viHumans
Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Not Available
♦Non-structural polyprotein p200 (p200) [Cleaved into: Protease p150 (p150) (EC 3.4.22.-)
♦ RNA-directed RNA polymerase/triphosphatase/helicase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
Rubella Virus (strain RN-UK86) (RUBV)
Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Togaviridae> Rubivirus> Rubella Virus (RUBV)> Rubella Virus (strain RN-UK86) (RUBV)
Various pathway(s) in which protein is involved
Not Available
Not Available
MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHWIEWGPKEALHVLIDPSPGLL
REVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHGGRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALA
AHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRPCTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRH
VRSLQPSARVRLPDLVHLAEVGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
LAGIMKSAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEIAATWIVHAASADRHCACAPR
CDVPRERPSAPACPPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPLAPRPARYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLR
GPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARAWAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPKLIALALRTLAQQGAALALSVRDLPGGAA
FDANAVTAAVRAGPGQFAATSPPPGDPPPPRRARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPDSPTSAEPADRARHAELEVVYEPSGPPTST
KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVATPGHGCGYTHIIHAVAPRRPR
DPAALEEGEALLERAYRSIVALAAARRWACVACPLLGAGVYGWSAAESLRAALAATRTEPAERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPL
ASCPAGDLGRPAQRSASPPATPLGDATAPEPRGCQGCELCRCTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPP
RGMCGSDMWRCRGWQGMPQVRCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SASHADASPDGTGDPLDPLMETVGCACSRVWVGTEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGGGPRRVSDRPHLWLAVPLSRG
GGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTTRILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATY
ERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVICVGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFAC
NLWDGRQVDLHLAFSRETVRRLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKNHTEMPGTERVLSAVCAVRRY
RAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAARELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAAL
GPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKIIMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALL
GLPCAEDYRALRAGSYCTLRELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVRELTAYARGRGLDHPATIGAL
EEIQTPYARANLHDAD
2116
Not Available
Not Available
01-03-2003
Inferred from homology
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
♦Non-structural polyprotein p200 replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved in p150 and p90 (By similarity).
♦ Protease p150 has 2 separate domains with different biological activities. The N-terminal section has presumably a cytoplasmic mRNA-capping activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The C-terminal section harbors a protease active in cis or in trans which specifically cleaves and releases the two mature proteins (By similarity).
♦ RNA-directed RNA polymerase/triphosphatase/helicase p90 replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 24S mRNA codes for structural proteins (By similarity).
3.4.22.-  ,   2.7.7.48  ,   3.6.1.15  ,   3.6.4.13  
GO:0003723  ;   GO:0003968  ;   GO:0004197  ;   GO:0004386  ;   GO:0005524  ;  
GO:0006351  ;   GO:0006396  ;   GO:0008174  ;   GO:0016020  ;   GO:0039694  ;  
GO:0044161  ;   GO:0044175  ;   GO:0044188  ;   GO:0046872  
♦ Non-structural polyprotein p200: Host endosome membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host lysosome membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host cytoplasmic vesicle . Note=Located in vesicles at the cytoplasmic surface of modified endosomes and lysosomes, also called replication complexes. .
♦ Protease p150: Host endosome membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host lysosome membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host cytoplasmic vesicle . Note=Located in vesicles at the cytoplasmic surface of modified endosomes and lysosomes, also called replication complexes. .
♦ RNA-directed RNA polymerase/triphosphatase/helicase p90: Host endosome membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host lysosome membrane
♦ Peripheral membrane protein
♦ Cytoplasmic side . Host cytoplasmic vesicle . Note=Located in vesicles at the cytoplasmic surface of modified endosomes and lysosomes, also called replication complexes. .
♦DOMAIN 57 247 Alphavirus-like MT.
♦ DOMAIN 806 985 Macro.
♦ DOMAIN 1109 1274 Peptidase C27.
♦ DOMAIN 1320 1468 (+)RNA virus helicase ATP-binding.
♦ DOMAIN 1469 1609 (+)RNA virus helicase C-terminal.
♦ DOMAIN 1870 1981 RdRp catalytic.
MOTIF 1902 1906 Human RB1 binding motif.
Predicted/Modelled
Not Available
♦ACT_SITE 1152 1152 For cysteine protease activity.
♦ ACT_SITE 1273 1273 For cysteine protease activity.
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