Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001411 | cellular_component | hyphal tip |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0008150 | biological_process | biological_process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030428 | cellular_component | cell septum |
| A | 0046589 | molecular_function | ribonuclease T1 activity |
| B | 0001411 | cellular_component | hyphal tip |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004521 | molecular_function | RNA endonuclease activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0008150 | biological_process | biological_process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030428 | cellular_component | cell septum |
| B | 0046589 | molecular_function | ribonuclease T1 activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 106 |
| Chain | Residue |
| A | ASP15 |
| A | HOH468 |
| A | HOH499 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 306 |
| Chain | Residue |
| B | ASP215 |
| B | HOH414 |
| B | HOH444 |
| B | HOH456 |
| B | HOH479 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2GP A 105 |
| Chain | Residue |
| A | HIS40 |
| A | LYS41 |
| A | TYR42 |
| A | ASN43 |
| A | ASN44 |
| A | TYR45 |
| A | GLU46 |
| A | GLU58 |
| A | ARG77 |
| A | HIS92 |
| A | ASN98 |
| A | PHE100 |
| A | TYR38 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2GP B 305 |
| Chain | Residue |
| B | TYR238 |
| B | HIS240 |
| B | TYR242 |
| B | ASN243 |
| B | ASN244 |
| B | TYR245 |
| B | GLU246 |
| B | GLU258 |
| B | ARG277 |
| B | HIS292 |
| B | ASN298 |
| B | ASN299 |
| B | PHE300 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS40 | |
| B | HIS240 | |
| Chain | Residue | Details |
| A | GLU58 | |
| B | GLU258 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS92 | |
| B | HIS292 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b2m |
| Chain | Residue | Details |
| A | GLU58 | |
| A | HIS40 | |
| A | HIS92 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b2m |
| Chain | Residue | Details |
| B | HIS292 | |
| B | GLU258 | |
| B | HIS240 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 414 |
| Chain | Residue | Details |
| A | TYR38 | electrostatic stabiliser |
| A | HIS40 | proton shuttle (general acid/base) |
| A | GLU58 | proton shuttle (general acid/base) |
| A | ARG77 | electrostatic stabiliser |
| A | HIS92 | proton shuttle (general acid/base) |
| A | PHE100 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 414 |
| Chain | Residue | Details |
| B | TYR238 | electrostatic stabiliser |
| B | HIS240 | proton shuttle (general acid/base) |
| B | GLU258 | proton shuttle (general acid/base) |
| B | ARG277 | electrostatic stabiliser |
| B | HIS292 | proton shuttle (general acid/base) |
| B | PHE300 | electrostatic stabiliser |
