6OQQ
Legionella pneumophila SidJ/Saccharomyces cerevisiae calmodulin complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0018117 | biological_process | protein adenylylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106437 | molecular_function | protein-glutamic acid ligase activity, initiating |
| A | 0106438 | molecular_function | protein-glutamic acid ligase activity, elongating |
| B | 0000131 | cellular_component | incipient cellular bud site |
| B | 0000226 | biological_process | microtubule cytoskeleton organization |
| B | 0000742 | biological_process | karyogamy involved in conjugation with cellular fusion |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005816 | cellular_component | spindle pole body |
| B | 0005823 | cellular_component | central plaque of spindle pole body |
| B | 0005933 | cellular_component | cellular bud |
| B | 0005934 | cellular_component | cellular bud tip |
| B | 0005935 | cellular_component | cellular bud neck |
| B | 0006606 | biological_process | protein import into nucleus |
| B | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| B | 0006897 | biological_process | endocytosis |
| B | 0006898 | biological_process | receptor-mediated endocytosis |
| B | 0007010 | biological_process | cytoskeleton organization |
| B | 0007114 | biological_process | cell budding |
| B | 0010968 | biological_process | regulation of microtubule nucleation |
| B | 0016237 | biological_process | microautophagy |
| B | 0030050 | biological_process | vesicle transport along actin filament |
| B | 0030234 | molecular_function | enzyme regulator activity |
| B | 0030479 | cellular_component | actin cortical patch |
| B | 0042144 | biological_process | vacuole fusion, non-autophagic |
| B | 0043332 | cellular_component | mating projection tip |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048306 | molecular_function | calcium-dependent protein binding |
| B | 0051019 | molecular_function | mitogen-activated protein kinase binding |
| B | 0051286 | cellular_component | cell tip |
| B | 0051300 | biological_process | spindle pole body organization |
| B | 0071474 | biological_process | cellular hyperosmotic response |
| B | 1903525 | biological_process | regulation of membrane tubulation |
| B | 2000601 | biological_process | positive regulation of Arp2/3 complex-mediated actin nucleation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016874 | molecular_function | ligase activity |
| C | 0018117 | biological_process | protein adenylylation |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0106437 | molecular_function | protein-glutamic acid ligase activity, initiating |
| C | 0106438 | molecular_function | protein-glutamic acid ligase activity, elongating |
| D | 0000131 | cellular_component | incipient cellular bud site |
| D | 0000226 | biological_process | microtubule cytoskeleton organization |
| D | 0000742 | biological_process | karyogamy involved in conjugation with cellular fusion |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005816 | cellular_component | spindle pole body |
| D | 0005823 | cellular_component | central plaque of spindle pole body |
| D | 0005933 | cellular_component | cellular bud |
| D | 0005934 | cellular_component | cellular bud tip |
| D | 0005935 | cellular_component | cellular bud neck |
| D | 0006606 | biological_process | protein import into nucleus |
| D | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| D | 0006897 | biological_process | endocytosis |
| D | 0006898 | biological_process | receptor-mediated endocytosis |
| D | 0007010 | biological_process | cytoskeleton organization |
| D | 0007114 | biological_process | cell budding |
| D | 0010968 | biological_process | regulation of microtubule nucleation |
| D | 0016237 | biological_process | microautophagy |
| D | 0030050 | biological_process | vesicle transport along actin filament |
| D | 0030234 | molecular_function | enzyme regulator activity |
| D | 0030479 | cellular_component | actin cortical patch |
| D | 0042144 | biological_process | vacuole fusion, non-autophagic |
| D | 0043332 | cellular_component | mating projection tip |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048306 | molecular_function | calcium-dependent protein binding |
| D | 0051019 | molecular_function | mitogen-activated protein kinase binding |
| D | 0051286 | cellular_component | cell tip |
| D | 0051300 | biological_process | spindle pole body organization |
| D | 0071474 | biological_process | cellular hyperosmotic response |
| D | 1903525 | biological_process | regulation of membrane tubulation |
| D | 2000601 | biological_process | positive regulation of Arp2/3 complex-mediated actin nucleation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue AMP A 901 |
| Chain | Residue |
| A | HIS492 |
| A | ASN733 |
| A | HOH1257 |
| A | ARG500 |
| A | ASP502 |
| A | ARG505 |
| A | TYR506 |
| A | GLN507 |
| A | GLN517 |
| A | GLN519 |
