Functional Information from GO Data
Chain | GOid | namespace | contents |
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
Chain | Residue | Details |
A | TYR87 | |
A | SER99 | |
A | LYS215 | |
A | TYR224 | |
A | GLY233 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP100 | |
A | ASP102 | |
A | ASP154 | |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Interaction with RNA |
Chain | Residue | Details |
A | PHE140 | |
A | LYS145 | |
A | GLN294 | |
A | HIS314 | |
A | ASN315 | |
A | ARG387 | |
A | LYS392 | |
A | GLU487 | |
Chain | Residue | Details |
A | SER452 | |
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 |