P06447 · L_SENDZ

Function

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.
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.

Miscellaneous

Least abundant structural protein (approximately 50 copies per virion). Unstable in the absence of P protein.

Caution

PubMed:11861877 sequence used for mutagenesis is in conflict with the sequence shown in positions 29, 210, 211, 262, 263 and 264.

Catalytic activity

  • a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
    EC:2.7.7.48 (UniProtKB | ENZYME | Rhea)
  • a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H+ + 2 S-adenosyl-L-homocysteine
    EC:2.1.1.375 (UniProtKB | ENZYME | Rhea)
  • a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H+ + S-adenosyl-L-homocysteine
  • a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H+ = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate
    EC:2.7.7.88 (UniProtKB | ENZYME | Rhea)
  • a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine
  • GTP + H2O = GDP + H+ + phosphate

pH Dependence

Optimum pH is 6 for mRNA (guanine-N7-)-methyltransferase activity.

Temperature Dependence

Optimum temperature is 30 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site1801-1810ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasm
Cellular Componentvirion component
Molecular FunctionATP binding
Molecular FunctionGTPase activity
Molecular FunctionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
Molecular FunctionRNA-dependent RNA polymerase activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    RNA-directed RNA polymerase L
  • Short names
    Protein L
  • Alternative names
    • Large structural protein
    • Replicase
    • Transcriptase

Including 4 domains:

  • Recommended name
    RNA-directed RNA polymerase
  • EC number
  • Recommended name
    GTP phosphohydrolase
  • EC number
  • Recommended name
    GDP polyribonucleotidyltransferase
  • EC number
  • Alternative names
    • PRNTase
  • Recommended name
    mRNA cap methyltransferase
  • EC number
  • Alternative names
    • mRNA (guanine-N(7)-)-methyltransferase
      (G-N7-MTase
      )
    • mRNA (nucleoside-2'-O-)-methyltransferase
      (N1-2'-O-MTase
      )

Gene names

    • Name
      L

Organism names

Accessions

  • Primary accession
    P06447
  • Secondary accessions
    • P27566
    • Q84185
    • Q98705

