IED ID | IndEnz0002004698 |
Enzyme Type ID | protease004698 |
Protein Name |
Probable aspartic-type endopeptidase CTSD EC 3.4.23.- |
Gene Name | CTSD TRV_03534 |
Organism | Trichophyton verrucosum (strain HKI 0517) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton verrucosum (Cattle ringworm fungus) Trichophyton verrucosum (strain HKI 0517) |
Enzyme Sequence | MQFLWLCLLSAVTLQFTGTLAFYPIKLPDFTKGLVSNHGSIDRRFFTFPGLYKHAHTGSTTLNIRRGPSNYRRDNNYPAQIASPPTAPNTLGINNDGYDFSYFSEVKVGSEGQKMWMLIDTGASGTWVFGSDCTSKACGRHNTFGKEDSKTIKVTDEKWGVTYGTGKVSGVIVNDTMSFAGFELVTPFGSASTASDDFLNYPMDGILGIGPQDPNAKTPTVVQLLMQQKLLKSNVIGINLQRASEGATDGQITFGDIDKSKFSGELIYSNVVPDGYQWEIAMDDLIMDGKSLNLKGRTGIIDTGTSFLILPPADADLIHSMIPQANKGSGFYTLPCSTKVDIKLSIGGVEYTIQPDDYVGNETATKGTCNSLIVGRQILGPKQWLVGDVFLKNVYSVFDFDKNRVGLAARKYAGTKNPPSSTPSPGMFLLHAILCPKTISVLMLHIDPTSNKAPSGGSPGLPAESGSDSTTNGEATNGATSSPNSSSSVLTPTWLTLAVFFAIGSSLWS |
Enzyme Length | 509 |
Uniprot Accession Number | D4D8U6 |
Absorption | |
Active Site | ACT_SITE 120; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 302; /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 (3); Lipidation (1); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | Aspartyl protease;Cell membrane;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Signal;Virulence |
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..21; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 54,631 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |