Reviewed, UniProtKB/Swiss-Prot P06447 (L_SENDZ)

Names and origin

Protein names

Recommended name:
    Large structural protein
      Short name=Protein L
Alternative name(s):
    Transcriptase
    Replicase
Including the following 3 domains:
    1- Recommended name:
            RNA-directed RNA polymerase
              EC=2.7.7.48
    2- Recommended name:
            mRNA (guanine-N(7)-)-methyltransferase
              EC=2.1.1.56
    3- Recommended name:
            mRNA guanylyltransferase
              EC=2.7.7.-

Gene names

Name:

L

Organism

Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) [Complete proteome]

Taxonomic identifier

11198 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Respirovirus

Virus host

Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]

Protein attributes

Sequence length	2228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Displays RNA-directed RNA polymerase, mRNA guanylyl transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A) synthetase activities. The viral mRNA guanylyl transferase displays a different biochemical reaction than the cellular enzyme. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). Functions either as transcriptase or as replicase. The transcriptase synthesizes subsequently six subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. The transcriptase stutters on a specific sequence, resulting on a cotranscriptional editing of the phosphoprotein (P) mRNA. The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing the transcriptional signals. 5' GpppApGpG sequence is required for mRNA cap methylation by the enzyme.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
Subunit structure	Homooligomer. Interacts with the P and C proteins. The L protein complexes with P protein to form the functional polymerase. C protein binding to L has an inhibitory effect. Ref.5 Ref.7 Ref.11 Ref.12 Ref.14
Subcellular location	Virion Potential. Host cytoplasm.
Domain	The N-terminal part (about 1-400) seems to be involved in binding to the P protein.
Miscellaneous	Least abundant structural protein (approximately 50 copies per virion). Unstable in the absence of P protein.
Sequence similarities	Belongs to the paramyxoviruses L protein family. Contains 1 RdRp catalytic domain.
Caution	Ref.12 sequence used for mutagenesis is in conflict with the sequence shown in positions 29, 210, 211, 262, 263 and 264.
Biophysicochemical properties	pH dependence: Optimum pH is 6 for mRNA (guanine-N(7)-)-methyltransferase activity. Temperature dependence: Optimum temperature is 30 degrees Celsius.