Proteomes

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis20-25Complete loss of P binding.
Mutagenesis29-33Complete loss of P binding.
Mutagenesis77-8180% loss of P binding.
Natural variant96in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R
Mutagenesis173-177Complete loss of P binding.
Mutagenesis209-213Complete loss of P binding.
Mutagenesis235-238Complete loss of P binding.
Mutagenesis262-26680% loss of P binding.
Mutagenesis287-291Complete loss of P binding.
Mutagenesis345-347Complete loss of P binding.
Mutagenesis349-35046% loss of transcription. Complete loss of replication.
Mutagenesis354-35562% loss of transcription. complete loss of replication.
Mutagenesis362Complete loss of transcription and replication.
Mutagenesis363Complete loss of transcription and replication.
Mutagenesis366Complete loss of transcription and replication.
Mutagenesis368Loss of phosphoprotein binding. Complete loss of transcription and replication.
Mutagenesis370No effect.
Mutagenesis376-37760% loss of transcription. 22% loss of replication.
Mutagenesis533-53575% loss of replication. No loss of transcription.
Mutagenesis540Complete loss of transcription and replication.
Mutagenesis54070% loss of transcription.
Mutagenesis542-543Complete loss of transcription and replication. No effect on template binding.
Mutagenesis543Complete loss of transcription and replication.
Mutagenesis544-548Complete loss of transcription and replication. No effect on template binding.
Mutagenesis55250% loss of transcription; complete loss of replication. No effect on template binding.
Mutagenesis556Complete loss of transcription and replication. No effect on template binding.
Mutagenesis562Complete loss of transcription and replication. No effect on template binding.
Mutagenesis569Complete loss of transcription and replication.
Natural variant581in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R
Natural variant625in strain: Mutant F1-R / T-5 revertant and Mutant F1-R
Mutagenesis661Complete loss od transcription and replication.
Mutagenesis663Complete loss of transcription and replication.
Mutagenesis66680% loss of transcription. Complete loss of replication.
Mutagenesis666Complete loss of transcription and replication.
Mutagenesis66676% loss of transcription. 40% loss of replication.
Mutagenesis668Complete loss of transcription and replication.
Mutagenesis66840% loss of transcription.
Mutagenesis73426% loss of transcription. No effect on replication.
Mutagenesis736Complete loss of transcription and replication.
Mutagenesis73680% loss of transcription. 50% increase of replication.
Mutagenesis73613% loss of transcription. No effect on replication.
Mutagenesis737Complete loss of transcription. 80% loss of replication.
Mutagenesis738Complete loss of transcription and replication.
Mutagenesis740Complete loss of transcription and replication.
Mutagenesis741Complete loss of transcription and replication.
Mutagenesis744Complete loss of transcription and replication.
Natural variant752in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R
Mutagenesis943-945No effect.
Mutagenesis957-95938% loss of transcription.
Mutagenesis963-966Complete loss of transcription and replication.
Natural variant971in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R
Mutagenesis1004-1006Complete loss of transcription and replication.
Mutagenesis1011-101370% loss of transcription and replication.
Mutagenesis1023-102430% loss of transcription and replication.
Mutagenesis1036-103725% loss of transcription. 40% loss of replication.
Mutagenesis1040-1042Complete loss of transcription and replication.
Mutagenesis1051-1053Complete loss of transcription and replication.
Mutagenesis1065-106614% loss of transcription. 48% loss of replication.
Mutagenesis1097-109916% loss of transcription. 66% loss of replication.
Mutagenesis1149-115070% loss of transcription.
Mutagenesis1172-117430% loss of transcription. 27% loss of replication.
Natural variant1207in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R
Mutagenesis1208-121080% loss of transcription. Complete loss replication.
Mutagenesis1220-1222Complete loss of transcription and replication.
Mutagenesis1254-125590% loss of transcription and replication.
Mutagenesis1293-129486% loss of transcription. Complete loss of replication.
Mutagenesis1303-130515% loss of replication. 45% loss of replication.
Mutagenesis1333-133477% loss of transcription. 94% loss of replication.
Mutagenesis1351-1354Complete loss of transcription and replication. No effect on template binding or complex formation with P protein.
Mutagenesis1571Almost no effect.
Mutagenesis1571Almost no effect.
Mutagenesis157180% loss of transcription and replication.
Mutagenesis1571Complete loss of transcription and replication.
Mutagenesis157130% loss of transcription.
Mutagenesis1571120% increase of transcription. 70% increase of replication.
Mutagenesis157170% loss of transcription. Complete loss of replication.
Mutagenesis1798-180080% loss of transcription. 27% loss of replication.
Mutagenesis1815-1817Complete loss of transcription and replication.
Mutagenesis1838-1839Complete loss of transcription and replication.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001427401-2228RNA-directed RNA polymerase L

Interaction

Subunit

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.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-174Oligomerization domain
Region610-633Disordered
Compositional bias613-633Basic and acidic residues
Domain656-840RdRp catalytic
Region1756-2228Involved in mRNA cap methylation
Domain1771-1978Mononegavirus-type SAM-dependent 2'-O-MTase

Domain

The N-terminal part (about 1-400) seems to be involved in binding to the P protein.

