Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000098 | biological_process | sulfur amino acid catabolic process |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004792 | molecular_function | thiosulfate-cyanide sulfurtransferase activity |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0008097 | molecular_function | 5S rRNA binding |
| A | 0009440 | biological_process | cyanate catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016783 | molecular_function | sulfurtransferase activity |
| A | 0030855 | biological_process | epithelial cell differentiation |
| A | 0035928 | biological_process | rRNA import into mitochondrion |
| A | 0051029 | biological_process | rRNA transport |
Functional Information from PROSITE/UniProt
| site_id | PS00380 |
| Number of Residues | 12 |
| Details | RHODANESE_1 Rhodanese signature 1. YlerHVPGAsfF |
| Chain | Residue | Details |
| A | TYR48-PHE59 | |
| site_id | PS00683 |
| Number of Residues | 11 |
| Details | RHODANESE_2 Rhodanese C-terminal signature. VavYDGSWsEW |
| Chain | Residue | Details |
| A | VAL269-TRP279 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 118 |
| Details | Domain: {"description":"Rhodanese 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 115 |
| Details | Domain: {"description":"Rhodanese 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Region: {"description":"Hinge"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00586","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24329","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52196","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52196","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