Ontologies

Keywords
Biological process	RNA replication mRNA capping mRNA processing
Cellular component	Cytoplasm Virion
Ligand	ATP-binding Nucleotide-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Nucleotidyltransferase RNA-directed RNA polymerase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW transcription, RNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW mRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2228	2228	Large structural protein		PRO_0000142740
Regions
	Domain	656 – 840	185	RdRp catalytic
	Nucleotide binding	1801 – 1810	10	ATP Potential
	Region	1 – 174	174	Oligomerization domain
	Region	1756 – 2228	473	Involved in mRNA cap methylation
	Compositional bias	2031 – 2034	4	Poly-Ser
Natural variations
	Natural variant	96	1	Q → H in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R.
	Natural variant	581	1	R → S in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R.
	Natural variant	625	1	E → G in strain: Mutant F1-R / T-5 revertant and Mutant F1-R.
	Natural variant	752	1	I → M in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R.
	Natural variant	971	1	D → G in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R.
	Natural variant	1207	1	C → S in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R.
Experimental info
	Mutagenesis	20 – 25	6	LNSPIV → ANAPAA: Complete loss of P binding.
	Mutagenesis	29 – 33	5	IAQLH → AAAAA: Complete loss of P binding.
	Mutagenesis	77 – 81	5	QRTIK → ASAIA: 80% loss of P binding.
	Mutagenesis	173 – 177	5	FLTWF → AAAWA: Complete loss of P binding.
	Mutagenesis	209 – 213	5	YTLVT → AEAAA: Complete loss of P binding.
	Mutagenesis	235 – 238	4	LVLM → AAAA: Complete loss of P binding.
	Mutagenesis	262 – 266	5	ITSKG → AAGRA: 80% loss of P binding.
	Mutagenesis	287 – 291	5	VIALL → AAAAA: Complete loss of P binding. Ref.12
	Mutagenesis	345 – 347	3	IFH → AAA: Complete loss of P binding. Ref.12
	Mutagenesis	349 – 350	2	TS → DD: 46% loss of transcription. Complete loss of replication.
	Mutagenesis	354 – 355	2	KA → TG: 62% loss of transcription. complete loss of replication.
	Mutagenesis	362	1	R → A: Complete loss of transcription and replication. Ref.7
	Mutagenesis	363	1	T → S: Complete loss of transcription and replication. Ref.7
	Mutagenesis	366	1	H → A: Complete loss of transcription and replication. Ref.7
	Mutagenesis	368	1	S → R: Loss of phosphoprotein binding. Complete loss of transcription and replication. Ref.7
	Mutagenesis	370	1	E → A: No effect. Ref.7
	Mutagenesis	376 – 377	2	DK → EN: 60% loss of transcription. 22% loss of replication.
	Mutagenesis	533 – 535	3	DEE → AAA: 75% loss of replication. No loss of transcription.
	Mutagenesis	540	1	Y → E or Q: Complete loss of transcription and replication. Ref.13
	Mutagenesis	540	1	Y → F: 70% loss of transcription. Ref.13
	Mutagenesis	542 – 543	2	LK → AA: Complete loss of transcription and replication. No effect on template binding. Ref.13
	Mutagenesis	543	1	K → H, I, L, N, P, Q, R, S, T or V: Complete loss of transcription and replication. Ref.13
	Mutagenesis	544 – 548	5	EKEIK → AAAIA: Complete loss of transcription and replication. No effect on template binding.
	Mutagenesis	552	1	R → A: 50% loss of transcription; complete loss of replication. No effect on template binding. Ref.8
	Mutagenesis	556	1	K → A: Complete loss of transcription and replication. No effect on template binding. Ref.8
	Mutagenesis	562	1	R → A: Complete loss of transcription and replication. No effect on template binding. Ref.8
	Mutagenesis	569	1	E → A: Complete loss of transcription and replication. Ref.8
	Mutagenesis	661	1	T → E or K: Complete loss od transcription and replication. Ref.13
	Mutagenesis	663	1	D → G, R, S, V or Y: Complete loss of transcription and replication. Ref.13
