0000255}.
CONFLICT 26 26 K -> R (in Ref. 2; AAA46857).
{ECO:0000305}.
SEQUENCE 2233 AA; 255806 MW; DBBB8B5DE74B4638 CRC64;
MDTESNNGTV SDILYPECHL NSPIVKGKIA QLHTIMSLPQ PYDMDDDSIL VITRQKIKLN
KLDKRQRSIR RLKLILTEKV NDLGKYTFIR YPEMSKEMFK LHIPGINSKV TELLLKADRT
YSQMTDGLRD LWINVLSKLA SKNDGSNYDL NEEINNISKV HTTYKSDKWY NPFKTWFTIK
YDMRRLQKAR NEVTFNMGKD YNLLEDQKNF LLIHPELVLI LDKQNYNGYL ITPELVLPYC
DVVEGRWNIS ACAKLDPKLQ SMYQKGNNLW EVIDKLFPIM GEKTFDVISL LEPLALSLIQ
THDPVKQLRG AFLNHVLSEM ELIFESRESI KEFLSVDYID KILDIFNKST IDEIAEIFSF
FRTFGHPPLE ASIAAEKVRK YMYIGKQLKF DTINKCHAIF CTIIINGYRE RHGGQWPPVT
LPDHAHEFII NAYGSNSAIS YENAVDYYQS FIGIKFNKFI EPQLDEDLTI YMKDKALSPK
KSNWDTVSPA SNLLYRTNAS NESRRLVEKF IADSKFDPNQ ILDYVESGDW LDDPEFNISY
SLKEKEIKQE GRLFAKMTYK MRATQVLSET LLANNIGKFF QENGMVKGEI ELLKRLTTIS
ISGVPRYNEV YNNSKSHTDD LKTYNKISNL NLSSNQKSKK FEFKSTDIYN DGYETVSCFL
TTDLKKYCLN WRYESTALFG ETCNQIFGLN KLFNWLHPRL EGSTIYVGDP YCPPSDKEHI
SLEDHPDSGF YVHNPRGGIE GFCQKLWTLI SISAIHLAAV RIGVRVTAMV QGDNQAIAVT
TRVPNNYDYR VKKEIVYKDV VRFFDSLREV MDDLGHELKL NETIISSKMF IYSKRIYYDG
RILPQALKAL SRCVFWSETV IDETRSASSN LATSFAKAIE NGYSPVLGYA CSIFKNIQQL
YIALGMNINP TITQNIKDLY FRNPNWMQYA SLIPASVGGF NYMAMSRCFV RNIGDPSVAA
LADIKRFIKA NLLDRSVLYR IMNQEPGESS FLDWASDPYS CNLPQSQNIT TMIKNITARN
VLQDSPNPLL SGLFTNTMIE EDEELAEFLM DRKVILPRVA HDILDNSLTG IRNAIAGMLD
TTKSLIRVGI NRGGLTYSLL RKISNYDLVQ YETLSRTLRL IVSDKIRYED MCSVDLAIAL
RQKMWIHLSG GRMISGLETP DPLELLSGVI ITGSEHCKIC YSSDGTNPYT WMYLPGNIKI
GSAETGISSL RVPYFGSVTD ERSEAQLGYI KNLSKPAKAA IRIAMIYTWA FGNDEISWME
ASQIAQTRAN FTLDSLKILT PVATSTNLSH RLKDTATQMK FSSTSLIRVS RFITMSNDNM
SIKEANETKD TNLIYQQIML TGLSVFEYLF RLEETTGHNP IVMHLHIEDE CCIKESFNDE
HINPESTLEL IRYPESNEFI YDKDPLKDVD LSKLMVIKDH SYTIDMNYWD DTDIIHAISI
CTAITIADTM SQLDRDNLKE IIVIANDDDI NSLITEFLTL DILVFLKTFG GLLVNQFAYT
LYSLKTEGRD LIWDYIMRTL RDTSHSILKV LSNALSHPKV FKRFWDCGVL NPIYGPNTAS
QDQIKLALSI CEYSLDLFMR EWLNGVSLEI YICDSDMEVA NDRKQAFISR HLSFVCCLAE
IASFGPNLLN LTYLERLDLL KQYLELNIKD DPTLKYVQIS GLLIKSFPST VTYVRKTAIK
YLRIRGISPP EVIDDWDPIE DENMLDNIVK TINDNCNKDN KGNKINNFWG LALKNYQVLK
IRSITSDSDN NDRSDASTGG LTLPQGGNYL SHQLRLFGIN STSCLKALEL SQILMKEVNK
DQDRLFLGEG AGAMLACYDA TLGPAVNYYN SGLNITDVIG QRELKIFPSE VSLVGKKLGN
VTQILNRVKV LFNGNPNSTW IGNMECETLI WSELNDKSIG LVHCDMEGAI GKSEETVLHE
HYSVIRITYL IGDDDVVLIS KIIPTITPNW SRILYLYKLY WKDVSIISLK TSNPASTELY
LISKDAYCTI MEPSEVVLSK LKRLSLLEEN NLLKWIILSK KKNNEWLHHE IKEGERDYGV
MRPYHMALQI FGFQINLNHL AKEFLSTPDL TNINNIIQSF QRTIKDVLFE WINITHDGKR
HKLGGRYNIF PLKNKGKLRL LSRRLVLSWI SLSLSTRLLT GRFPDEKFEH RAQTGYVSLP
DTDLESLKLL SKNTIKNYRE CIGSISYWFL TKEVKILMKL IGGAKLLGIP RQYKEPEEQL
LEDYNQHDEF DID


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