ID   L_SENDE                 Reviewed;        2228 AA.
AC   P06829;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Large structural protein;
DE            Short=Protein L;
DE   AltName: Full=Transcriptase;
DE   AltName: Full=Replicase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.56;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.-;
GN   Name=L;
OS   Sendai virus (strain Enders) (SeV).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Paramyxoviridae; Paramyxovirinae; Respirovirus.
OX   NCBI_TaxID=11194;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=36483; Cricetidae sp. (Hamster).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=86317720; PubMed=3019006; DOI=10.1016/0042-6822(86)90427-7;
RA   Morgan E.M., Rakestraw K.M.;
RT   "Sequence of the Sendai virus L gene: open reading frames upstream of
RT   the main coding region suggest that the gene may be polycistronic.";
RL   Virology 154:31-40(1986).
CC   -!- FUNCTION: Displays RNA-directed RNA polymerase, mRNA guanylyl
CC       transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A)
CC       synthetase activities. The viral mRNA guanylyl transferase
CC       displays a different biochemical reaction than the cellular
CC       enzyme. The template is composed of the viral RNA tightly
CC       encapsidated by the nucleoprotein (N). Functions either as
CC       transcriptase or as replicase. The transcriptase synthesizes
CC       subsequently six subgenomic RNAs, assuring their capping and
CC       polyadenylation by a stuttering mechanism. The transcriptase
CC       stutters on a specific sequence, resulting on a cotranscriptional
CC       editing of the phosphoprotein (P) mRNA. The replicase mode is
CC       dependent on intracellular N protein concentration. In this mode,
CC       the polymerase replicates the whole viral genome without
CC       recognizing the transcriptional signals. 5' GpppApGpG sequence is
CC       required for mRNA cap methylation by the enzyme (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBUNIT: Homooligomer. Interacts with the P and C proteins. The L
CC       protein complexes with P protein to form the functional
CC       polymerase. C protein binding to L has an inhibitory effect (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Virion (Potential). Host cytoplasm (By
CC       similarity).
CC   -!- DOMAIN: The N-terminal part (about 1-400) seems to be involved in
CC       binding to the P protein (By similarity).
CC   -!- MISCELLANEOUS: Least abundant structural protein (approximately 50
CC       copies per virion). Unstable in the absence of P protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the paramyxoviruses L protein family.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69579.1; Type=Frameshift; Positions=1, 194;
CC       Sequence=BAA00036.1; Type=Frameshift; Positions=1, 194;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M14887; AAA69579.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; D00053; BAA00036.1; ALT_FRAME; Genomic_RNA.
DR   PIR; A24293; ZLNZSE.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR016269; RNA-dir_RNA_pol_paramyxovir.
DR   InterPro; IPR014023; RNA_pol_cat.
DR   InterPro; IPR001016; RNA_pol_L_viral.
DR   Pfam; PF00946; Paramyx_RNA_pol; 1.
DR   PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN         1   2228       Large structural protein.
FT                                /FTId=PRO_0000142737.
FT   DOMAIN      656    840       RdRp catalytic.
FT   NP_BIND    1801   1810       ATP (Potential).
FT   REGION        1    174       Oligomerization domain (By similarity).
FT   REGION     1756   2228       Involved in mRNA cap methylation (By
FT                                similarity).
FT   COMPBIAS   2031   2034       Poly-Ser.
SQ   SEQUENCE   2228 AA;  252890 MW;  7164A3EBCCB17D8E CRC64;
     MDGQESSQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYRLKDDSII NITKHKIRNG
     GLSPRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL
     TRELSSGFQD LWLNIFKQLG NIEGREGYDP LQDISTIPEI TDKYSRNRWY RPFLTWFSIK
     YDMRWMQKTR PGGPIDTSNS HNLLECKSYT LVTYGDLVMI LNKLTLTGYI LTPELVLMYC
     DVVEGRWNMS AAGHLDKRSI GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ
     LNDPVIPLRG AFMRHVLTEL QTVLTSRDVY TDAEADTIVE SLLAIFHGTS IDEKAEIFSF
     FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLYECHAVF CTIIINGYRE RHGGQWPPCD
     FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR
     KEAWDSVYPD SNLYYKAPES EETRRLIEVF INDENFNPEE IINYVESGDW LKDEKFNISY
     SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF SENGMVKGEI DLLKRLTTLS
     VSGVPRTDSV YNNSKSSEKR NEGMKKKNSG GYWDEKKRSR HEFKATDSST DGYETLSCFL
     TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPIL ERCTIYVGDP YCPVADRMHR
     QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT
     SRVPVAQTYK QKKNHVYEET TKYFGALRHV MFDVGHELKL NETIISSKMF VYSKRIYYDG
     KILPQCLKAL TRCVFWSETL VDENRSACSN ISTSIAKAIE NGYSPILGYC IALYKTCQQV
     CISLGMTINP TISPTVRDQY FKGKNWLRCA VLIPANVGGF NYMSTSRCFV RNIGDPAVAA
     LADLKRFIRA DLLDKQVLYR VMNQEPGDSS FLDWAPDPYS CNLPHSQSIT TIIKNITARS
     VLQESPNPLL SGLFTETSGE EDLNLASFLM DRKVILPRVA HEILGNSLTG VREAIAGMLD
     TTKSLVRASV RKGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL
     RQKMWIHLTY GRPIHGLETP DPLELLRGTF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL
     DTLTNGSPAI RIPYFGSATD ERSEAQLGYV RNLSKPAKAA IRIAMVYTWA YGTDEISWME
     AALIAQTRAN LSLENLKLLT PVSTPTNLSH RLKDTATQMK FSSATLVRAS RFITISNDNM
     ALKEAGESKD TNLVYQQIML TGLSLFEFNM RYKKGSLGKP LILHLHLNNG CCIMESPQEA
     NIPPRSTLDL EITQENNKLI YDPDPLKDVD LELFSKVRDV VHTVDMTYWS DDEVIRATSI
     CTAMTIADTM SQLDRDNLKE MIALVNDDDV NSLITEFMVI DVPLFCSTFG GILVNQFAYS
     LYGLNIRGRE EIWGHVVRIL KDTSHAVLKV LSNALSHPKI FKRFWNAGVV EPVYGPNLSN
     QDKILLALSV CEYSVDLFMH DWQGGVPLEI FICDNDPDVA DMRRSSFLAR HLAYLCSLAE
     ISRDGPRLES MNSLERLESL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK
     VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR
     GYKEITRGEI GRSGVGLTLP FDGRYLSHQL RLFGINSTSC LKALELTYLL SPLVDKDKDR
     LYLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL
     GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNSSIGLVHC DMEGGDHKDD QVVLHEHYSV
     IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLIVLKTSNP ASTEMYLLSR
     HPKSDIIEDS KTVLASLLPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY
     HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMIAFNRVL KDTIFEWARI TESDKRLKLT
     GKYDLYPVRD SGKLKTISRR LVLSWISLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI
     RNLRVITKTL LDRFEDIIHS ITYRFLTKEI KILMKILGAV KMFGARQNEY TTVIDDGSLG
     DIEPYDSS
//