Reviewed, UniProtKB/Swiss-Prot O55528 (L_SENDO)

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 Ohita) (SeV) [Complete proteome]

Taxonomic identifier

302272 [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	Inferred from homology.

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 By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(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 By similarity.
Subcellular location	VirionPotential. CytoplasmBy similarity.
Domain	The N-terminal part (about 1-400) seems to be involved in binding to the P protein By similarity.
Miscellaneous	Least abundant structural protein (approximately 50 copies per virion). Unstable in the absence of P protein By similarity.
Sequence similarities	Belongs to the paramyxoviruses L protein family. Contains 1 RdRp catalytic domain.

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 virion Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro 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_0000142739
Regions
	Domain	656 – 840	185	RdRp catalytic
	Nucleotide binding	1801 – 1810	10	ATP Potential
	Region	1 – 174	174	Oligomerization domain By similarity
	Region	1756 – 2228	473	Involved in mRNA cap methylation By similarity
	Compositional bias	2031 – 2034	4	Poly-Ser
Natural variations
	Natural variant	2050	1	E → A in avirulent isolate MVC11.

Sequences

	Sequence		Length	Mass (Da)
	O55528-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 9BDAC6F266B13B1F	FASTA	2,228	253,061
	10 20 30 40 50 60 MDGQESTQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYILKDDSII NITKHKIRNG 70 80 90 100 110 120 GLSLRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL 130 140 150 160 170 180 TKELSNGFQD LWLNIFKQLG NIEGREGYDP LQDISTIPEI TERYSRNKWY RPFLTWFSIK 190 200 210 220 230 240 YDMRWMQKTR PGGPLDTSNS HNLLECKSYT LVTYGDLVMI LNKSTLTGYI LTPELVLMYC 250 260 270 280 290 300 DVVEGRWNMS AAGQLDKRST GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ 310 320 330 340 350 360 LSDPVIPLRG AFMRHVLTEL QTVLTSKDVY TDPEADAIVE SLLAIFHGTS IDEKAEIFSF 370 380 390 400 410 420 FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLHECHAVF CTIIINGYRE RHGGQWPPCD 430 440 450 460 470 480 FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR 490 500 510 520 530 540 KEAWDSVYPD SNLYYKVPES EETRRLIEVF INDENFNPED IIDYVESGDW LKDEKFNISY 550 560 570 580 590 600 SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF SENGMVKGEI DLLKRLTTLS 610 620 630 640 650 660 VSGVPRTDSV YNNPRSSEKR NESMKKRNSK GYWDEKKRSR HEFKATDSST DGYETLSCFL 670 680 690 700 710 720 TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPVL EKCTIYVGDP YCPVADRMHR 730 740 750 760 770 780 QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT 790 800 810 820 830 840 SRVPVAQTYK QKKNHVYEEI TRYFGALRHV MFDIGHELKL NETIISSKMF VYSKRIYYDG 850 860 870 880 890 900 KILPQCLKAL TRCVFWSETL 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 HEILSNSLTG VREAIAGMLD 1090 1100 1110 1120 1130 1140 TTKSLVRASV KRGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL 1150 1160 1170 1180 1190 1200 RQKMWIHLTY GRPIHGLETP DPLELLRGTF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL 1210 1220 1230 1240 1250 1260 DTLTNGSPAI 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 RYKKGSLEKP LILHLHLNNG CCIMESPQEA 1390 1400 1410 1420 1430 1440 NIPPRSTLDL EITQENNKLI YDPDPLRDVD 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 QDKTLLALSV CEYSVDLFMH DWQGGVPLEV FICDNDPDVA DMRRSSFLAR HLAYLCSLAE 1630 1640 1650 1660 1670 1680 ISRDGPRLES MNSLERLETL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK 1690 1700 1710 1720 1730 1740 VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR 1750 1760 1770 1780 1790 1800 GYEEITRGEV GRSGVGLTLP FDGRYLSHQL RLFGVNSTSC LKALELTYLL SPLVDKDKDR 1810 1820 1830 1840 1850 1860 LFLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL 1870 1880 1890 1900 1910 1920 GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNNSIGLVHC DMEGGDHKDD QVVLHEHYSV 1930 1940 1950 1960 1970 1980 IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLVVLKTSNP ASTEMYLLSR 1990 2000 2010 2020 2030 2040 HPKSDIIEDS KTVLASLHPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY 2050 2060 2070 2080 2090 2100 HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMTAFNRVL KDTIFEWARI TESDKRLKLT 2110 2120 2130 2140 2150 2160 GKYDLYPVRD SGKLKTISRR LVLSWVSLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI 2170 2180 2190 2200 2210 2220 RNLRVITKTI LDRFENTIHS ITYRFLTKEV KILMKILGAV KMFGARQNEY TTVVDDGSLD DIEPYDSL

References

[1]

"Isolation of an avirulent mutant of Sendai virus with two amino acid mutations from a highly virulent field strain through adaptation to LLC-MK2 cells." Itoh M., Isegawa Y., Hotta H., Homma M. J. Gen. Virol. 78:3207-3215(1997) [PubMed: 9400971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate M1 and Isolate MVC11.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB005795 Genomic RNA. Translation: BAA24392.1. AB005796 Genomic RNA. Translation: BAA24401.1.
RefSeq	NP_056879.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1489777.
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_SENDO

Accession

Primary (citable) accession number: O55528
Secondary accession number(s): O55530

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	June 1, 1998
Last modified:	November 25, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)