Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| A | 0004692 | molecular_function | cGMP-dependent protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007165 | biological_process | signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030553 | molecular_function | cGMP binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGTFGTVKlVhhkptqir..........YALK |
| Chain | Residue | Details |
| A | ILE540-LYS563 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL |
| Chain | Residue | Details |
| A | ILE653-LEU665 | |
| site_id | PS00888 |
| Number of Residues | 17 |
| Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIkQGEkGSyFFIInsG |
| Chain | Residue | Details |
| A | VAL78-GLY94 | |
| A | ILE196-GLY212 | |
| A | ILE438-GLY454 | |
| site_id | PS00889 |
| Number of Residues | 18 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEaALihntq......RSAtImA |
| Chain | Residue | Details |
| A | PHE114-ALA131 | |
| A | PHE232-ALA249 | |
| A | PHE474-SER491 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP657 | |
| Chain | Residue | Details |
| A | LYS106 | |
| A | ALA478 | |
| A | ARG485 | |
| A | THR486 | |
| A | GLY115 | |
| A | GLU116 | |
| A | ALA118 | |
| A | ARG125 | |
| A | SER126 | |
| A | ARG466 | |
| A | GLY475 | |
| A | GLU476 | |
| Chain | Residue | Details |
| A | ILE540 | |
| Chain | Residue | Details |
| A | LYS563 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Part of a catalytic triad required for cGMP binding and cGMP-dependent kinase activity => ECO:0000250|UniProtKB:Q8I719 |
| Chain | Residue | Details |
| A | ARG477 | |
| A | GLN525 | |
| A | ASP526 | |