| A | GLY521 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue POP A 902 |
| Chain | Residue |
| A | ARG352 |
| A | LYS367 |
| A | LYS370 |
| A | ASN534 |
| A | ARG536 |
| A | ASP542 |
| A | MG903 |
| A | MG904 |
| A | MG905 |
| A | HOH1033 |
| A | HOH1160 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 903 |
| Chain | Residue |
| A | ASP542 |
| A | ASP545 |
| A | POP902 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 904 |
| Chain | Residue |
| A | TYR449 |
| A | ARG536 |
| A | POP902 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 905 |
| Chain | Residue |
| A | GLN350 |
| A | TYR452 |
| A | ARG536 |
| A | POP902 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue MG A 906 |
| Chain | Residue |
| A | THR493 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 907 |
| Chain | Residue |
| A | ARG522 |
| A | ASN733 |
| A | HOH1043 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 908 |
| Chain | Residue |
| A | LEU478 |
| A | ARG479 |
| A | TYR599 |
| A | HOH1022 |
| A | HOH1037 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 909 |
| Chain | Residue |
| A | PHE563 |
| A | LEU598 |
| A | ASN601 |
| A | THR602 |
| A | GLU605 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 910 |
| Chain | Residue |
| A | LEU694 |
| A | GLN695 |
| A | GLN698 |
| A | GLU707 |
| A | HOH1343 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 911 |
| Chain | Residue |
| A | LYS666 |
| A | GLN667 |
| A | ALA669 |
| A | ASN670 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 912 |
| Chain | Residue |
| A | ARG636 |
| A | ILE671 |
| A | GLU672 |
| A | HOH1142 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 913 |
| Chain | Residue |
| A | GLU637 |
| A | ASN640 |
| A | THR644 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 914 |
| Chain | Residue |
| A | LYS219 |
| A | HIS226 |
| A | HIS280 |
| A | LEU792 |
| A | ASP793 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 915 |
| Chain | Residue |
| A | ARG262 |
| A | PHE292 |
| A | GLU294 |
| C | ARG295 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 916 |
| Chain | Residue |
| A | THR574 |
| A | PHE575 |
| A | HOH1118 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 201 |
| Chain | Residue |
| B | ASP21 |
| B | ASP23 |
| B | ASN25 |
| B | SER27 |
| B | HOH321 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 202 |
| Chain | Residue |
| B | ASP94 |
| B | ASN96 |
| B | ASP98 |
| B | LEU100 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 203 |
| Chain | Residue |
| B | ALA18 |
| B | ASP21 |
| B | ASN24 |
| B | HOH330 |
| site_id | AE2 |
| Number of Residues | 14 |
| Details | binding site for residue AMP C 901 |
| Chain | Residue |
| C | HOH1133 |
| C | HOH1180 |
| C | HIS492 |
| C | ARG500 |
| C | ASP502 |
| C | ARG505 |
| C | TYR506 |
| C | GLN507 |
| C | VAL510 |
| C | GLN517 |
| C | GLN519 |
| C | GLY521 |
| C | POP903 |
| C | MG906 |
| site_id | AE3 |
| Number of Residues | 10 |
| Details | binding site for residue POP C 902 |
| Chain | Residue |
| C | ARG352 |
| C | LYS367 |
| C | ARG536 |
| C | ASP542 |
| C | MG904 |
| C | MG905 |
| C | HOH1003 |
| C | HOH1039 |
| C | HOH1062 |
| C | HOH1075 |
| site_id | AE4 |
| Number of Residues | 8 |
| Details | binding site for residue POP C 903 |
| Chain | Residue |
| C | THR493 |
| C | ARG500 |
| C | TYR732 |
| C | ASN733 |
| C | AMP901 |
| C | MG906 |
| C | HOH1011 |
| C | HOH1160 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 904 |
| Chain | Residue |
| C | ASP542 |
| C | ASP545 |
| C | POP902 |
| C | HOH1186 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue MG C 905 |
| Chain | Residue |
| C | ARG536 |
| C | POP902 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 906 |
| Chain | Residue |
| C | ASN733 |
| C | AMP901 |
| C | POP903 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 907 |
| Chain | Residue |
| C | LYS252 |
| C | THR574 |
| C | PHE575 |
| C | HOH1048 |
| C | HOH1071 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 908 |
| Chain | Residue |
| C | LYS260 |
| C | SER303 |
| C | THR304 |
| C | ASP307 |
| C | GLN511 |
| C | HOH1037 |
| site_id | AF1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 909 |
| Chain | Residue |
| C | GLU284 |
| C | ARG660 |
| C | THR663 |
| C | PRO797 |
| C | GLY798 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 910 |
| Chain | Residue |
| C | LYS260 |
| C | SER585 |
| C | LEU586 |
| C | PHE587 |
| C | HOH1079 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 201 |
| Chain | Residue |
| D | ASP21 |
| D | ASP23 |
| D | ASN25 |
| D | SER27 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 202 |
| Chain | Residue |
| D | ASP94 |
| D | ASN96 |
| D | ASP98 |
| D | LEU100 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDNNGSISssEL |
| Chain | Residue | Details |
| B | ASP21-LEU33 | |
| B | ASP57-PHE69 | |
| B | ASP94-LEU106 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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_FI2 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
