Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001510 | biological_process | RNA methylation |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006364 | biological_process | rRNA processing |
| A | 0006396 | biological_process | RNA processing |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008173 | molecular_function | RNA methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019843 | molecular_function | rRNA binding |
| A | 0030490 | biological_process | maturation of SSU-rRNA |
| A | 0032040 | cellular_component | small-subunit processome |
| A | 0032259 | biological_process | methylation |
| A | 0042254 | biological_process | ribosome biogenesis |
| A | 0042274 | biological_process | ribosomal small subunit biogenesis |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070037 | molecular_function | rRNA (pseudouridine) methyltransferase activity |
| A | 0070475 | biological_process | rRNA base methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue SAH A 301 |
| Chain | Residue |
| A | ILE87 |
| A | VAL217 |
| A | SER218 |
| A | ILE219 |
| A | SER220 |
| A | TYR222 |
| A | LEU224 |
| A | SER225 |
| A | ALA226 |
| A | THR229 |
| A | CIT302 |
| A | ARG128 |
| A | HOH415 |
| A | HOH421 |
| A | HOH447 |
| A | HOH457 |
| A | HOH467 |
| A | HOH476 |
| A | THR176 |
| A | SER177 |
| A | PHE178 |
| A | VAL200 |
| A | GLY201 |
| A | PHE203 |
| A | ALA204 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue CIT A 302 |
| Chain | Residue |
| A | SER177 |
| A | PHE178 |
| A | SER179 |
| A | GLY206 |
| A | SAH301 |
| A | HOH415 |
| A | HOH416 |
| A | HOH421 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue CIT A 303 |
| Chain | Residue |
| A | CYS66 |
| A | ASP67 |
| A | LYS70 |
| A | ASP79 |
| A | ARG84 |
| A | ARG125 |
| A | PRO127 |
| A | ARG128 |
| A | THR129 |
| A | ARG132 |
| A | HOH483 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q06287","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interaction with substrate rRNA","evidences":[{"source":"UniProtKB","id":"Q06287","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Stabilizes Arg-84","evidences":[{"source":"UniProtKB","id":"Q06287","evidenceCode":"ECO:0000250"}]} |
