Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0008447 | molecular_function | L-ascorbate oxidase activity |
A | 0009506 | cellular_component | plasmodesma |
A | 0009615 | biological_process | response to virus |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042542 | biological_process | response to hydrogen peroxide |
A | 0046872 | molecular_function | metal ion binding |
A | 0050687 | biological_process | negative regulation of defense response to virus |
B | 0005507 | molecular_function | copper ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0008447 | molecular_function | L-ascorbate oxidase activity |
B | 0009506 | cellular_component | plasmodesma |
B | 0009615 | biological_process | response to virus |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042542 | biological_process | response to hydrogen peroxide |
B | 0046872 | molecular_function | metal ion binding |
B | 0050687 | biological_process | negative regulation of defense response to virus |
Functional Information from PROSITE/UniProt
site_id | PS00079 |
Number of Residues | 21 |
Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GvWaFhChIEphLhMGMgvvF |
Chain | Residue | Details |
A | GLY501-PHE521 | |
site_id | PS00080 |
Number of Residues | 12 |
Details | MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHiepHlhmGM |
Chain | Residue | Details |
A | HIS506-MET517 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 242 |
Details | Domain: {"description":"Plastocyanin-like 1"} |
site_id | SWS_FT_FI2 |
Number of Residues | 332 |
Details | Domain: {"description":"Plastocyanin-like 2"} |
site_id | SWS_FT_FI3 |
Number of Residues | 358 |
Details | Domain: {"description":"Plastocyanin-like 3"} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | Binding site: {"description":"type 3 copper site","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000149","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a65 |
Chain | Residue | Details |
A | HIS506 | |
A | CYS507 | |
A | HIS508 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a65 |
Chain | Residue | Details |
B | HIS506 | |
B | CYS507 | |
B | HIS508 | |