ID   L_SENDO                 Reviewed;        2228 AA.
AC   O55528; O55530;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 50.
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 Ohita) (SeV).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Paramyxoviridae; Paramyxovirinae; Respirovirus.
OX   NCBI_TaxID=302272;
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].
RC   STRAIN=Isolate M1, and Isolate MVC11;
RX   MEDLINE=98062143; PubMed=9400971;
RA   Itoh M., Isegawa Y., Hotta H., Homma M.;
RT   "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT   mutations from a highly virulent field strain through adaptation to
RT   LLC-MK2 cells.";
RL   J. Gen. Virol. 78:3207-3215(1997).
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.
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DR   EMBL; AB005795; BAA24392.1; -; Genomic_RNA.
DR   EMBL; AB005796; BAA24401.1; -; Genomic_RNA.
DR   RefSeq; NP_056879.1; -.
DR   GeneID; 1489777; -.
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; Complete proteome; Cytoplasm; Methyltransferase;
KW   mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA replication;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW   Virion.
FT   CHAIN         1   2228       Large structural protein.
FT                                /FTId=PRO_0000142739.
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.
FT   VARIANT    2050   2050       E -> A (in avirulent isolate MVC11).
SQ   SEQUENCE   2228 AA;  253061 MW;  9BDAC6F266B13B1F CRC64;
     MDGQESTQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYILKDDSII NITKHKIRNG
     GLSLRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL
     TKELSNGFQD LWLNIFKQLG NIEGREGYDP LQDISTIPEI TERYSRNKWY RPFLTWFSIK
     YDMRWMQKTR PGGPLDTSNS HNLLECKSYT LVTYGDLVMI LNKSTLTGYI LTPELVLMYC
     DVVEGRWNMS AAGQLDKRST GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ
     LSDPVIPLRG AFMRHVLTEL QTVLTSKDVY TDPEADAIVE SLLAIFHGTS IDEKAEIFSF
     FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLHECHAVF CTIIINGYRE RHGGQWPPCD
     FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR
     KEAWDSVYPD SNLYYKVPES EETRRLIEVF INDENFNPED IIDYVESGDW LKDEKFNISY
     SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF SENGMVKGEI DLLKRLTTLS
     VSGVPRTDSV YNNPRSSEKR NESMKKRNSK GYWDEKKRSR HEFKATDSST DGYETLSCFL
     TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPVL EKCTIYVGDP YCPVADRMHR
     QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT
     SRVPVAQTYK QKKNHVYEEI TRYFGALRHV MFDIGHELKL NETIISSKMF VYSKRIYYDG
     KILPQCLKAL TRCVFWSETL VDENRSACSN ISTSIAKAIE NGYSPILGYC IALYKTCQQV
     CISLGMTINP TISPTVRDQY FKGKNWLRCA VLIPANVGGF NYMSTSRCFV RNIGDPAVAA
     LADLKRFIRA DLLDKQVLYR VMNQEPGDSS FLDWASDPYS CNLPHSQSIT TIIKNITARS
     VLQESPNPLL SGLFTETSGE EDLNLASFLM DRKVILPRVA HEILSNSLTG VREAIAGMLD
     TTKSLVRASV KRGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL
     RQKMWIHLTY GRPIHGLETP DPLELLRGTF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL
     DTLTNGSPAI RIPYFGSATD ERSEAQLGYV RNLSKPAKAA IRIAMVYTWA YGTDEISWME
     AALIAQTRAN LSLENLKLLT PVSTSTNLSH RLKDTATQMK FSSATLVRAS RFITISNDNM
     ALKEAGESKD TNLVYQQIML TGLSLFEFNM RYKKGSLEKP LILHLHLNNG CCIMESPQEA
     NIPPRSTLDL EITQENNKLI YDPDPLRDVD LELFSKVRDV VHTVDMTYWS DDEVIRATSI
     CTAMTIADTM SQLDRDNLKE MIALVNDDDV NSLITEFMVI DVPLFCSTFG GILVNQFAYS
     LYGLNIRGRE EIWGHVVRIL KDTSHAVLKV LSNALSHPKI FKRFWNAGVV EPVYGPNLSN
     QDKTLLALSV CEYSVDLFMH DWQGGVPLEV FICDNDPDVA DMRRSSFLAR HLAYLCSLAE
     ISRDGPRLES MNSLERLETL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK
     VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR
     GYEEITRGEV GRSGVGLTLP FDGRYLSHQL RLFGVNSTSC LKALELTYLL SPLVDKDKDR
     LFLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL
     GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNNSIGLVHC DMEGGDHKDD QVVLHEHYSV
     IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLVVLKTSNP ASTEMYLLSR
     HPKSDIIEDS KTVLASLHPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY
     HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMTAFNRVL KDTIFEWARI TESDKRLKLT
     GKYDLYPVRD SGKLKTISRR LVLSWVSLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI
     RNLRVITKTI LDRFENTIHS ITYRFLTKEV KILMKILGAV KMFGARQNEY TTVVDDGSLD
     DIEPYDSL
//