5A97
Hazara virus nucleocapsid protain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019013 | cellular_component | viral nucleocapsid |
A | 0019029 | cellular_component | helical viral capsid |
A | 1990904 | cellular_component | ribonucleoprotein complex |
B | 0003723 | molecular_function | RNA binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019013 | cellular_component | viral nucleocapsid |
B | 0019029 | cellular_component | helical viral capsid |
B | 1990904 | cellular_component | ribonucleoprotein complex |
C | 0003723 | molecular_function | RNA binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0019013 | cellular_component | viral nucleocapsid |
C | 0019029 | cellular_component | helical viral capsid |
C | 1990904 | cellular_component | ribonucleoprotein complex |
D | 0003723 | molecular_function | RNA binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0019013 | cellular_component | viral nucleocapsid |
D | 0019029 | cellular_component | helical viral capsid |
D | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | SITE: Homooligomerization => ECO:0000269|PubMed:26715309 |
Chain | Residue | Details |
A | PHE216 | |
B | GLN270 | |
B | VAL271 | |
B | LYS275 | |
B | LEU279 | |
B | PRO355 | |
C | PHE216 | |
C | TRP263 | |
C | GLN270 | |
C | VAL271 | |
C | LYS275 | |
A | TRP263 | |
C | LEU279 | |
C | PRO355 | |
D | PHE216 | |
D | TRP263 | |
D | GLN270 | |
D | VAL271 | |
D | LYS275 | |
D | LEU279 | |
D | PRO355 | |
A | GLN270 | |
A | VAL271 | |
A | LYS275 | |
A | LEU279 | |
A | PRO355 | |
B | PHE216 | |
B | TRP263 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Cleavage by host CASP3/caspase 3 => ECO:0000269|PubMed:30720418, ECO:0000269|PubMed:31118258 |
Chain | Residue | Details |
A | ASP272 | |
B | ASP272 | |
C | ASP272 | |
D | ASP272 |