	Mutagenesis	666	1	K → A: 80% loss of transcription. Complete loss of replication. Ref.13
	Mutagenesis	666	1	K → G, L or V: Complete loss of transcription and replication. Ref.13
	Mutagenesis	666	1	K → R: 76% loss of transcription. 40% loss of replication. Ref.13
	Mutagenesis	668	1	C → K or L: Complete loss of transcription and replication. Ref.13
	Mutagenesis	668	1	C → Y: 40% loss of transcription. Ref.13
	Mutagenesis	734	1	N → E: 26% loss of transcription. No effect on replication. Ref.13
	Mutagenesis	736	1	R → D, E or P: Complete loss of transcription and replication. Ref.13
	Mutagenesis	736	1	R → L or V: 80% loss of transcription. 50% increase of replication. Ref.13
	Mutagenesis	736	1	R → M: 13% loss of transcription. No effect on replication. Ref.13
	Mutagenesis	737	1	G → E: Complete loss of transcription. 80% loss of replication. Ref.13
	Mutagenesis	738	1	G → F: Complete loss of transcription and replication. Ref.13
	Mutagenesis	740	1	E → S: Complete loss of transcription and replication. Ref.13
	Mutagenesis	741	1	G → R: Complete loss of transcription and replication. Ref.13
	Mutagenesis	744	1	Q → K: Complete loss of transcription and replication. Ref.13
	Mutagenesis	943 – 945	3	MST → LNM: No effect.
	Mutagenesis	957 – 959	3	AVA → VTS: 38% loss of transcription.
	Mutagenesis	963 – 966	4	DLKR → ALAA: Complete loss of transcription and replication.
	Mutagenesis	1004 – 1006	3	PHS → VCV: Complete loss of transcription and replication.
	Mutagenesis	1011 – 1013	3	TII → RLL: 70% loss of transcription and replication.
	Mutagenesis	1023 – 1024	2	QE → IH: 30% loss of transcription and replication.
	Mutagenesis	1036 – 1037	2	ET → DD: 25% loss of transcription. 40% loss of replication.
	Mutagenesis	1040 – 1042	3	EED → AAA: Complete loss of transcription and replication.
	Mutagenesis	1051 – 1053	3	DRK → AAA: Complete loss of transcription and replication.
	Mutagenesis	1065 – 1066	2	GN → DH: 14% loss of transcription. 48% loss of replication.
	Mutagenesis	1097 – 1099	3	YGI → SRV: 16% loss of transcription. 66% loss of replication.
	Mutagenesis	1149 – 1150	2	TY → AR: 70% loss of transcription.
	Mutagenesis	1172 – 1174	3	EGS → RRH: 30% loss of transcription. 27% loss of replication.
	Mutagenesis	1208 – 1210	3	PAI → SSL: 80% loss of transcription. Complete loss replication.
	Mutagenesis	1220 – 1222	3	DER → AAA: Complete loss of transcription and replication.
	Mutagenesis	1254 – 1255	2	DE → AA: 90% loss of transcription and replication.
	Mutagenesis	1293 – 1294	2	KD → AA: 86% loss of transcription. Complete loss of replication.
	Mutagenesis	1303 – 1305	3	SAT → GTS: 15% loss of replication. 45% loss of replication.
	Mutagenesis	1333 – 1334	2	LV → FI: 77% loss of transcription. 94% loss of replication.
	Mutagenesis	1351 – 1354	4	RYKK → AAAA: Complete loss of transcription and replication. No effect on template binding or complex formation with P protein. Ref.9
	Mutagenesis	1571	1	C → F, L or S: Almost no effect. Ref.6
	Mutagenesis	1571	1	C → F or L: Almost no effect. Ref.6
	Mutagenesis	1571	1	C → G: 80% loss of transcription and replication. Ref.6
	Mutagenesis	1571	1	C → H or R: Complete loss of transcription and replication. Ref.6
	Mutagenesis	1571	1	C → T: 30% loss of transcription. Ref.6
	Mutagenesis	1571	1	C → V: 120% increase of transcription. 70% increase of replication. Ref.6
	Mutagenesis	1571	1	C → Y: 70% loss of transcription. Complete loss of replication. Ref.6
	Mutagenesis	1798 – 1800	3	KDR → AAA: 80% loss of transcription. 27% loss of replication.
	Mutagenesis	1815 – 1817	3	DAT → KEI: Complete loss of transcription and replication. Ref.10
	Mutagenesis	1838 – 1839	2	RE → AA: Complete loss of transcription and replication.

