5JM9
Structure of S. cerevesiae mApe1 dodecamer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000324 | cellular_component | fungal-type vacuole |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005773 | cellular_component | vacuole |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0015031 | biological_process | protein transport |
A | 0032258 | biological_process | cytoplasm to vacuole targeting by the Cvt pathway |
A | 0034270 | cellular_component | Cvt complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9ULA0 |
Chain | Residue | Details |
A | HIS88 | |
A | HIS166 | |
A | ASP259 | |
A | GLU295 | |
A | GLU296 | |
A | ASP341 | |
A | HIS344 | |
A | HIS435 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by protease B (PrB/PRB1) => ECO:0000269|PubMed:1400574 |
Chain | Residue | Details |
A | LEU1 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER312 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN63 | |
A | ASN66 | |
A | ASN404 |