7PPO
Structure of SidJ/CaM bound to SdeA in pre-glutamylation state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0106274 | molecular_function | NAD+-protein-arginine ADP-ribosyltransferase activity |
| B | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| B | 0000922 | cellular_component | spindle pole |
| B | 0002027 | biological_process | regulation of heart rate |
| B | 0005246 | molecular_function | calcium channel regulator activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005513 | biological_process | detection of calcium ion |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005813 | cellular_component | centrosome |
| B | 0005819 | cellular_component | spindle |
| B | 0005876 | cellular_component | spindle microtubule |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0008076 | cellular_component | voltage-gated potassium channel complex |
| B | 0008179 | molecular_function | adenylate cyclase binding |
| B | 0010856 | molecular_function | adenylate cyclase activator activity |
| B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| B | 0016020 | cellular_component | membrane |
| B | 0019855 | molecular_function | calcium channel inhibitor activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0021762 | biological_process | substantia nigra development |
| B | 0030017 | cellular_component | sarcomere |
| B | 0030672 | cellular_component | synaptic vesicle membrane |
| B | 0031432 | molecular_function | titin binding |
| B | 0031982 | cellular_component | vesicle |
| B | 0032465 | biological_process | regulation of cytokinesis |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034704 | cellular_component | calcium channel complex |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
| B | 0044305 | cellular_component | calyx of Held |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048306 | molecular_function | calcium-dependent protein binding |
| B | 0050848 | biological_process | regulation of calcium-mediated signaling |
| B | 0051592 | biological_process | response to calcium ion |
| B | 0055117 | biological_process | regulation of cardiac muscle contraction |
| B | 0060291 | biological_process | long-term synaptic potentiation |
| B | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
| B | 0072542 | molecular_function | protein phosphatase activator activity |
| B | 0097225 | cellular_component | sperm midpiece |
| B | 0097720 | biological_process | calcineurin-mediated signaling |
| B | 0099523 | cellular_component | presynaptic cytosol |
| B | 0140238 | biological_process | presynaptic endocytosis |
| B | 0141110 | molecular_function | transporter inhibitor activity |
| B | 1901844 | biological_process | regulation of cell communication by electrical coupling involved in cardiac conduction |
| B | 1902494 | cellular_component | catalytic complex |
| B | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
| Chain | Residue | Details |
| B | ASP21-LEU33 | |
| B | ASP57-PHE69 | |
| B | ASP94-LEU106 | |
| B | ASP130-PHE142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Region: {"description":"Ubiquitin transferase","evidences":[{"source":"PubMed","id":"27049943","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P21454","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"27049943","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"5-glutamyl glutamate","evidences":[{"source":"PubMed","id":"31330531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31330532","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31123136","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OQQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP30","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
