Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002939 | biological_process | tRNA N1-guanine methylation |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008175 | molecular_function | tRNA methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030488 | biological_process | tRNA methylation |
| A | 0032259 | biological_process | methylation |
| A | 0052906 | molecular_function | tRNA (guanine(37)-N1)-methyltransferase activity |
| B | 0002939 | biological_process | tRNA N1-guanine methylation |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008175 | molecular_function | tRNA methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030488 | biological_process | tRNA methylation |
| B | 0032259 | biological_process | methylation |
| B | 0052906 | molecular_function | tRNA (guanine(37)-N1)-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAM A 401 |
| Chain | Residue |
| A | GLU143 |
| A | PHE209 |
| A | ASP223 |
| A | ILE224 |
| A | ASN225 |
| A | SER250 |
| A | ASP251 |
| A | VAL252 |
| A | ASN265 |
| A | PHE273 |
| C | G37 |
| A | PHE144 |
| D | U46 |
| A | TYR177 |
| A | PHE178 |
| A | ARG186 |
| A | MET202 |
| A | PHE203 |
| A | GLY205 |
| A | PRO208 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAM B 402 |
| Chain | Residue |
| B | GLU143 |
| B | PHE144 |
| B | TYR177 |
| B | PHE178 |
| B | SER179 |
| B | ARG186 |
| B | PHE203 |
| B | PRO208 |
| B | PHE209 |
| B | ASP223 |
| B | ILE224 |
| B | ASN225 |
| B | ASP251 |
| B | VAL252 |
| B | ASN265 |
| B | PHE273 |
| D | G37 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 102 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 103 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 104 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 105 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 106 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 201 |
| Chain | Residue |
| D | A26 |
| D | G27 |
| D | HOH801 |
Functional Information from PROSITE/UniProt
| site_id | PS00539 |
| Number of Residues | 6 |
| Details | PYROKININ Pyrokinins signature. FSPRLG |
| Chain | Residue | Details |
| A | PHE178-GLY183 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01021","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19749755","evidenceCode":"ECO:0000269"}]} |