Sequences

	Sequence		Length	Mass (Da)
	P06447-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 074A4DFE8F8A37B5	FASTA	2,228	252,867
	10 20 30 40 50 60 MDGQESSQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYRLKDDSII NITKHKIRNG 70 80 90 100 110 120 GLSPRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL 130 140 150 160 170 180 TRELSSGFQD LWLNIFKQLG NIEGREGYDP LQDIGTIPEI TDKYSRNRWY RPFLTWFSIK 190 200 210 220 230 240 YDMRWMQKTR PGGPLDTSNS HNLLECKSYT LVTYGDLVMI LNKLTLTGYI LTPELVLMYC 250 260 270 280 290 300 DVVEGRWNMS AAGHLDKKSI GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ 310 320 330 340 350 360 LNDPVIPLRG AFMRHVLTEL QTVLTSRDVY TDAEADTIVE SLLAIFHGTS IDEKAEIFSF 370 380 390 400 410 420 FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLYECHAVF CTIIINGYRE RHGGQWPPCD 430 440 450 460 470 480 FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR 490 500 510 520 530 540 KEAWDSVYPD SNLYYKAPES EETRRLIEVF INDENFNPEE IINYVESGDW LKDEEFNISY 550 560 570 580 590 600 SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF RENGMVKGEI DLLKRLTTLS 610 620 630 640 650 660 VSGVPRTDSV YNNSKSSEKR NEGMENKNSG GYWDEKKRSR HEFKATDSST DGYETLSCFL 670 680 690 700 710 720 TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPVL ERCTIYVGDP YCPVADRMHR 730 740 750 760 770 780 QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT 790 800 810 820 830 840 SRVPVAQTYK QKKNHVYEEI TKYFGALRHV MFDVGHELKL NETIISSKMF VYSKRIYYDG 850 860 870 880 890 900 KILPQCLKAL TKCVFWSETL VDENRSACSN ISTSIAKAIE NGYSPILGYC IALYKTCQQV 910 920 930 940 950 960 CISLGMTINP TISPTVRDQY FKGKNWLRCA VLIPANVGGF NYMSTSRCFV RNIGDPAVAA 970 980 990 1000 1010 1020 LADLKRFIRA DLLDKQVLYR VMNQEPGDSS FLDWASDPYS CNLPHSQSIT TIIKNITARS 1030 1040 1050 1060 1070 1080 VLQESPNPLL SGLFTETSGE EDLNLASFLM DRKVILPRVA HEILGNSLTG VREAIAGMLD 1090 1100 1110 1120 1130 1140 TTKSLVRASV RKGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL 1150 1160 1170 1180 1190 1200 RQKMWIHLTY GRPIHGLETP DPLELLRGIF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL 1210 1220 1230 1240 1250 1260 DTLTNGCPAI RIPYFGSATD ERSEAQLGYV RNLSKPAKAA IRIAMVYTWA YGTDEISWME 1270 1280 1290 1300 1310 1320 AALIAQTRAN LSLENLKLLT PVSTSTNLSH RLKDTATQMK FSSATLVRAS RFITISNDNM 1330 1340 1350 1360 1370 1380 ALKEAGESKD TNLVYQQIML TGLSLFEFNM RYKKGSLGKP LILHLHLNNG CCIMESPQEA 1390 1400 1410 1420 1430 1440 NIPPRSTLDL EITQENNKLI YDPDPLKDVD LELFSKVRDV VHTVDMTYWS DDEVIRATSI 1450 1460 1470 1480 1490 1500 CTAMTIADTM SQLDRDNLKE MIALVNDDDV NSLITEFMVI DVPLFCSTFG GILVNQFAYS 1510 1520 1530 1540 1550 1560 LYGLNIRGRE EIWGHVVRIL KDTSHAVLKV LSNALSHPKI FKRFWNAGVV EPVYGPNLSN 1570 1580 1590 1600 1610 1620 QDKILLALSV CEYSVDLFMH DWQGGVPLEI FICDNDPDVA DMRRSSFLAR HLAYLCSLAE 1630 1640 1650 1660 1670 1680 ISRDGPRLES MNSLERLESL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK 1690 1700 1710 1720 1730 1740 VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR 1750 1760 1770 1780 1790 1800 GYKEITRGEI GRSGVGLTLP FDGRYLSHQL RLFGINSTSC LKALELTYLL SPLVDKDKDR 1810 1820 1830 1840 1850 1860 LYLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL 1870 1880 1890 1900 1910 1920 GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNSSIGLVHC DMEGGDHKDD QVVLHEHYSV 1930 1940 1950 1960 1970 1980 IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLIVLKTSNP ASTEMYLLSR 1990 2000 2010 2020 2030 2040 HPKSDIIEDS KTVLASLLPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY 2050 2060 2070 2080 2090 2100 HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMIAFNRVL KDTIFEWARI TESDKRLKLT 2110 2120 2130 2140 2150 2160 GKYDLYPVRD SGKLKTISRR LVLSWISLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI 2170 2180 2190 2200 2210 2220 RNLRVITKTL LDRFEDIIHS ITYRFLTKEI KILMKILGAV KMFGARQNEY TTVIDDGSLG DIEPYDSS

