Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0008502 | molecular_function | melatonin receptor activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043448 | biological_process | alkane catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0008502 | molecular_function | melatonin receptor activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0043448 | biological_process | alkane catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue JEY A 2201 |
| Chain | Residue |
| A | ALA117 |
| A | ASN268 |
| A | TYR294 |
| A | ALA297 |
| A | TYR298 |
| A | MET120 |
| A | GLY121 |
| A | VAL124 |
| A | ASN175 |
| A | PHE192 |
| A | GLN194 |
| A | TYR200 |
| A | LEU267 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 2202 |
| Chain | Residue |
| A | CYS1005 |
| A | CYS1008 |
| A | CYS1038 |
| A | CYS1041 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue JEY B 2201 |
| Chain | Residue |
| B | ALA117 |
| B | MET120 |
| B | GLY121 |
| B | VAL124 |
| B | ASN175 |
| B | PHE192 |
| B | GLN194 |
| B | TYR200 |
| B | LEU267 |
| B | ASN268 |
| B | TYR294 |
| B | ALA297 |
| B | TYR298 |
Functional Information from PROSITE/UniProt
| site_id | PS00202 |
| Number of Residues | 11 |
| Details | RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG |
| Chain | Residue | Details |
| A | ILE1032-GLY1042 | |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. GSVwNITAIAIDRYLyI |
| Chain | Residue | Details |
| A | GLY126-ILE142 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 26 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 60 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 104 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31019305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ME6","evidenceCode":"ECO:0007744"}]} |
