viHumans
P16379
Reviewed
Aedes [TaxID: 7158]; Bos Taurus (Bovine) [TaxID: 9913]; Culicoides [TaxID: 58271]; Equus Asinus (Donkey) (Equus Africanus Asinus) [TaxID: 9793]; Equus Caballus (Horse) [TaxID: 9796]; Homo Sapiens (Human) [TaxID: 9606]; Lutzomyia [TaxID: 252607]; Musca Domestica (House Fly) [TaxID: 7370]; Simuliidae (black Flies) [TaxID: 7190]; Sus Scrofa (Pig) [TaxID: 9823]
L
♦RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48)
♦ mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56)
♦ GDP polyribonucleotidyltransferase (EC 2.7.7.88)
♦ Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]
Vesicular Stomatitis New Jersey Virus (strain Ogden Subtype Concan) (VSNJV)
Viruses> SsRNA Viruses> SsRNA Negative-strand Viruses> Mononegavirales> Rhabdoviridae> Vesiculovirus> New Jersey Vesiculovirus> Vesicular Stomatitis New Jersey Virus> Vesicular Stomatitis New Jersey Virus (strain Ogden Subtype Concan) (VSNJV)
NC_024473.1 ;  JX121109.2 
2155516 ;   
Various pathway(s) in which protein is involved
Not Available
Not Available
MDFDLIEDSANWEDDESDFFLRDILSQEDQMSYLNTADYNLNSPLISDDMVYIIKRMNHEEVPPIWRSKEWDSPLDMLRGCQAQPMSHQEMHNWFGTWIQ
NIQHDSAQGFTFLKEVDKESEMTYDLVSTFLKGWVGKDYPFKSKNKEIDSMALVGPLCQKFLDLHKITLILNAVSLGETKELLATFKGKYRMSCENIPIA
RLRLPSLGPVFMCKGWTYIHKERVLMDRNFLLMCKDVIIGRMQTFLSMIGRSDNKFSPDQIYTLANVYRIGDKILEQCGNKAYDLIKMIEPICNLKMMEL
ARLHRPKIPKFPHFEEHVKGSVRELTQRSNRIQTLYDLIMSMKDVDLVLVVYGSFRHWGHPFIDYFEGLEKLHTQVNMEKHIDKEYPQQLASDLARLVLN
KQFSESKKWFVDPSKMSPKHPFYEHVINKTWPTAAKIQDFGDNWHKLPLIQCFEIPDLIDPSVIYSDKSHSMNKKEVIQHVRSKPNIPIPSKKVLQTMLT
NRATNWKAFLKDIDENGLDDDDLIIGLKGKERELKIAGRFFSLMSWRLREYFVITEYLIKTYYVPLFKGLTMADDLTSVIKKMMDSSSGQGLDDYSSVCL
ANHIDYEKWNNHQRKESNGPIFRVMGQFLGYPSLIERTHEFFEKSLIYYNGRPDLMTIRNGTLCNSTKHRVCWNGQKGGLEGLRQKGWSIVNLLVIQREA
KIRNTAVKVLAQGDNQVICTQYKTKKTRSELELRAVLHQMAGNNNKIMEEIKRGTEKLGLIINDDETMQSADYLNYGKIPIFRGVIRGLETKRWSRVTCV
TNDQIPTCANLMSSVSTNALTVAHFAENPINAMIQYNYFGTFARLLLFMHDPAIRQSLYKVQDKIPGLHTRTFKYAMLYLDPSIGGVCGMALSRFLIRAF
PDPVTESLSFWKFIYEHASEPHLRKMAVMFGDPPIAKFRIEHINKLLEDPTSLNISMGMSPANLLKSEVKKCLIESRSSIKNEIIKDATIYMHQEEEKLR
GFLWSIKPLFPRFLSEFKAGTFLGVSEGLINLFQNSRTIRNSFKKRYHKDLDELIIKSEISSLSHLGSMHYRLGDNQIWSCSASRADILRYKSWTRKVVG