Sequence similarities

Belongs to the paramyxovirus L protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,228
  • Mass (Da)
    252,867
  • Last updated
    1988-01-01 v1
  • Checksum
    074A4DFE8F8A37B5
MDGQESSQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYRLKDDSIINITKHKIRNGGLSPRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTRELSSGFQDLWLNIFKQLGNIEGREGYDPLQDIGTIPEITDKYSRNRWYRPFLTWFSIKYDMRWMQKTRPGGPLDTSNSHNLLECKSYTLVTYGDLVMILNKLTLTGYILTPELVLMYCDVVEGRWNMSAAGHLDKKSIGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLNDPVIPLRGAFMRHVLTELQTVLTSRDVYTDAEADTIVESLLAIFHGTSIDEKAEIFSFFRTFGHPSLEAVTAADKVRAHMYAQKAIKLKTLYECHAVFCTIIINGYRERHGGQWPPCDFPDHVCLELRNAQGSNTAISYECAVDNYTSFIGFKFRKFIEPQLDEDLTIYMKDKALSPRKEAWDSVYPDSNLYYKAPESEETRRLIEVFINDENFNPEEIINYVESGDWLKDEEFNISYSLKEKEIKQEGRLFAKMTYKMRAVQVLAETLLAKGIGELFRENGMVKGEIDLLKRLTTLSVSGVPRTDSVYNNSKSSEKRNEGMENKNSGGYWDEKKRSRHEFKATDSSTDGYETLSCFLTTDLKKYCLNWRFESTALFGQRCNEIFGFKTFFNWMHPVLERCTIYVGDPYCPVADRMHRQLQDHADSGIFIHNPRGGIEGYCQKLWTLISISAIHLAAVRVGVRVSAMVQGDNQAIAVTSRVPVAQTYKQKKNHVYEEITKYFGALRHVMFDVGHELKLNETIISSKMFVYSKRIYYDGKILPQCLKALTKCVFWSETLVDENRSACSNISTSIAKAIENGYSPILGYCIALYKTCQQVCISLGMTINPTISPTVRDQYFKGKNWLRCAVLIPANVGGFNYMSTSRCFVRNIGDPAVAALADLKRFIRADLLDKQVLYRVMNQEPGDSSFLDWASDPYSCNLPHSQSITTIIKNITARSVLQESPNPLLSGLFTETSGEEDLNLASFLMDRKVILPRVAHEILGNSLTGVREAIAGMLDTTKSLVRASVRKGGLSYGILRRLVNYDLLQYETLTRTLRKPVKDNIEYEYMCSVELAVGLRQKMWIHLTYGRPIHGLETPDPLELLRGIFIEGSEVCKLCRSEGADPIYTWFYLPDNIDLDTLTNGCPAIRIPYFGSATDERSEAQLGYVRNLSKPAKAAIRIAMVYTWAYGTDEISWMEAALIAQTRANLSLENLKLLTPVSTSTNLSHRLKDTATQMKFSSATLVRASRFITISNDNMALKEAGESKDTNLVYQQIMLTGLSLFEFNMRYKKGSLGKPLILHLHLNNGCCIMESPQEANIPPRSTLDLEITQENNKLIYDPDPLKDVDLELFSKVRDVVHTVDMTYWSDDEVIRATSICTAMTIADTMSQLDRDNLKEMIALVNDDDVNSLITEFMVIDVPLFCSTFGGILVNQFAYSLYGLNIRGREEIWGHVVRILKDTSHAVLKVLSNALSHPKIFKRFWNAGVVEPVYGPNLSNQDKILLALSVCEYSVDLFMHDWQGGVPLEIFICDNDPDVADMRRSSFLARHLAYLCSLAEISRDGPRLESMNSLERLESLKSYLELTFLDDPVLRYSQLTGLVIKVFPSTLTYIRKSSIKVLRTRGIGVPEVLEDWDPEADNALLDGIAAEIQQNIPLGHQTRAPFWGLRVSKSQVLRLRGYKEITRGEIGRSGVGLTLPFDGRYLSHQLRLFGINSTSCLKALELTYLLSPLVDKDKDRLYLGEGAGAMLSCYDATLGPCINYYNSGVYSCDVNGQRELNIYPAEVALVGKKLNNVTSLGQRVKVLFNGNPGSTWIGNDECEALIWNELQNSSIGLVHCDMEGGDHKDDQVVLHEHYSVIRIAYLVGDRDVVLISKIAPRLGTDWTRQLSLYLRYWDEVNLIVLKTSNPASTEMYLLSRHPKSDIIEDSKTVLASLLPLSKEDSIKIEKWILIEKAKAHEWVTRELREGSSSSGMLRPYHQALQTFGFEPNLYKLSRDFLSTMNIADTHNCMIAFNRVLKDTIFEWARITESDKRLKLTGKYDLYPVRDSGKLKTISRRLVLSWISLSMSTRLVTGSFPDQKFEARLQLGIVSLSSREIRNLRVITKTLLDRFEDIIHSITYRFLTKEIKILMKILGAVKMFGARQNEYTTVIDDGSLGDIEPYDSS

Sequence caution

The sequence CAA27272.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias613-633Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X03614
EMBL· GenBank· DDBJ
CAA27272.1
EMBL· GenBank· DDBJ
Genomic RNA Different initiation
X03614
EMBL· GenBank· DDBJ
CAA27273.1
EMBL· GenBank· DDBJ
Genomic RNA
M30202
EMBL· GenBank· DDBJ
AAB06283.1
EMBL· GenBank· DDBJ
Genomic RNA
M30203
EMBL· GenBank· DDBJ
AAB06289.1
EMBL· GenBank· DDBJ
Genomic RNA
M30204
EMBL· GenBank· DDBJ
AAB06201.1
EMBL· GenBank· DDBJ
Genomic RNA
M69046
EMBL· GenBank· DDBJ
AAB06295.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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