Detail Information for IndEnz0002012379
IED ID IndEnz0002012379
Enzyme Type ID protease012379
Protein Name Vacuolar membrane protease
EC 3.4.-.-
FXNA-related family protease 1
Gene Name An18g03780
Organism Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Enzyme Sequence MAPLRLSRANPLAFARWPVTLITAVVYLAFLIPLLIVHHVVPSPPTANPNGLDLTQAWADLQVLTDGFHPYNSRRNDEVHTWLLQRIHEILDAAPPADQYLSVDEEKPKPAVFVFDDTQSNLSFVGNSLSSSNTAVYFEGTNILVYIRGSDDDHENWWEEPNGVPSGKGGVLVNAHYDSVSTGYGATDDGVGVVTCLQLIQYFMTPGHAPRRGLVVLLNNGEEDYLNGARVYGQHPISKFPHTFLNLEGAGAGGRAILFRSSDTEVTRPYMSSKYPFGSVLAADGFATGLIGSQTDYVVFEVDLGLRGLDVAFMEPRARYHTEQDDSRHTSKSSLWHMLSAAVATTEGLVSDKSDQFEGAPTDDAKVASGSGSKAVWFDLFGTTFVLFELHTLFALSVTLLVVAPLALLVTGIALTRADKMYLFRTSAKADESLDSVPLQGLRGFFRFPFLFAIPTAVTVGLAYLVTKVNPLIIHSSEYAVWSMMLSAWTFLAWFVSRMADFARPTALHRIYTLTWMFVLAWVLLVISTVYQNQRGLAGSYSVFFFFSGTFLATWISYLELFSLPRKSEYANQNRPTSRRASSYGGSRLGTASGEDHEEDDHDAEEEEEEQEPTESTSLLGGGQRTTFANYVRVAGDHRDSDTDHHYYPGVYKHEQRWSASLPTWTWTLQFLLMAPLVLIMVGPLALLLTSALHQTGQDGSSSLFIYVAIAALTTFLLTPLLPFIHRHTYHLPVFLLLVFLGTLIYNLVAFPFSPTNRLKLFFIQDIDLSTGSTTASLAGVQPYVHAAASTLPSTANQNITCTEHTTRGTKCAWPGLAPRVVPDTPYSDWLDFTISQQHNTTDDKEGDEDTHHPRKARITLSGRNTRACKLLFDSPISSFAVLGSSTDPRFPTSSPHGTKEIRLWSREWENEWVVDVAWTTSTNDDSEEGDEGEGKLNGKAVCLWSDNNSAGVIPALDEVRQFAPSWVAVSKAADGLVEGWKGFSI
Enzyme Length 986
Uniprot Accession Number A2RAN5
Absorption
Active Site ACT_SITE 222; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: May be involved in vacuolar sorting and osmoregulation. {ECO:0000250|UniProtKB:P38244}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (3); Glycosylation (4); Metal binding (6); Region (2); Site (1); Topological domain (10); Transmembrane (9)
Keywords Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Vacuole;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P38244}; Multi-pass membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 108,883
Kinetics
Metal Binding METAL 176; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 188; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 188; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 223; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 248; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 321; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561
Rhea ID
Cross Reference Brenda