Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
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 |
Functional Information from PROSITE/UniProt
site_id | PS00327 |
Number of Residues | 12 |
Details | BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. YSVLDVfAKyVF |
Chain | Residue | Details |
A | TYR234-PHE245 | |
site_id | PS00950 |
Number of Residues | 13 |
Details | BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYlTWaLSTPMIL |
Chain | Residue | Details |
A | ARG108-LEU120 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 37 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"10827943","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 25 |
Details | Transmembrane: {"description":"Helical; Name=Helix A"} |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10827943","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=Helix B"} |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=Helix C"} |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=Helix D"} |
site_id | SWS_FT_FI7 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=Helix E"} |
site_id | SWS_FT_FI8 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=Helix F"} |
site_id | SWS_FT_FI9 |
Number of Residues | 28 |
Details | Transmembrane: {"description":"Helical; Name=Helix G"} |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10827943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17117890","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-(retinylidene)lysine"} |