TTVPHPLEMHGPPSKKERPCQLCNSSGLTYISVHCPKGIIDVFNRRGPLPAYLGSNTSESTSILQPWEKESKIPIIKRATRLRDAISWFIPPESPLSTCI
LNNIQALTGEDWSSKQHGFKRTGSALHRFSTSRMSNGGFASQSPATLTRMIATTDTMRDFGTKNYDFMFQASLLYGQMTTSISRYGTPGSCTDHYHIRCK
GCIREIEEVELNTSLEYKTPDVSHILEKWRNNTGSWGHQIKQLKPAEGNWESLSPVEQSYQVARCIGFLYGELTHKKSRQADDSSLFPLSIQLKVRGRGF
LRGLLDGLMRSSCCQVIHRRSVSTLKRPANAVYGGLIYLIDKLSASSPFLSLVRTGPIRQELEQVPHKMSTSYPTNIRDLGSIVRNYFKYQCRPVERGNY
KTCYNQIWLFSDVLSTEFIGPMAISSSLLRLLYRPSLTKKDREELRELAALSSNLRSGEDWDDSHIKFFSNDLLFCSQEIRHACKFGIKKDNEDITFYPN
WGTEYIGNVIDIPVFYRAQNVKKDIKVPPRIQNPLMSGLRLGQLPTGAHYKMRAIVFRLKIPYHDFLACGDGSGGMTAALLRYNRTSRGIFNSLLDLSDT
MLRGSSPEPPSALETLGGERVRCVNGDSCWEHPSDLSDENTWKYFLHLKKGCGMSINLITMDMEVQDSVISYKIESLVRQYVPVLLESDGCLIYKTYGTY
IATQEDNSLTLIGSLFHSVQLVQTDLSSSNTSELYLVCRGLKDYVDTPFVDWIELYDNWEKQYAFRSFKDEFQRAQSLTPETTLIGIPPQFVPDPGVNLE
TLFQIAGVPTGVAHGITHHILQSKDKLISNAIGSMCVISHFTINTIRTTDSMPGPPSDGDVNKMCSALIGTCFWLSWMESDLNLYKTCLRSIMKSMPVRW
FRTLKNEKWSQKWDCKGDAIPKDSRLGDSLANIGNWIRAWELIRNGNKSEPFDSMVAEALPKSVDKSLSWRKISKSTGIPRLLNSDIDLVDQSILNVQID
IVENQAWQN
2109
Not Available
Not Available
15-05-2007
Evidence at transcript level
Amino Acid Count % Frequency Amino Acid Count % Frequency
Alanine (A) Leucine (L)
Arginine (R) Lysine (K)
Asparagine (N) Methionine (M)
Aspartic Acid (D) Phenylalanine (F)
Cysteine (C) Proline (P)
Glutamine (Q) Serine (S)
Glutamic Acid (E) Threonine (T)
Glycine (G) Tryptophan (W)
Histidine (H) Tyrosine (Y)
Isoleucine (I) Valine (V)
% Number of Residues in Helices % Number of Residues in Strands % Number of Residues in Coils
♦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 acticities 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.
2.7.7.48  ,   2.1.1.56  ,   2.7.7.88  ,   2.1.1.296  
GO:0003968  ;   GO:0004482  ;   GO:0005524  ;   GO:0019012  ;   GO:0030430  ;  
GO:0039689  
Virion . Host cytoplasm . Note=L and P are packaged asymmetrically towards the blunt end of the virus. .
♦DOMAIN 598 784 RdRp catalytic.
♦ DOMAIN 1640 1837 Mononegavirus-type SAM-dependent 2'-O-MTase.
Not Available
Predicted/Modelled
Not Available
Not Available
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
Not Available
Virtual screening has been performed using RASPD
  • Million Molecules

Best 20 Hit molecules

    Not Available