Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0008218 | biological_process | bioluminescence |
| B | 0008800 | molecular_function | beta-lactamase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNSTVA |
| Chain | Residue | Details |
| B | PHE233-ALA244 | |
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL |
| Chain | Residue | Details |
| B | PHE251-LEU266 | |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSIfSLLAIAIDRYIaI |
| Chain | Residue | Details |
| B | SER90-ILE106 | |
| site_id | PS00626 |
| Number of Residues | 11 |
| Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IAGGyFHGLAL |
| Chain | Residue | Details |
| A | ILE69-LEU79 | |
| A | ILE108-LEU118 | |
| A | VAL225-LEU235 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 17 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21593763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YDO","evidenceCode":"ECO:0007744"}]} |