Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001750 | cellular_component | photoreceptor outer segment |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004703 | molecular_function | G protein-coupled receptor kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007165 | biological_process | signal transduction |
A | 0007601 | biological_process | visual perception |
A | 0009966 | biological_process | regulation of signal transduction |
A | 0016020 | cellular_component | membrane |
A | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0022400 | biological_process | regulation of opsin-mediated signaling pathway |
A | 0042995 | cellular_component | cell projection |
A | 0046777 | biological_process | protein autophosphorylation |
A | 0050254 | molecular_function | rhodopsin kinase activity |
A | 0097381 | cellular_component | photoreceptor disc membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 563 |
Chain | Residue |
A | ASP332 |
A | HOH582 |
A | HOH583 |
A | HOH761 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 564 |
Chain | Residue |
A | ASP332 |
A | HOH584 |
A | HOH585 |
A | HOH586 |
A | HOH587 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 565 |
Chain | Residue |
A | LEU166 |
A | GLN173 |
A | HOH654 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 566 |
Chain | Residue |
A | GLY387 |
A | PHE389 |
A | ARG390 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ADP A 562 |
Chain | Residue |
A | LEU193 |
A | GLY194 |
A | ARG195 |
A | GLY196 |
A | GLY197 |
A | ALA214 |
A | LYS216 |
A | MET264 |
A | THR265 |
A | MET267 |
A | LEU321 |
A | ASP332 |
A | HOH581 |
A | HOH582 |
A | HOH583 |
A | HOH585 |
A | HOH586 |
A | HOH587 |
A | HOH588 |
A | HOH666 |
A | HOH671 |
A | HOH699 |
A | HOH759 |
A | HOH760 |
A | HOH761 |
A | HOH838 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGEVFaCqmkatgkl..........YACK |
Chain | Residue | Details |
A | LEU193-LYS216 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNVLL |
Chain | Residue | Details |
A | ILE310-LEU322 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 265 |
Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"1527025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP314 | |
A | GLU318 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS316 | |
A | ASP314 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS316 | |
A | THR352 | |
A | ASP314 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS316 | |
A | ASN319 | |
A | ASP314 | |