General information | DisProt: | DP00673_C001 | Name: | Protein C | Synonym(s): | POLG_WNV
Core protein
Capsid protein
cleavage product 1 of Genome polyprotein
| First appeared in release: | Release 5.1 (05/28/2010) | UniProt: | P06935 | UniGene: | | SwissProt: | POLG_WNV | TrEMBL: | | NCBI (GI): | 37999909 | Source organism: | West Nile virus (WNV) | Sequence length: | 105 | Percent disordered: | 48% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA - 60 PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST KQKKR
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Functional narrative |
The virion of this virus is a nucleocapsid covered by a lipoprotein envelope. The envelope contains two proteins: the protein M and glycoprotein E. The nucleocapsid is a complex of protein C and mRNA. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. Protein C is cleavage product 1 of Genome polyprotein, comprising aa 2-123 of the polyprotein.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 24 | Length: | 24 | Region sequence: |
MSKKPGGPGKNRAVNMLKRGMPRG | Modification type: | Native
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Chaperones
| Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; 2-mercaptoethanol 5 mM; path-length (quartz cuvette (Hellma)) 0.02 cm; protein (sample) 20 uM; sodium phosphate (buffer) 20 mM)
| References:
- Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. "RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae." Nucleic Acids Res. 2008; 36(3): 712-725. PubMed: 18033802
| Comments:
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Region 2 | Type: | Disordered | Name: | | Location: | 80 - 105 | Length: | 26 | Region sequence: |
HLLSFKKELGTLTSAINRRSTKQKKR | Modification type: | Native
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Chaperones
| Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; 2-mercaptoethanol 5 mM; path-length (quartz cuvette (Hellma)) 0.02 cm; protein (sample) 20 uM; sodium phosphate (buffer) 20 mM)
| References:
- Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. "RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae." Nucleic Acids Res. 2008; 36(3): 712-725. PubMed: 18033802
| Comments:
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