Detail Information for IndEnz0002006003
IED ID IndEnz0002006003
Enzyme Type ID protease006003
Protein Name Vacuolar aspartic protease
EC 3.4.23.-
ACP
Aspartate protease
Gene Name APR1 PRA PRA1
Organism Candida albicans (Yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast)
Enzyme Sequence MQLSLSALTTVALALTSSLVDAKAHSIKLSKLSNEETLDASNFQEYTNSLANKYLNLFNTAHGNPSNFGLQHVLTNQEAEVPFVTPKKGGKYDAPLTNYLNAQYFTEIQIGTPGQPFKVILDTGSSNLWVPSQDCTSLACFLHAKYDHDASSTYKVNGSEFSIQYGSGSMEGYISQDVLTIGDLVIPGQDFAEATSEPGLAFAFGKFDGILGLAYDTISVNHIVPPIYNAINQGLLEKPQFGFYLGSTDKDENDGGLATFGGYDASLFQGKITWLPIRRKAYWEVSFEGIGLGDEYAELHKTGAAIDTGTSLITLPSSLAEIINAKIGATKSWSGQYQVDCAKRDSLPDLTLTFAGYNFTLTPYDYILEVSGSCISVFTPMDFPQPIGDLAIVGDAFLRKYYSIYDLDKNAVGLAPTKV
Enzyme Length 419
Uniprot Accession Number P10977
Absorption
Active Site ACT_SITE 122; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 307; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Motif (1); Sequence conflict (9); Signal peptide (1)
Keywords Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Vacuole
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles. {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 417..419; /note=Microbody targeting signal; /evidence=ECO:0000255
Gene Encoded By
Mass 45,421
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda