Detail Information for IndEnz0002006684
IED ID IndEnz0002006684
Enzyme Type ID protease006684
Protein Name Probable aspartic-type endopeptidase opsB
EC 3.4.23.-
Gene Name opsB AFUA_6G05350
Organism Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Enzyme Sequence MRHIFSLLSIVCLMVKHGACLTLHQRDVPAVVSLDIKRSIVSDPVVRDRVRRKRDKTIGQTLDNAETLYFCNVTLGTPGQALRLVLDTGSSDLWCNAANSTLCSDSNDSCNISGSYDPSSSSTYAYVSSDFNISYADGTGAVGDYATDILHIGGSTLRNLQFGIGYSSTSSEGVLGIGYPSNEVQVGQYGKDTYPNLPRAMVDQGLINSNAYSLWLNDLESNTGSILFGGVNTGKYLGELQTLPIQKVNGRYSEFVIALTGVAFDSESHHKTYSSDALPAAVLLDSGSSLTYLPDSIVENIYRDLNVAYEPSSGVGYLPCKLAGNNINITYTFSSPNITVMIDELLLDAGDLRFRDGARACIFGIVPAGDSTAVLGDTFLRSAYVVYDIANNEISIANTNFNSTEDNILEIGVGPDSVPSATQVSHPVTSVVADGSGARIGAPTGASSTTVPSISSAGALSAGVARADKQYLAIALIAVWFVLGL
Enzyme Length 485
Uniprot Accession Number Q4WDN4
Absorption
Active Site ACT_SITE 87; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 285; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function FUNCTION: Probable GPI-anchored aspartic-type endopeptidase which contributes to virulence. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Domain (1); Glycosylation (8); Lipidation (1); Propeptide (1); Signal peptide (1)
Keywords Aspartyl protease;Cell membrane;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Signal;Virulence;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,337
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda