Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005847 | cellular_component | mRNA cleavage and polyadenylation specificity factor complex |
| A | 0006397 | biological_process | mRNA processing |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0030846 | biological_process | termination of RNA polymerase II transcription, poly(A)-coupled |
| A | 0031123 | biological_process | RNA 3'-end processing |
| A | 0031124 | biological_process | mRNA 3'-end processing |
| A | 0031126 | biological_process | sno(s)RNA 3'-end processing |
| A | 0043631 | biological_process | obsolete RNA polyadenylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990817 | molecular_function | poly(A) RNA polymerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FLC A 531 |
| Chain | Residue |
| A | ALA20 |
| A | ASN23 |
| A | LYS24 |
| A | THR417 |
| A | GLU418 |
| A | ASP419 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FLC A 532 |
| Chain | Residue |
| A | VAL234 |
| A | MG533 |
| A | HOH582 |
| A | HOH670 |
| A | HOH759 |
| A | HOH761 |
| A | HOH817 |
| A | HOH833 |
| A | HOH866 |
| A | TYR224 |
| A | GLY232 |
| A | GLY233 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 533 |
| Chain | Residue |
| A | ASP102 |
| A | ASP154 |
| A | FLC532 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 109 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mssqkvfgitgpvstvgataaenklndsliqelkkegsfeteqetanrvqvlkilqelaqrfvyevskkknmsdgmardaggkiftygsyrlgvhgpgsdi..............DTLVVVPK |
| Chain | Residue | Details |
| A | MET1-LYS109 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17850751","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Site: {"description":"Interaction with RNA"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fa0 |
| Chain | Residue | Details |
| A | LYS215 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 796 |
| Chain | Residue | Details |
| A | SER89 | electrostatic stabiliser, polar interaction |
| A | ASP100 | metal ligand |
| A | ASP102 | metal ligand |
| A | ASP154 | metal ligand |
| A | LYS215 | electrostatic stabiliser, polar interaction |
| A | TYR224 | electrostatic stabiliser, polar interaction |
