Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0007602 | biological_process | phototransduction |
A | 0009881 | molecular_function | photoreceptor activity |
A | 0016020 | cellular_component | membrane |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
B | 0007165 | biological_process | signal transduction |
B | 0016020 | cellular_component | membrane |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0005515 | molecular_function | protein binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0007602 | biological_process | phototransduction |
C | 0009881 | molecular_function | photoreceptor activity |
C | 0016020 | cellular_component | membrane |
C | 0034220 | biological_process | monoatomic ion transmembrane transport |
D | 0007165 | biological_process | signal transduction |
D | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00327 |
Number of Residues | 12 |
Details | BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. IVYLDLvTKvGF |
Chain | Residue | Details |
A | ILE197-PHE208 | |
site_id | PS00950 |
Number of Residues | 13 |
Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYiDWiLTTPLIV |
Chain | Residue | Details |
A | ARG72-VAL84 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
B | GLY23-GLU43 | |
D | GLY23-GLU43 | |
site_id | SWS_FT_FI2 |
Number of Residues | 30 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
B | VAL44-ALA59 | |
D | VAL44-ALA59 | |
A | SER150-SER153 | |
A | HIS223-ASP239 | |
C | GLY26-GLU33 | |
C | GLY92-ASP94 | |
C | SER150-SER153 | |
C | HIS223-ASP239 | |
site_id | SWS_FT_FI3 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
B | ALA60-THR81 | |
D | ALA60-THR81 | |
site_id | SWS_FT_FI4 |
Number of Residues | 46 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
A | LEU56-PHE69 | |
A | VAL118-ILE121 | |
A | PRO182-THR189 | |
C | LEU56-PHE69 | |
C | VAL118-ILE121 | |
C | PRO182-THR189 | |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Helix C |
Chain | Residue | Details |
A | ALA70-ALA91 | |
C | ALA70-ALA91 | |
site_id | SWS_FT_FI6 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=Helix D |
Chain | Residue | Details |
A | SER95-MET117 | |
C | SER95-MET117 | |
site_id | SWS_FT_FI7 |
Number of Residues | 54 |
Details | TRANSMEM: Helical; Name=Helix E |
Chain | Residue | Details |
A | GLU122-ALA149 | |
C | GLU122-ALA149 | |
site_id | SWS_FT_FI8 |
Number of Residues | 54 |
Details | TRANSMEM: Helical; Name=Helix F |
Chain | Residue | Details |
A | SER154-GLY181 | |
C | SER154-GLY181 | |
site_id | SWS_FT_FI9 |
Number of Residues | 64 |
Details | TRANSMEM: Helical; Name=Helix G |
Chain | Residue | Details |
A | PRO190-GLU222 | |
C | PRO190-GLU222 | |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-(retinylidene)lysine |
Chain | Residue | Details |
A | LYS205 | |
C | LYS205 | |