3Q5I
Crystal Structure of PBANKA_031420
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005516 | molecular_function | calmodulin binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006468 | biological_process | protein phosphorylation |
A | 0009931 | molecular_function | calcium-dependent protein serine/threonine kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0018105 | biological_process | peptidyl-serine phosphorylation |
A | 0020002 | cellular_component | host cell plasma membrane |
A | 0020005 | cellular_component | symbiont-containing vacuole membrane |
A | 0031514 | cellular_component | motile cilium |
A | 0035556 | biological_process | intracellular signal transduction |
A | 0044024 | molecular_function | histone H2AS1 kinase activity |
A | 0045727 | biological_process | positive regulation of translation |
A | 0046777 | biological_process | protein autophosphorylation |
A | 0046872 | molecular_function | metal ion binding |
A | 2000147 | biological_process | positive regulation of cell motility |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1 |
Chain | Residue |
A | ASP384 |
A | ASN386 |
A | ASP388 |
A | GLN390 |
A | GLU395 |
A | HOH530 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 524 |
Chain | Residue |
A | TYR434 |
A | GLU436 |
A | GLU439 |
A | ASP428 |
A | ASP430 |
A | ASN432 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 525 |
Chain | Residue |
A | HOH2 |
A | ASP464 |
A | ASP466 |
A | SER468 |
A | LYS470 |
A | GLU475 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 526 |
Chain | Residue |
A | HOH3 |
A | ASP498 |
A | ASN500 |
A | ASP502 |
A | MET504 |
A | GLU509 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 528 |
Chain | Residue |
A | ASN195 |
A | ASP211 |
A | HOH531 |
A | HOH532 |
A | ANP1634 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ANP A 1634 |
Chain | Residue |
A | VAL71 |
A | ALA84 |
A | LYS86 |
A | ILE128 |
A | THR144 |
A | GLU145 |
A | PHE146 |
A | TYR147 |
A | GLU151 |
A | ASN195 |
A | LEU197 |
A | ASP211 |
A | CA528 |
A | MG529 |
A | HOH532 |
A | HOH591 |
A | HOH622 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 529 |
Chain | Residue |
A | ASP211 |
A | GLU412 |
A | HOH553 |
A | ANP1634 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 527 |
Chain | Residue |
A | HOH12 |
A | GLU31 |
A | TYR34 |
A | PHE35 |
A | GLN36 |
A | HOH610 |
A | HOH660 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKNGDGQLDkkEL |
Chain | Residue | Details |
A | ASP384-LEU396 | |
A | ASP428-PHE440 | |
A | ASP464-LEU476 | |
A | ASP498-PHE510 |
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAYGEVLlCkeknghsekaik......VIKK |
Chain | Residue | Details |
A | LEU63-LYS90 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpeNILL |
Chain | Residue | Details |
A | ILE186-LEU198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP190 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU63 | |
A | LYS86 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10141 |
Chain | Residue | Details |
A | LYS90 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
A | ASP384 | |
A | GLU439 | |
A | ASP464 | |
A | ASP466 | |
A | SER468 | |
A | LYS470 | |
A | GLU475 | |
A | ASP498 | |
A | ASN500 | |
A | ASP502 | |
A | MET504 | |
A | ASN386 | |
A | GLU509 | |
A | ASP388 | |
A | GLN390 | |
A | GLU395 | |
A | ASP428 | |
A | ASP430 | |
A | ASN432 | |
A | TYR434 |
site_id | SWS_FT_FI5 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62344 |
Chain | Residue | Details |
A | SER65 | |
A | SER117 | |
A | SER216 | |
A | SER219 | |
A | SER334 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62344 |
Chain | Residue | Details |
A | THR230 |