Entry |
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Symbol |
L
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Name |
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Pathway |
map03265 | Virion - Ebolavirus, Lyssavirus and Morbillivirus |
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Brite |
KEGG Orthology (KO) [BR:ko00001]
09120 Genetic Information Processing
09125 Information processing in viruses
03230 Viral genome structure
K19376 L; Morbillivirus RNA-directed RNA polymerase L
03240 Viral replication
K19376 L; Morbillivirus RNA-directed RNA polymerase L
03265 Virion - Ebolavirus, Lyssavirus and Morbillivirus
K19376 L; Morbillivirus RNA-directed RNA polymerase L
09160 Human Diseases
09172 Infectious disease: viral
05162 Measles
K19376 L; Morbillivirus RNA-directed RNA polymerase L
09180 Brite Hierarchies
09185 Viral protein families
03200 Viral proteins
K19376 L; Morbillivirus RNA-directed RNA polymerase L
Enzymes [BR:ko01000]
2. Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.375 NNS virus cap methyltransferase
K19376 L; Morbillivirus RNA-directed RNA polymerase L
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.48 RNA-directed RNA polymerase
K19376 L; Morbillivirus RNA-directed RNA polymerase L
2.7.7.88 GDP polyribonucleotidyltransferase
K19376 L; Morbillivirus RNA-directed RNA polymerase L
Viral proteins [BR:ko03200]
-ssRNA viruses
Measles virus
K19376 L; Morbillivirus RNA-directed RNA polymerase L
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Other DBs |
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Genes |
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Reference |
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Authors |
Krumm SA, Takeda M, Plemper RK |
Title |
The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity. |
Journal |
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Sequence |
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LinkDB |
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