Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016020 | cellular_component | membrane |
A | 0019031 | cellular_component | viral envelope |
A | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
A | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
A | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
A | 0055036 | cellular_component | virion membrane |
A | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
B | 0016020 | cellular_component | membrane |
B | 0019031 | cellular_component | viral envelope |
B | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
B | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
B | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
B | 0055036 | cellular_component | virion membrane |
B | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
C | 0016020 | cellular_component | membrane |
C | 0019031 | cellular_component | viral envelope |
C | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
C | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
C | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
C | 0055036 | cellular_component | virion membrane |
C | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
E | 0006508 | biological_process | proteolysis |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0008241 | molecular_function | peptidyl-dipeptidase activity |
E | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ |
Chain | Residue | Details |
E | THR371-GLN380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
Chain | Residue | Details |
E | GLU375 | |
B | GLN14-PRO1213 | |
C | GLN14-PRO1213 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
E | HIS505 | |
B | SER685 | |
C | SER685 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
Chain | Residue | Details |
E | ARG169 | |
E | TRP477 | |
E | LYS481 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
E | ARG273 | |
E | HIS345 | |
E | TYR515 | |
B | ASN17 | |
B | PRO1158 | |
B | VAL1173 | |
C | ASN17 | |
C | PRO1158 | |
C | VAL1173 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
E | HIS374 | |
B | ALA1074 | |
C | TRP61 | |
C | ASN122 | |
C | SER717 | |
C | ILE801 | |
C | ALA1074 | |
E | HIS378 | |
E | GLU402 | |
A | ILE801 | |
A | ALA1074 | |
B | TRP61 | |
B | ASN122 | |
B | SER717 | |
B | ILE801 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
E | ASN53 | |
E | ASN322 | |
A | ILE1194 | |
B | LYS74 | |
B | MET149 | |
B | ILE1194 | |
C | LYS74 | |
C | MET149 | |
C | ILE1194 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
E | ASN90 | |
B | LEU331 | |
B | PHE343 | |
B | VAL616 | |
B | GLU657 | |
B | TRP1098 | |
C | GLU165 | |
C | THR282 | |
C | LEU331 | |
C | PHE343 | |
C | VAL616 | |
A | THR282 | |
C | GLU657 | |
C | TRP1098 | |
A | LEU331 | |
A | PHE343 | |
A | VAL616 | |
A | GLU657 | |
A | TRP1098 | |
B | GLU165 | |
B | THR282 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
E | ASN103 | |
E | ASN432 | |
B | PHE234 | |
B | ALA709 | |
C | PHE234 | |
C | ALA709 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
E | ASN546 | |
B | VAL323 | |
C | VAL323 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
A | PHE325 | |
B | PHE325 | |
C | PHE325 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
A | GLN603 | |
B | GLN603 | |
C | GLN603 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583 |
Chain | Residue | Details |
A | SER676 | |
A | GLY678 | |
B | SER676 | |
B | GLY678 | |
C | SER676 | |
C | GLY678 |
site_id | SWS_FT_FI13 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
Chain | Residue | Details |
A | TYR1134 | |
B | TYR1134 | |
C | TYR1134 |