Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0019028 | cellular_component | viral capsid |
B | 0055036 | cellular_component | virion membrane |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0019028 | cellular_component | viral capsid |
C | 0055036 | cellular_component | virion membrane |
F | 0004252 | molecular_function | serine-type endopeptidase activity |
F | 0006508 | biological_process | proteolysis |
G | 0004252 | molecular_function | serine-type endopeptidase activity |
G | 0019028 | cellular_component | viral capsid |
G | 0055036 | cellular_component | virion membrane |
I | 0004252 | molecular_function | serine-type endopeptidase activity |
I | 0019028 | cellular_component | viral capsid |
I | 0055036 | cellular_component | virion membrane |
J | 0005198 | molecular_function | structural molecule activity |
J | 0019028 | cellular_component | viral capsid |
P | 0004252 | molecular_function | serine-type endopeptidase activity |
P | 0019028 | cellular_component | viral capsid |
P | 0055036 | cellular_component | virion membrane |
Q | 0005198 | molecular_function | structural molecule activity |
Q | 0019028 | cellular_component | viral capsid |
R | 0005198 | molecular_function | structural molecule activity |
R | 0019028 | cellular_component | viral capsid |
S | 0004252 | molecular_function | serine-type endopeptidase activity |
S | 0006508 | biological_process | proteolysis |
T | 0004252 | molecular_function | serine-type endopeptidase activity |
T | 0019028 | cellular_component | viral capsid |
T | 0055036 | cellular_component | virion membrane |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 447 |
Details | Domain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Site: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1221 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 120 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 16 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 51 |
Details | Region: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 18 |
Details | Site: {"description":"Interaction with host receptor LDLRAD3","evidences":[{"source":"PubMed","id":"34646020","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 9 |
Details | Lipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |