Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000448 | biological_process | cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| A | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006397 | biological_process | mRNA processing |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019003 | molecular_function | GDP binding |
| A | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090730 | cellular_component | Las1 complex |
| A | 0110152 | molecular_function | RNA NAD+-cap (NAD+-forming) hydrolase activity |
| A | 0110155 | biological_process | NAD-cap decapping |
| A | 0140432 | molecular_function | 5'-hydroxyl dinucleotide hydrolase activity |
| A | 1990174 | molecular_function | phosphodiesterase decapping endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | GLU150 |
| A | ASP201 |
| A | GLU239 |
| A | LEU240 |
| A | UBG403 |
| A | HOH546 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH565 |
| A | HOH567 |
| A | HOH584 |
| A | GLU199 |
| A | HOH515 |
| A | HOH550 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | binding site for residue UBG A 403 |
| Chain | Residue |
| A | PRO65 |
| A | LYS66 |
| A | SER67 |
| A | ASP68 |
| A | PRO69 |
| A | ASP70 |
| A | TRP93 |
| A | ARG94 |
| A | GLY95 |
| A | GLU128 |
| A | THR130 |
| A | ASN138 |
| A | TYR147 |
| A | GLN180 |
| A | ALA197 |
| A | GLY198 |
| A | GLU199 |
| A | GLU239 |
| A | LYS241 |
| A | GLN263 |
| A | MG401 |
| A | HOH506 |
| A | HOH510 |
| A | HOH511 |
| A | HOH546 |
| A | HOH551 |
| A | HOH557 |
| A | HOH571 |
| A | HOH583 |
| A | HOH584 |
| A | HOH602 |
| A | HOH610 |
| A | HOH629 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | PHE265 |
| A | ILE269 |
| A | HIS292 |
| A | HOH530 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O70348","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19194460","evidenceCode":"ECO:0000269"}]} |
