3.4.21.90: Togavirin
This is an abbreviated version!
For detailed information about Togavirin, go to the full flat file.
Word Map on EC 3.4.21.90
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3.4.21.90
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viruses
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proteoglycans
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virion
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vaccine
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epitope
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infectious
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virus-like
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glycosaminoglycans
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chondroitin
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heparan
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papillomavirus
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serotype
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cartilage
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icosahedral
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bacteriophage
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nucleocapsids
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self-assembly
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serological
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baculovirus
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polyprotein
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parvovirus
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encapsidation
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aggrecan
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chondroitinase
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immunodominant
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enterovirus
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decorin
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norovirus
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nonstructural
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polyomavirus
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poliovirus
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rna-dependent
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foot-and-mouth
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gastroenteritis
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rotavirus
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reovirus
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keratan
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hbeag
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mottle
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pentamers
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uncoating
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subgenomic
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anti-hcv
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coxsackievirus
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virus-specific
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hcv-infected
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cryo-electron
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drug development
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reassortant
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ns5a
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syndecan-1
- 3.4.21.90
- viruses
- proteoglycans
- virion
- vaccine
- epitope
- infectious
-
virus-like
- glycosaminoglycans
- chondroitin
- heparan
- papillomavirus
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serotype
- cartilage
-
icosahedral
- bacteriophage
- nucleocapsids
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self-assembly
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serological
- baculovirus
- polyprotein
- parvovirus
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encapsidation
- aggrecan
- chondroitinase
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immunodominant
- enterovirus
- decorin
- norovirus
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nonstructural
- polyomavirus
- poliovirus
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rna-dependent
- foot-and-mouth
- gastroenteritis
- rotavirus
- reovirus
- keratan
-
hbeag
-
mottle
-
pentamers
-
uncoating
-
subgenomic
-
anti-hcv
- coxsackievirus
-
virus-specific
-
hcv-infected
-
cryo-electron
- drug development
-
reassortant
- ns5a
- syndecan-1
Reaction
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-/-Ser- bond =
Synonyms
capsid protein, core protein, NsP2 proteinase, Sindbis virus core protein, Sindbis virus protease
ECTree
3.4.21.90 TogavirinAdvanced search results
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Substrates Products on EC 3.4.21.90 - Togavirin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Sindbis virus core protein + H2O
?
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autocatalytic cleavage at Trp264, . Besides its catalytic activity it also plays important roles in the formation of the viral core, the recognition of the spike proteins during the budding process, the recognition and packaging of the viral RNA, and possibly the inhibition of the host cell protein synthesis
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?
Sindbis virus core protein + H2O
Hydrolyzed Sindbis core protein
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autocatalytic cleavage at Trp264
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?
additional information
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the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. Core protein is associated to the large 60S ribosomal subunit during in vitro protein synthesis and in the infected cell
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additional information
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the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. A short linker sequence connects the basic domain to the protease domain. In the Sindbis virus core protein, the basic domain, the linker sequence and the protease domain comprise amino acid residues M(1) to Q(94), P(95) to D(113), and R(114) to W(264), respectively. Core protein domain beginning at M(106) does not bind to the 60S ribosomal subunit, whereas core protein domain beginning at Q(94) binds to the 60S ribosomal subunit and inhibits the disassembly of cores in vitro
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additional information
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the region that is responsible for nucleocapsid core accumulation has considerable overlap with the region that controls encapsidation specificity. Amino acids 96 to 113 are responsible for the specific encapsidation of genomic RNA. Amino acids 99 and 105 may interact directly with the encapsidation signal. Amino acids 106 to 113 are responsible for nucleocapsid core accumulation
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