| IED ID |
IndEnz0002003434 |
| Enzyme Type ID |
protease003434 |
| Protein Name |
Virion membrane protein A17 precursor homolog
|
| Gene Name |
FPV182 |
| Organism |
Fowlpox virus (strain NVSL) (FPV) |
| Taxonomic Lineage |
Viruses
Varidnaviria
Bamfordvirae
Nucleocytoviricota
Pokkesviricetes
Chitovirales
Poxviridae
Chordopoxvirinae
Avipoxvirus
Fowlpox virus (FPV)
Fowlpox virus (strain NVSL) (FPV)
|
| Enzyme Sequence |
MDNNYLNYYNVFEEFDAGAGIKEKELFTEEQQLSFLPKKGLGNGGFDGVERLYSNIINNNDIKSLLALIMLVFAINTNSLVALIFIILSAIFVPVPALIIAYCIALHLKNGSDATHVGISILLMLASAVTIYLTSTSKISKGFKRAIDVVLLVILGFYIVKIYGIDRQISIPSRRYCRQMSGPSSLENLNAFQTHSNY |
| Enzyme Length |
198 |
| Uniprot Accession Number |
Q9J551 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
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| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| Enzyme Function |
FUNCTION: Envelope protein which participates in virus morphogenesis. Needed for an early step in viral crescent membrane formation by interacting with D13 scaffold protein. Its interaction with D13 scaffold protein leads to the formation of rigid, crescent-shaped membranes that assemble around the cytoplasmic virus factory. Membrane anchor for the protein A27. A17-A27 virus envelope protein might be involved in fusion or attachment, and can further associate to A26 (By similarity). {ECO:0000250}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
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| Features |
Chain (1); Disulfide bond (1); Modified residue (1); Site (2); Topological domain (3); Transmembrane (2) |
| Keywords |
Disulfide bond;Membrane;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Viral envelope protein;Virion |
| Interact With |
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| Induction |
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| Subcellular Location |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue |
MOD_RES 198; /note=Phosphotyrosine; /evidence=ECO:0000250 |
| Post Translational Modification |
PTM: The 22 kDa precursor is probably cleaved by the I7 protease during virus maturation. {ECO:0000250}.; PTM: Phosphorylated on tyrosine and threonine. Its phosphorylation state is regulated by the F10 kinase and the H1 phosphatase (By similarity). Phosphorylation by F10 kinase seems to be required to form the membranes associated with IV (By similarity). {ECO:0000250}. |
| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
21,966 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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