References

[1]	"Determination of the complete nucleotide sequence of the Sendai virus genome RNA and the predicted amino acid sequences of the F, HN and L proteins." Shioda T., Iwasaki K., Shibuta H. Nucleic Acids Res. 14:1545-1563(1986) [PubMed: 3005975] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L proteins of two host range mutants of Sendai virus." Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E., Klenk H.-D., Rott R., Seto J.T. Virology 176:656-657(1990) [PubMed: 2161155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Mutant F1-R and Mutant ts-f1.
[3]	Middleton Y. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 581 AND 971.
[4]	"Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai virus." Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R., Seto J.T. Virology 184:227-234(1991) [PubMed: 1651590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Mutant F1-R / T-5 revertant.
[5]	"Complexes of Sendai virus NP-P and P-L proteins are required for defective interfering particle genome replication in vitro." Horikami S.M., Curran J., Kolakofsky D., Moyer S.A. J. Virol. 66:4901-4908(1992) [PubMed: 1321276] [Abstract] Cited for: INTERACTION WITH P PROTEIN.
[6]	"Alternative amino acids at a single site in the Sendai virus L protein produce multiple defects in RNA synthesis in vitro." Horikami S.M., Moyer S.A. Virology 211:577-582(1995) [PubMed: 7645261] [Abstract] Cited for: MUTAGENESIS OF CYS-1571.
[7]	"Mutations in conserved domain I of the Sendai virus L polymerase protein uncouple transcription and replication." Chandrika R., Horikami S.M., Smallwood S., Moyer S.A. Virology 213:352-363(1995) [PubMed: 7491760] [Abstract] Cited for: INTERACTION WITH P PROTEIN, MUTAGENESIS OF 349-THR-SER-350; 354-LYS-ALA-355; ARG-362; THR-363; HIS-366; SER-368; GLU-370 AND 376-ASP-LYS-377.
[8]	"Mutations in conserved domain II of the large (L) subunit of the Sendai virus RNA polymerase abolish RNA synthesis." Smallwood S., Easson C.D., Feller J.A., Horikami S.M., Moyer S.A. Virology 262:375-383(1999) [PubMed: 10502516] [Abstract] Cited for: MUTAGENESIS OF 533-ASP--GLU-535; 542-LEU-LYS-543; 544-ASP--LYS-548; ARG-552; LYS-556; ARG-562 AND GLU-569.
[9]	"Mutations in domain V of the Sendai virus L polymerase protein uncouple transcription and replication and differentially affect replication in vitro and in vivo." Cortese C.K., Feller J.A., Moyer S.A. Virology 277:387-396(2000) [PubMed: 11080486] [Abstract] Cited for: MUTAGENESIS OF 1149-THR-TYR-1150; 1172-GLU--SER-1174; 1208-PRO--ILE-1210; 1220-ASP--ARG-1222; 1254-ASP-GLU-1255; 1293-LYS-ASP-1294; 1303-SER--THR-1305; 1333-LEU-VAL-1334 AND 1351-ARG--LYS-1354.
[10]	"Mutations in conserved domains IV and VI of the large (L) subunit of the Sendai virus RNA polymerase give a spectrum of defective RNA synthesis phenotypes." Feller J.A., Smallwood S., Horikami S.M., Moyer S.A. Virology 269:426-439(2000) [PubMed: 10753721] [Abstract] Cited for: MUTAGENESIS OF 943-MET--THR-945; 957-ALA--ALA-959; 963-ASP--ARG-966; 1004-PRO--SER-1006; 1011-THR--ILE-1013; 1023-GLN-GLU-1024; 1036-GLU-THR-1037; 1040-GLU--ASP-1042; 1051-ASP--LYS-1053; 1065-GLY-ASN-1066; 1097-TYR--ILE-1099; 1798-LYS--ARG-1800; 1815-ASP--THR-1817 AND 1838-ARG-GLU-1839.
[11]	"Sendai virus wild-type and mutant C proteins show a direct correlation between L polymerase binding and inhibition of viral RNA synthesis." Grogan C.C., Moyer S.A. Virology 288:96-108(2001) [PubMed: 11543662] [Abstract] Cited for: INTERACTION WITH C PROTEIN.
[12]	"The phosphoprotein (P) binding site resides in the N-terminus of the L polymerase subunit of Sendai virus." Holmes D.E., Moyer S.A. J. Virol. 76:3078-3083(2002) [PubMed: 11861877] [Abstract] Cited for: INTERACTION WITH P PROTEIN, MUTAGENESIS OF 20-SER--VAL-25; 29-ILE--HIS-33; 77-GLN--LYS-81; 173-PHE--PHE-177; 209-TYR--THR-213; 235-LEU--MET-238; 262-ILE--GLY-266; 287-VAL--LEU-291 AND 345-ILE--HIS-347.
[13]	"Different substitutions at conserved amino acids in domains II and III in the Sendai L RNA polymerase protein inactivate viral RNA synthesis." Smallwood S., Hoevel T., Neubert W.J., Moyer S.A. Virology 304:135-145(2002) [PubMed: 12490411] [Abstract] Cited for: MUTAGENESIS OF TYR-540; LYS-543; THR-661; ASP-663; LYS-666; CYS-668; ASN-734; ARG-736; GLY-737; GLY-738; GLU-740; GLY-741 AND GLN-744.
[14]	"The L-L oligomerization domain resides at the very N-terminus of the Sendai virus L RNA polymerase protein." Cevik B., Smallwood S., Moyer S.A. Virology 313:525-536(2003) [PubMed: 12954219] [Abstract] Cited for: OLIGOMERIZATION.
[15]	"Sendai virus RNA-dependent RNA Polymerase L protein catalyzes cap methylation of virus-specific mRNA." Ogino T., Kobayashi M., Iwama M., Mizumoto K. J. Biol. Chem. 280:4429-4435(2005) [PubMed: 15574411] [Abstract] Cited for: MRNA (GUANINE-N(7)-)-METHYLTRANSFERASE ACTIVITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X03614 Genomic RNA. Translation: CAA27272.1. Different initiation. X03614 Genomic RNA. Translation: CAA27273.1. M30202 Genomic RNA. Translation: AAB06283.1. M30203 Genomic RNA. Translation: AAB06289.1. M30204 Genomic RNA. Translation: AAB06201.1. M69046 Genomic RNA. Translation: AAB06295.1.
PIR	ZLNZSV. A04120.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR016269. RNA-dir_RNA_pol_paramyxovir. IPR014023. RNA_pol_cat. IPR001016. RNA_pol_L_viral. [Graphical view]
Pfam	PF00946. Paramyx_RNA_pol. 1 hit. [Graphical view]
PIRSF	PIRSF000830. RNA_pol_ParamyxoV. 1 hit.
PROSITE	PS50526. RDRP_SSRNA_NEG_NONSEG. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

L_SENDZ

Accession

Primary (citable) accession number: P06447
Secondary accession number(s): P27566, Q84185, Q98705

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)