Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003774 | molecular_function | cytoskeletal motor activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016459 | cellular_component | myosin complex |
| A | 0051015 | molecular_function | actin filament binding |
| 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 | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| B | 0017022 | molecular_function | myosin binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051401 | molecular_function | CH domain binding |
| B | 0097718 | molecular_function | disordered domain specific binding |
| B | 0097720 | biological_process | calcineurin-mediated signaling |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005513 | biological_process | detection of calcium ion |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005813 | cellular_component | centrosome |
| D | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| D | 0017022 | molecular_function | myosin binding |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0043209 | cellular_component | myelin sheath |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051401 | molecular_function | CH domain binding |
| D | 0097718 | molecular_function | disordered domain specific binding |
| D | 0097720 | biological_process | calcineurin-mediated signaling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1826 |
| Chain | Residue |
| A | GLU152 |
| A | GLY154 |
| A | ALA155 |
| A | GLY156 |
| A | LYS157 |
| A | THR158 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1148 |
| Chain | Residue |
| B | THR26 |
| B | GLU31 |
| B | ASP20 |
| B | ASP22 |
| B | ASP24 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 1149 |
| Chain | Residue |
| B | ASP56 |
| B | ASN60 |
| B | THR62 |
| B | GLU67 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1150 |
| Chain | Residue |
| B | ASP93 |
| B | ASP95 |
| B | ASN97 |
| B | TYR99 |
| B | GLU104 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1151 |
| Chain | Residue |
| B | ASP129 |
| B | ASP131 |
| B | ASP133 |
| B | GLN135 |
| B | GLU140 |
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 | ASP20-LEU32 | |
| B | ASP56-PHE68 | |
| B | ASP93-LEU105 | |
| B | ASP129-PHE141 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 51 |
| Details | Domain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Region: {"description":"Responsible for slow ATPase activity","evidences":[{"source":"PubMed","id":"15944696","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Region: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | Region: {"description":"Required for binding calmodulin","evidences":[{"source":"PubMed","id":"15037754","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9UM54","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12682054","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64331","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 25 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| A | GLY459 | |
| A | GLU461 | |
| A | ASN200 | |
| A | GLY154 | |
